MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Isovaleryl-CoA dehydrogenase, mitochondrial; Short=IVD; EC=1.3.8.4; Flags: Precursor; |
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| MyHits synonyms | IVD_HUMAN , P26440 , B2RCV5 , B3KVI7 , J3KR54 , Q53XZ9 , Q96AF6 , 121AF14C7F1FA13D |
 Legends: 1, ACT_SITE Proton acceptor. {ECO:0000269|PubMed:7640268}; 2, BINDING Substrate; via carbonyl oxygen; 3, BINDING FAD. {ECO:0000269|PubMed:9214289}; 4, N6-acetyllysine; alternate. {ECO:0000250|UniProtKB:Q9JHI5}; 5, N6-succinyllysine; alternate. {ECO:0000250|UniProtKB:Q9JHI5}; 6, N6-acetyllysine; alternate. {ECO:0000244|PubMed:19608861}; 7, N6-acetyllysine. {ECO:0000250|UniProtKB:Q9JHI5}; 8, N6-succinyllysine. {ECO:0000250|UniProtKB:Q9JHI5}; 9, VARIANT L -> P (in IVA). {ECO:0000269|PubMed:2063866}; 10, VARIANT R -> P (in IVA). {ECO:0000269|PubMed:9665741}; 11, VARIANT D -> N (in IVA). {ECO:0000269|PubMed:9665741}; 12, VARIANT A -> G (in IVA). {ECO:0000269|PubMed:22004070}; 13, VARIANT G -> R (in IVA; dbSNP:rs142761835). {ECO:0000269|PubMed:22004070, ECO:0000269|PubMed:22350545}; 14, VARIANT I -> M (in IVA). {ECO:0000269|PubMed:23587913}; 15, VARIANT G -> V (in IVA). {ECO:0000269|PubMed:2063866}; 16, VARIANT L -> P (in IVA). {ECO:0000269|PubMed:22004070}; 17, VARIANT A -> V (in IVA; dbSNP:rs28940889). {ECO:0000269|PubMed:9665741}; 18, VARIANT C -> R (in IVA). {ECO:0000269|PubMed:9665741}; 19, VARIANT V -> A (in IVA). {ECO:0000269|PubMed:9665741}; 20, VARIANT R -> C (in IVA). {ECO:0000269|PubMed:9665741}; 21, VARIANT Y -> C (in IVA). {ECO:0000269|PubMed:22004070}; 22, VARIANT R -> L (in IVA). {ECO:0000269|PubMed:9665741}; 23, MUTAGEN E->D: Residual activity. {ECO:0000269|PubMed:7640268}; 24, MUTAGEN E->G,Q: Loss of activity. {ECO:0000269|PubMed:7640268}; 25, CONFLICT W -> C (in Ref. 3; AAP35809 and 7; AAH17202). {ECO:0000305}; 26, TRANSIT Mitochondrion. {ECO:0000244|PubMed:25944712, ECO:0000269|PubMed:12665801, ECO:0000269|PubMed:1310317}; 27, NP_BIND FAD. {ECO:0000269|PubMed:9214289}; 28, REGION Substrate binding; 29, VAR_SEQ Missing (in isoform 2). {ECO:0000303|PubMed:14702039}; 30, ipat:ACYL_COA_DH_2 [T]; 31, ipat:ACYL_COA_DH_1 [T]; 32, HELIX {ECO:0000244|PDB:1IVH}; 33, TURN {ECO:0000244|PDB:1IVH}; 34, STRAND {ECO:0000244|PDB:1IVH}.
| |
ID IVD_HUMAN Reviewed; 423 AA.
AC P26440; B2RCV5; B3KVI7; J3KR54; Q53XZ9; Q96AF6;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 02-NOV-2016, entry version 181.
DE RecName: Full=Isovaleryl-CoA dehydrogenase, mitochondrial;
DE Short=IVD;
DE EC=1.3.8.4;
DE Flags: Precursor;
GN Name=IVD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2318964; DOI=10.1172/JCI114536;
RA Matsubara Y., Ito M., Glassberg R., Satyabhama S., Ikeda Y.,
RA Tanaka K.;
RT "Nucleotide sequence of messenger RNA encoding human isovaleryl-
RT coenzyme A dehydrogenase and its expression in isovaleric acidemia
RT fibroblasts.";
RL J. Clin. Invest. 85:1058-1064(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10677295; DOI=10.1086/302751;
RA Vockley J., Rogan P.K., Anderson B.D., Willard J., Seelan R.S.,
RA Smith D.I., Liu W.;
RT "Exon skipping in IVD RNA processing in isovaleric acidemia caused by
RT point mutations in the coding region of the IVD gene.";
RL Am. J. Hum. Genet. 66:356-367(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Pericardium, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 15.";
RL Nature 440:671-675(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 381-423.
RX PubMed=8468053; DOI=10.1006/geno.1993.1111;
RA Parimoo B., Tanaka K.;
RT "Structural organization of the human isovaleryl-CoA dehydrogenase
RT gene.";
RL Genomics 15:582-590(1993).
RN [9]
RP PROTEIN SEQUENCE OF N-TERMINUS.
RX PubMed=1310317;
RA Vockley J., Nagao M., Parimoo B., Tanaka K.;
RT "The variant human isovaleryl-CoA dehydrogenase gene responsible for
RT type II isovaleric acidemia determines an RNA splicing error, leading
RT to the deletion of the entire second coding exon and the production of
RT a truncated precursor protein that interacts poorly with mitochondrial
RT import receptors.";
RL J. Biol. Chem. 267:2494-2501(1992).
RN [10]
RP PROTEIN SEQUENCE OF 30-47.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [11]
RP ACTIVE SITE, AND MUTAGENESIS OF GLU-283.
RX PubMed=7640268; DOI=10.1021/bi00032a007;
RA Mohsen A.W., Vockley J.;
RT "Identification of the active site catalytic residue in human
RT isovaleryl-CoA dehydrogenase.";
RL Biochemistry 34:10146-10152(1995).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-75, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-29, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 30-423 IN COMPLEX WITH FAD
RP AND SUBSTRATE ANALOG, AND COFACTOR.
RX PubMed=9214289; DOI=10.1021/bi970422u;
RA Tiffany K.A., Roberts D.L., Wang M., Paschke R., Mohsen A.W.,
RA Vockley J., Kim J.-J.P.;
RT "Structure of human isovaleryl-CoA dehydrogenase at 2.6-A resolution:
RT structural basis for substrate specificity.";
RL Biochemistry 36:8455-8464(1997).
RN [17]
RP VARIANTS IVA PRO-42 AND VAL-199.
RX PubMed=2063866;
RA Vockley J., Parimoo B., Tanaka K.;
RT "Molecular characterization of four different classes of mutations in
RT the isovaleryl-CoA dehydrogenase gene responsible for isovaleric
RT acidemia.";
RL Am. J. Hum. Genet. 49:147-157(1991).
RN [18]
RP VARIANTS IVA PRO-50; ASN-69; VAL-311; ARG-357; ALA-371; CYS-392 AND
RP LEU-411.
RX PubMed=9665741; DOI=10.1021/bi973096r;
RA Mohsen A.-W.A., Anderson B.D., Volchenboum S.L., Battaile K.P.,
RA Tiffany K.A., Roberts D.L., Kim J.-J.P., Vockley J.;
RT "Characterization of molecular defects in isovaleryl-CoA dehydrogenase
RT in patients with isovaleric acidemia.";
RL Biochemistry 37:10325-10335(1998).
RN [19]
RP VARIANTS IVA GLY-94; ARG-120; PRO-276 AND CYS-400.
RX PubMed=22004070; DOI=10.1111/j.1442-200X.2011.03488.x;
RA Vatanavicharn N., Liammongkolkul S., Sakamoto O.,
RA Sathienkijkanchai A., Wasant P.;
RT "Phenotypic and mutation spectrums of Thai patients with isovaleric
RT acidemia.";
RL Pediatr. Int. 53:990-994(2011).
RN [20]
RP VARIANT IVA ARG-120.
RX PubMed=22350545; DOI=10.1007/s10545-012-9457-2;
RA Dercksen M., Duran M., Ijlst L., Mienie L.J., Reinecke C.J.,
RA Ruiter J.P., Waterham H.R., Wanders R.J.;
RT "Clinical variability of isovaleric acidemia in a genetically
RT homogeneous population.";
RL J. Inherit. Metab. Dis. 35:1021-1029(2012).
RN [21]
RP VARIANT IVA MET-196.
RX PubMed=23587913; DOI=10.1016/j.gene.2013.03.139;
RA Bei F., Sun J.H., Yu Y.G., Jia J., Zheng Z.J., Fu Q.H., Cai W.;
RT "Two novel isovaleryl-CoA dehydrogenase gene mutations in a Chinese
RT infant.";
RL Gene 524:396-400(2013).
CC -!- CATALYTIC ACTIVITY: Isovaleryl-CoA + electron-transfer
CC flavoprotein = 3-methylcrotonyl-CoA + reduced electron-transfer
CC flavoprotein.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:9214289};
CC -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-
CC hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 1/3.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9214289}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P26440-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P26440-2; Sequence=VSP_045193;
CC Note=No experimental confirmation available.;
CC -!- DISEASE: Isovaleric acidemia (IVA) [MIM:243500]: A metabolic
CC disorder characterized by retarded psychomotor development, a
CC peculiar odor resembling sweaty feet, an aversion to dietary
CC protein, and pernicious vomiting, leading to acidosis and coma.
CC The acute neonatal form leads to massive metabolic acidosis from
CC the first days of life and rapid death.
CC {ECO:0000269|PubMed:2063866, ECO:0000269|PubMed:22004070,
CC ECO:0000269|PubMed:22350545, ECO:0000269|PubMed:23587913,
CC ECO:0000269|PubMed:9665741}. Note=The disease is caused by
CC mutations affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG53799.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC Sequence=EAW92413.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAW92414.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAW92415.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR EMBL; M34192; AAA52711.1; -; mRNA.
DR EMBL; AF191218; AAF20182.1; -; Genomic_DNA.
DR EMBL; AF191214; AAF20182.1; JOINED; Genomic_DNA.
DR EMBL; AF191215; AAF20182.1; JOINED; Genomic_DNA.
DR EMBL; AF191216; AAF20182.1; JOINED; Genomic_DNA.
DR EMBL; AF191217; AAF20182.1; JOINED; Genomic_DNA.
DR EMBL; BT007145; AAP35809.1; -; mRNA.
DR EMBL; AK122922; BAG53799.1; ALT_INIT; mRNA.
DR EMBL; AK315296; BAG37702.1; -; mRNA.
DR EMBL; AC013356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471125; EAW92413.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471125; EAW92414.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471125; EAW92415.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC017202; AAH17202.1; -; mRNA.
DR EMBL; AF038318; AAB92584.1; -; Genomic_DNA.
DR PIR; A37033; A37033.
DR RefSeq; NP_001152980.1; NM_001159508.1.
DR RefSeq; NP_002216.2; NM_002225.3.
DR UniGene; Hs.513646; -.
DR PDB; 1IVH; X-ray; 2.60 A; A/B/C/D=30-423.
DR PDBsum; 1IVH; -.
DR ProteinModelPortal; P26440; -.
DR SMR; P26440; -.
DR BioGrid; 109916; 10.
DR IntAct; P26440; 2.
DR STRING; 9606.ENSP00000418397; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR SwissLipids; SLP:000000936; -.
DR iPTMnet; P26440; -.
DR PhosphoSitePlus; P26440; -.
DR SwissPalm; P26440; -.
DR BioMuta; IVD; -.
DR DMDM; 125051; -.
DR REPRODUCTION-2DPAGE; IPI00645805; -.
DR UCD-2DPAGE; P26440; -.
DR EPD; P26440; -.
DR MaxQB; P26440; -.
DR PaxDb; P26440; -.
DR PeptideAtlas; P26440; -.
DR PRIDE; P26440; -.
DR DNASU; 3712; -.
DR Ensembl; ENST00000479013; ENSP00000417990; ENSG00000128928.
DR GeneID; 3712; -.
DR KEGG; hsa:3712; -.
DR UCSC; uc001zlq.3; human. [P26440-1]
DR CTD; 3712; -.
DR DisGeNET; 3712; -.
DR GeneCards; IVD; -.
DR HGNC; HGNC:6186; IVD.
DR HPA; HPA041391; -.
DR HPA; HPA044250; -.
DR MalaCards; IVD; -.
DR MIM; 243500; phenotype.
DR MIM; 607036; gene.
DR neXtProt; NX_P26440; -.
DR Orphanet; 33; Isovaleric acidemia.
DR PharmGKB; PA29984; -.
DR eggNOG; KOG0141; Eukaryota.
DR eggNOG; ENOG410XNMY; LUCA.
DR HOGENOM; HOG000131659; -.
DR HOVERGEN; HBG000224; -.
DR InParanoid; P26440; -.
DR KO; K00253; -.
DR PhylomeDB; P26440; -.
DR TreeFam; TF105050; -.
DR BioCyc; ZFISH:HS05233-MONOMER; -.
DR BRENDA; 1.3.8.4; 2681.
DR Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
DR SABIO-RK; P26440; -.
DR UniPathway; UPA00363; UER00860.
DR ChiTaRS; IVD; human.
DR EvolutionaryTrace; P26440; -.
DR GenomeRNAi; 3712; -.
DR PRO; PR:P26440; -.
DR Proteomes; UP000005640; Chromosome 15.
DR Bgee; ENSG00000128928; -.
DR CleanEx; HS_IVD; -.
DR ExpressionAtlas; P26440; baseline and differential.
DR Genevisible; P26440; HS.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0009055; F:electron carrier activity; IBA:GO_Central.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0008470; F:isovaleryl-CoA dehydrogenase activity; ISS:BHF-UCL.
DR GO; GO:0052890; F:oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor; IBA:GO_Central.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR GO; GO:0006552; P:leucine catabolic process; ISS:BHF-UCL.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR Gene3D; 1.10.540.10; -; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Disease mutation; FAD; Flavoprotein;
KW Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1 29 Mitochondrion.
FT {ECO:0000244|PubMed:25944712,
FT ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:1310317}.
FT CHAIN 30 423 Isovaleryl-CoA dehydrogenase,
FT mitochondrial.
FT /FTId=PRO_0000000531.
FT NP_BIND 162 171 FAD. {ECO:0000269|PubMed:9214289}.
FT NP_BIND 195 197 FAD. {ECO:0000269|PubMed:9214289}.
FT NP_BIND 377 381 FAD. {ECO:0000269|PubMed:9214289}.
FT NP_BIND 406 408 FAD. {ECO:0000269|PubMed:9214289}.
FT REGION 219 220 Substrate binding.
FT REGION 281 284 Substrate binding.
FT REGION 404 405 Substrate binding.
FT ACT_SITE 283 283 Proton acceptor.
FT {ECO:0000269|PubMed:7640268}.
FT BINDING 171 171 Substrate; via carbonyl oxygen.
FT BINDING 274 274 Substrate.
FT BINDING 309 309 FAD. {ECO:0000269|PubMed:9214289}.
FT BINDING 320 320 FAD. {ECO:0000269|PubMed:9214289}.
FT MOD_RES 55 55 N6-acetyllysine; alternate.
FT {ECO:0000250|UniProtKB:Q9JHI5}.
FT MOD_RES 55 55 N6-succinyllysine; alternate.
FT {ECO:0000250|UniProtKB:Q9JHI5}.
FT MOD_RES 64 64 N6-acetyllysine; alternate.
FT {ECO:0000250|UniProtKB:Q9JHI5}.
FT MOD_RES 64 64 N6-succinyllysine; alternate.
FT {ECO:0000250|UniProtKB:Q9JHI5}.
FT MOD_RES 75 75 N6-acetyllysine; alternate.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 75 75 N6-succinyllysine; alternate.
FT {ECO:0000250|UniProtKB:Q9JHI5}.
FT MOD_RES 238 238 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:Q9JHI5}.
FT MOD_RES 259 259 N6-acetyllysine; alternate.
FT {ECO:0000250|UniProtKB:Q9JHI5}.
FT MOD_RES 259 259 N6-succinyllysine; alternate.
FT {ECO:0000250|UniProtKB:Q9JHI5}.
FT MOD_RES 315 315 N6-succinyllysine.
FT {ECO:0000250|UniProtKB:Q9JHI5}.
FT VAR_SEQ 49 78 Missing (in isoform 2).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_045193.
FT VARIANT 42 42 L -> P (in IVA).
FT {ECO:0000269|PubMed:2063866}.
FT /FTId=VAR_000423.
FT VARIANT 50 50 R -> P (in IVA).
FT {ECO:0000269|PubMed:9665741}.
FT /FTId=VAR_015960.
FT VARIANT 69 69 D -> N (in IVA).
FT {ECO:0000269|PubMed:9665741}.
FT /FTId=VAR_015961.
FT VARIANT 94 94 A -> G (in IVA).
FT {ECO:0000269|PubMed:22004070}.
FT /FTId=VAR_070061.
FT VARIANT 120 120 G -> R (in IVA; dbSNP:rs142761835).
FT {ECO:0000269|PubMed:22004070,
FT ECO:0000269|PubMed:22350545}.
FT /FTId=VAR_070062.
FT VARIANT 196 196 I -> M (in IVA).
FT {ECO:0000269|PubMed:23587913}.
FT /FTId=VAR_070063.
FT VARIANT 199 199 G -> V (in IVA).
FT {ECO:0000269|PubMed:2063866}.
FT /FTId=VAR_000424.
FT VARIANT 276 276 L -> P (in IVA).
FT {ECO:0000269|PubMed:22004070}.
FT /FTId=VAR_070064.
FT VARIANT 311 311 A -> V (in IVA; dbSNP:rs28940889).
FT {ECO:0000269|PubMed:9665741}.
FT /FTId=VAR_015962.
FT VARIANT 357 357 C -> R (in IVA).
FT {ECO:0000269|PubMed:9665741}.
FT /FTId=VAR_015963.
FT VARIANT 371 371 V -> A (in IVA).
FT {ECO:0000269|PubMed:9665741}.
FT /FTId=VAR_015964.
FT VARIANT 392 392 R -> C (in IVA).
FT {ECO:0000269|PubMed:9665741}.
FT /FTId=VAR_015965.
FT VARIANT 400 400 Y -> C (in IVA).
FT {ECO:0000269|PubMed:22004070}.
FT /FTId=VAR_070065.
FT VARIANT 411 411 R -> L (in IVA).
FT {ECO:0000269|PubMed:9665741}.
FT /FTId=VAR_015966.
FT MUTAGEN 283 283 E->D: Residual activity.
FT {ECO:0000269|PubMed:7640268}.
FT MUTAGEN 283 283 E->G,Q: Loss of activity.
FT {ECO:0000269|PubMed:7640268}.
FT CONFLICT 10 10 W -> C (in Ref. 3; AAP35809 and 7;
FT AAH17202). {ECO:0000305}.
FT HELIX 38 40 {ECO:0000244|PDB:1IVH}.
FT HELIX 44 60 {ECO:0000244|PDB:1IVH}.
FT TURN 61 64 {ECO:0000244|PDB:1IVH}.
FT HELIX 65 71 {ECO:0000244|PDB:1IVH}.
FT HELIX 77 87 {ECO:0000244|PDB:1IVH}.
FT TURN 90 93 {ECO:0000244|PDB:1IVH}.
FT HELIX 96 98 {ECO:0000244|PDB:1IVH}.
FT HELIX 105 118 {ECO:0000244|PDB:1IVH}.
FT HELIX 120 130 {ECO:0000244|PDB:1IVH}.
FT TURN 131 133 {ECO:0000244|PDB:1IVH}.
FT HELIX 134 140 {ECO:0000244|PDB:1IVH}.
FT HELIX 143 154 {ECO:0000244|PDB:1IVH}.
FT STRAND 160 163 {ECO:0000244|PDB:1IVH}.
FT STRAND 169 172 {ECO:0000244|PDB:1IVH}.
FT HELIX 173 175 {ECO:0000244|PDB:1IVH}.
FT STRAND 179 182 {ECO:0000244|PDB:1IVH}.
FT STRAND 184 197 {ECO:0000244|PDB:1IVH}.
FT HELIX 199 201 {ECO:0000244|PDB:1IVH}.
FT STRAND 203 211 {ECO:0000244|PDB:1IVH}.
FT HELIX 218 221 {ECO:0000244|PDB:1IVH}.
FT STRAND 222 228 {ECO:0000244|PDB:1IVH}.
FT STRAND 234 236 {ECO:0000244|PDB:1IVH}.
FT STRAND 242 244 {ECO:0000244|PDB:1IVH}.
FT STRAND 250 261 {ECO:0000244|PDB:1IVH}.
FT HELIX 262 264 {ECO:0000244|PDB:1IVH}.
FT STRAND 265 267 {ECO:0000244|PDB:1IVH}.
FT HELIX 272 287 {ECO:0000244|PDB:1IVH}.
FT HELIX 289 306 {ECO:0000244|PDB:1IVH}.
FT HELIX 316 318 {ECO:0000244|PDB:1IVH}.
FT HELIX 320 348 {ECO:0000244|PDB:1IVH}.
FT HELIX 354 379 {ECO:0000244|PDB:1IVH}.
FT HELIX 380 384 {ECO:0000244|PDB:1IVH}.
FT HELIX 390 399 {ECO:0000244|PDB:1IVH}.
FT TURN 400 404 {ECO:0000244|PDB:1IVH}.
FT HELIX 407 419 {ECO:0000244|PDB:1IVH}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 161 258 ipfam:Acyl-CoA_dh_M [T]
FT MYHIT 377 396 ipat:ACYL_COA_DH_2 [T]
FT MYHIT 163 175 ipat:ACYL_COA_DH_1 [T]
FT MYHIT 270 417 ipfam:Acyl-CoA_dh_1 [T]
FT MYHIT 43 157 ipfam:Acyl-CoA_dh_N [T]
SQ SEQUENCE 423 AA; 46319 MW; 121AF14C7F1FA13D CRC64;
MATATRLLGW RVASWRLRPP LAGFVSQRAH SLLPVDDAIN GLSEEQRQLR QTMAKFLQEH
LAPKAQEIDR SNEFKNLREF WKQLGNLGVL GITAPVQYGG SGLGYLEHVL VMEEISRASG
AVGLSYGAHS NLCINQLVRN GNEAQKEKYL PKLISGEYIG ALAMSEPNAG SDVVSMKLKA
EKKGNHYILN GNKFWITNGP DADVLIVYAK TDLAAVPASR GITAFIVEKG MPGFSTSKKL
DKLGMRGSNT CELIFEDCKI PAANILGHEN KGVYVLMSGL DLERLVLAGG PLGLMQAVLD
HTIPYLHVRE AFGQKIGHFQ LMQGKMADMY TRLMACRQYV YNVAKACDEG HCTAKDCAGV
ILYSAECATQ VALDGIQCFG GNGYINDFPM GRFLRDAKLY EIGAGTSEVR RLVIGRAFNA
DFH
//
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