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=3-isopropylmalate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01033}; EC=1.1.1.85 {ECO:0000255|HAMAP-Rule:MF_01033}; AltName: Full=3-IPM-DH {ECO:0000255|HAMAP-Rule:MF_01033}; AltName: Full=Beta-IPM dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01033}; Short=IMDH {ECO:0000255|HAMAP-Rule:MF_01033}; |
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MyHits synonyms | LEU3_RHORT , Q2RV53 , EB6B4847C8DF8B6B |
![]() Legends: 1, Magnesium or manganese. {ECO:0000255|HAMAP-Rule:MF_01033}; 2, BINDING Substrate. {ECO:0000255|HAMAP- Rule:MF_01033}; 3, SITE Important for catalysis. {ECO:0000255|HAMAP-Rule:MF_01033}; 4, NP_BIND NAD. {ECO:0000255|HAMAP-Rule:MF_01033}; 5, ipat:IDH_IMDH [T].
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ID LEU3_RHORT Reviewed; 370 AA. AC Q2RV53; DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 02-NOV-2016, entry version 79. DE RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01033}; DE EC=1.1.1.85 {ECO:0000255|HAMAP-Rule:MF_01033}; DE AltName: Full=3-IPM-DH {ECO:0000255|HAMAP-Rule:MF_01033}; DE AltName: Full=Beta-IPM dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01033}; DE Short=IMDH {ECO:0000255|HAMAP-Rule:MF_01033}; GN Name=leuB {ECO:0000255|HAMAP-Rule:MF_01033}; GN OrderedLocusNames=Rru_A1191; OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG OS 4362 / NCIB 8255 / S1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=269796; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., RA Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., RA Reslewic S., Zhou S., Schwartz D.C.; RT "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC RT 11170."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- CC methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- CC oxopentanoate. The product decarboxylates to 4-methyl-2 CC oxopentanoate. {ECO:0000255|HAMAP-Rule:MF_01033}. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl- CC 2-oxopentanoate + CO(2) + NADH. {ECO:0000255|HAMAP-Rule:MF_01033}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01033}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01033}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01033}; CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 3/4. CC {ECO:0000255|HAMAP-Rule:MF_01033}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01033}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01033}. CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. LeuB type 1 subfamily. {ECO:0000255|HAMAP- CC Rule:MF_01033}. DR EMBL; CP000230; ABC21992.1; -; Genomic_DNA. DR RefSeq; WP_011388946.1; NC_007643.1. DR RefSeq; YP_426279.1; NC_007643.1. DR ProteinModelPortal; Q2RV53; -. DR STRING; 269796.Rru_A1191; -. DR PRIDE; Q2RV53; -. DR EnsemblBacteria; ABC21992; ABC21992; Rru_A1191. DR GeneID; 3834701; -. DR KEGG; rru:Rru_A1191; -. DR PATRIC; 23325994; VBIRhoRub82919_1255. DR eggNOG; ENOG4105C0C; Bacteria. DR eggNOG; COG0473; LUCA. DR HOGENOM; HOG000021112; -. DR KO; K00052; -. DR OMA; RRPKQFD; -. DR OrthoDB; POG091H01YH; -. DR UniPathway; UPA00048; UER00072. DR Proteomes; UP000001929; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.718.10; -; 1. DR HAMAP; MF_01033; LeuB_type1; 1. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR001804; Isocitrate/isopropylmalate_DH. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR InterPro; IPR004429; Isopropylmalate_DH. DR PANTHER; PTHR11835; PTHR11835; 1. DR Pfam; PF00180; Iso_dh; 1. DR SMART; SM01329; Iso_dh; 1. DR TIGRFAMs; TIGR00169; leuB; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium; KW Manganese; Metal-binding; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 370 3-isopropylmalate dehydrogenase. FT /FTId=PRO_0000250135. FT NP_BIND 290 302 NAD. {ECO:0000255|HAMAP-Rule:MF_01033}. FT METAL 227 227 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_01033}. FT METAL 251 251 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_01033}. FT METAL 255 255 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_01033}. FT BINDING 99 99 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01033}. FT BINDING 109 109 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01033}. FT BINDING 137 137 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01033}. FT BINDING 227 227 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01033}. FT SITE 144 144 Important for catalysis. FT {ECO:0000255|HAMAP-Rule:MF_01033}. FT SITE 195 195 Important for catalysis. FT {ECO:0000255|HAMAP-Rule:MF_01033}. CC -------------------------------------------------------------------------- CC The following FT lines are automated annotations from the MyHits database. CC -------------------------------------------------------------------------- FT MYHIT 6 360 ipfam:Iso_dh [T] FT MYHIT 5 365 ihamap:LeuB_type1 [T] FT MYHIT 6 361 ismart:Iso_dh [T] FT MYHIT 247 266 ipat:IDH_IMDH [T] SQ SEQUENCE 370 AA; 39536 MW; EB6B4847C8DF8B6B CRC64; MPVSKKILFL AGDGIGPEVM AQVRRVMDWL NQTGRTAFEV EDALVGGAAY DAQGTPLHDD TVALALAADA VLLGAVGGPK WDASLPFELK PERGLLRLRK DLELFANLRP AMVFDALAEA STLKTELVSG LDVMIVRELT GGVYFGQPRG ISALPNGERR GVNTQVYDTH EIVRVAKVAF DLAGKRGKRL CSVEKANVME SGLLWREEVT KLGADYPEIA LSHMYADNCA MQLVRQPKQF DVIVTDNLFG DILSDCAAML TGSLGMLPSA SLGAADAAGN RRAMYEPVHG SAPDIAGQDK ANPLATILSF SMMLRYSFDL AEEADLVDNA VRGVLAKGLR TGDIFQPGKT LVGTTGMGDA LLAEMAQLAN // |