ID SAHH_CAEEL Reviewed; 437 AA.
AC P27604;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 30-NOV-2016, entry version 143.
DE RecName: Full=Adenosylhomocysteinase;
DE Short=AdoHcyase;
DE EC=3.3.1.1;
DE AltName: Full=Protein dumpy-14;
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase;
GN Name=ahcy-1; Synonyms=ahh, dpy-14; ORFNames=K02F2.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8458573;
RA Prasad S.S., Starr T., Rose A.M.;
RT "Molecular characterization in the dpy-14 region identifies the
RT adenosylhomocysteine hydrolase gene in Caenorhabditis elegans.";
RL Genome 36:57-65(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for
RT investigating biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Adenosylhomocysteine is a competitive inhibitor of S-
CC adenosyl-L-methionine-dependent methyl transferase reactions;
CC therefore adenosylhomocysteinase may play a key role in the
CC control of methylations via regulation of the intracellular
CC concentration of adenosylhomocysteine.
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = L-
CC homocysteine + adenosine.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Note=Binds 1 NAD(+) per subunit.;
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000305}.
DR EMBL; M64306; AAA28062.1; -; Genomic_DNA.
DR EMBL; S57284; AAB25906.1; -; Genomic_DNA.
DR EMBL; FO081029; CCD68626.1; -; Genomic_DNA.
DR PIR; T32918; T32918.
DR RefSeq; NP_491955.1; NM_059554.6.
DR UniGene; Cel.7612; -.
DR ProteinModelPortal; P27604; -.
DR SMR; P27604; -.
DR BioGrid; 37854; 6.
DR DIP; DIP-25388N; -.
DR IntAct; P27604; 1.
DR MINT; MINT-1076618; -.
DR STRING; 6239.K02F2.2.2; -.
DR iPTMnet; P27604; -.
DR World-2DPAGE; 0011:P27604; -.
DR World-2DPAGE; 0020:P27604; -.
DR EPD; P27604; -.
DR PaxDb; P27604; -.
DR PeptideAtlas; P27604; -.
DR PRIDE; P27604; -.
DR EnsemblMetazoa; K02F2.2.1; K02F2.2.1; WBGene00019322.
DR EnsemblMetazoa; K02F2.2.2; K02F2.2.2; WBGene00019322.
DR GeneID; 172408; -.
DR KEGG; cel:CELE_K02F2.2; -.
DR UCSC; K02F2.2.1; c. elegans.
DR CTD; 172408; -.
DR WormBase; K02F2.2; CE17154; WBGene00019322; ahcy-1.
DR eggNOG; KOG1370; Eukaryota.
DR eggNOG; COG0499; LUCA.
DR GeneTree; ENSGT00390000003626; -.
DR HOGENOM; HOG000227987; -.
DR InParanoid; P27604; -.
DR KO; K01251; -.
DR OMA; IELWTKF; -.
DR OrthoDB; EOG091G06EB; -.
DR PhylomeDB; P27604; -.
DR Reactome; R-CEL-156581; Methylation.
DR Reactome; R-CEL-1614635; Sulfur amino acid metabolism.
DR UniPathway; UPA00314; UER00076.
DR PRO; PR:P27604; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00019322; -.
DR GO; GO:0005829; C:cytosol; ISS:WormBase.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; ISS:WormBase.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019510; P:S-adenosylhomocysteine catabolic process; ISS:WormBase.
DR GO; GO:0033353; P:S-adenosylmethionine cycle; IBA:GO_Central.
DR CDD; cd00401; SAHH; 1.
DR Gene3D; 3.40.50.720; -; 1.
DR HAMAP; MF_00563; AdoHcyase; 1.
DR InterPro; IPR000043; Adenosylhomocysteinase.
DR InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR PANTHER; PTHR23420; PTHR23420; 1.
DR Pfam; PF05221; AdoHcyase; 1.
DR Pfam; PF00670; AdoHcyase_NAD; 1.
DR PIRSF; PIRSF001109; Ad_hcy_hydrolase; 1.
DR SMART; SM00996; AdoHcyase; 1.
DR SMART; SM00997; AdoHcyase_NAD; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00936; ahcY; 1.
DR PROSITE; PS00738; ADOHCYASE_1; 1.
DR PROSITE; PS00739; ADOHCYASE_2; 1.
PE 3: Inferred from homology;
KW Complete proteome; Hydrolase; NAD; One-carbon metabolism;
KW Reference proteome.
FT CHAIN 1 437 Adenosylhomocysteinase.
FT /FTId=PRO_0000116910.
FT NP_BIND 159 161 NAD. {ECO:0000250}.
FT NP_BIND 224 229 NAD. {ECO:0000250}.
FT NP_BIND 301 303 NAD. {ECO:0000250}.
FT BINDING 58 58 Substrate. {ECO:0000250}.
FT BINDING 133 133 Substrate. {ECO:0000250}.
FT BINDING 158 158 Substrate. {ECO:0000250}.
FT BINDING 188 188 Substrate. {ECO:0000250}.
FT BINDING 192 192 Substrate. {ECO:0000250}.
FT BINDING 193 193 NAD. {ECO:0000250}.
FT BINDING 245 245 NAD. {ECO:0000250}.
FT BINDING 348 348 NAD. {ECO:0000250}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 7 436 ismart:AdoHcyase [T]
FT MYHIT 193 354 ismart:AdoHcyase_NAD [T]
FT MYHIT 193 354 ipfam:AdoHcyase_NAD [T]
FT MYHIT 3 429 ihamap:AdoHcyase [T]
FT MYHIT 215 232 ipat:ADOHCYASE_2 [T]
FT MYHIT 8 143 ipfam:AdoHcyase [T]
FT MYHIT 79 93 ipat:ADOHCYASE_1 [T]
SQ SEQUENCE 437 AA; 47536 MW; 53ADAB24507CFCD6 CRC64;
MAQSKPAYKV ADIKLADFGR KEIILAENEM PGLMAMRSKY GPSQPLKGAR IAGCLHMTIQ
TAVLIETLTA LGAEVQWSSC NIFSTQDHAA AAIAQTGVPV YAWKGETDEE YEWCIEQTIV
FKDGQPLNMI LDDGGDLTNL VHAKYPQYLA GIRGLSEETT TGVHNLAKML AKGDLKVPAI
NVNDSVTKSK FDNLYGIRES LPDGIKRATD VMLAGKVAVV AGYGDVGKGS AASLKAFGSR
VIVTEIDPIN ALQAAMEGYE VTTLEEAAPK ANIIVTTTGC KDIVTGKHFE LLPNDAIVCN
VGHFDCEIDV KWLNTNATKK DTIKPQVDRY TLKNGRHVIL LAEGRLVNLG CATGHPSFVM
SNSFTNQVLA QVELWTKFGT PQEYKLGLYV LPKTLDEEVA YLHLAQLGVK LTKLSDEQAS
YLGVPVAGPY KPDHYRY
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