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Database: UniProt
Entry: I7CT75_NATSJ
LinkDB: I7CT75_NATSJ
Original site: I7CT75_NATSJ 
ID   I7CT75_NATSJ            Unreviewed;       429 AA.
AC   I7CT75;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Adenosylhomocysteinase {ECO:0000256|HAMAP-Rule:MF_00563};
DE            EC=3.13.2.1 {ECO:0000256|HAMAP-Rule:MF_00563};
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000256|HAMAP-Rule:MF_00563};
DE            Short=AdoHcyase {ECO:0000256|HAMAP-Rule:MF_00563};
GN   Name=ahcY {ECO:0000256|HAMAP-Rule:MF_00563};
GN   OrderedLocusNames=NJ7G_0602 {ECO:0000313|EMBL:AFO55856.1};
OS   Natrinema sp. (strain J7-2).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=406552 {ECO:0000313|EMBL:AFO55856.1, ECO:0000313|Proteomes:UP000006507};
RN   [1] {ECO:0000313|EMBL:AFO55856.1, ECO:0000313|Proteomes:UP000006507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J7-2 {ECO:0000313|EMBL:AFO55856.1,
RC   ECO:0000313|Proteomes:UP000006507};
RX   PubMed=22911826; DOI=10.1371/journal.pone.0041621;
RA   Feng J., Liu B., Zhang Z., Ren Y., Li Y., Gan F., Huang Y., Chen X.,
RA   Shen P., Wang L., Tang B., Tang X.F.;
RT   "The complete genome sequence of Natrinema sp. J7-2, a haloarchaeon capable
RT   of growth on synthetic media without amino acid supplements.";
RL   PLoS ONE 7:E41621-E41621(2012).
CC   -!- FUNCTION: May play a key role in the regulation of the intracellular
CC       concentration of adenosylhomocysteine. {ECO:0000256|HAMAP-
CC       Rule:MF_00563}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine;
CC         Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.13.2.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00563};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00563,
CC         ECO:0000256|PIRSR:PIRSR001109-2};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|HAMAP-Rule:MF_00563,
CC       ECO:0000256|PIRSR:PIRSR001109-2};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC       homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00563}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00563}.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000256|ARBA:ARBA00007122, ECO:0000256|HAMAP-Rule:MF_00563,
CC       ECO:0000256|RuleBase:RU004166}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00563}.
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DR   EMBL; CP003412; AFO55856.1; -; Genomic_DNA.
DR   RefSeq; WP_014862997.1; NC_018224.1.
DR   AlphaFoldDB; I7CT75; -.
DR   STRING; 406552.NJ7G_0602; -.
DR   GeneID; 13350444; -.
DR   KEGG; nat:NJ7G_0602; -.
DR   PATRIC; fig|406552.5.peg.531; -.
DR   eggNOG; arCOG04137; Archaea.
DR   HOGENOM; CLU_025194_2_1_2; -.
DR   OMA; YIGVTVE; -.
DR   OrthoDB; 8479at2157; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000006507; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00401; SAHH; 1.
DR   Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00563; AdoHcyase; 1.
DR   InterPro; IPR042172; Adenosylhomocyst_ase-like_sf.
DR   InterPro; IPR000043; Adenosylhomocysteinase-like.
DR   InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR   NCBIfam; TIGR00936; ahcY; 1.
DR   PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR   PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 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; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00738; ADOHCYASE_1; 1.
DR   PROSITE; PS00739; ADOHCYASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00563};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00563};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00563};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_00563}.
FT   DOMAIN          194..355
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         160..162
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         194
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         223..228
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         225..230
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         246
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         281
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         302..304
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         349
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         358
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ   SEQUENCE   429 AA;  46918 MW;  DD368890B7AF573B CRC64;
     MTETEYPPIS EQLDDLESAR EEGRRKMDWA AQHMPILERV REEFVANRPF EGERIGMAMH
     VEAKTAMLVE TLAEGGAEVA VTGCNPLSTH DDVSAALDTH ENITSYAKRG VDDDEYYAAI
     EAVIAHEPTI TVDDGMDLVA AIHEDYPELI DGIIGGAEET TTGVHRLRAM DDDGALEYPV
     FAVNDTPMKR LFDNVHGTGE SSLASIAMTT NLSWAGKNVV VSGYGYCGKG VAKKAAGQNA
     NVIVTEVEPR RALEAHMEGY EVMPMAEAAA VGDVFLTTTG NRDVIVEEHF EKMQDGVLLA
     NAGHFDIEID LEALDDLAVD RYEARDGVEA YELDDGRTLN VIAEGRLVNL AAPVSLGHPV
     EVMDQSFGIQ AVCVREMLEN GDEYDAGVYD VPDELDKEIA EIKLEAEGVD FDSLTETQRE
     YMDAWDHGT
//
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