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Database: UniProt
Entry: W1N6J9_9GAMM
LinkDB: W1N6J9_9GAMM
Original site: W1N6J9_9GAMM 
ID   W1N6J9_9GAMM            Unreviewed;       480 AA.
AC   W1N6J9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
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   ORFNames=BJB45_14640 {ECO:0000313|EMBL:ERL51139.1};
OS   Halomonas huangheensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1178482 {ECO:0000313|EMBL:ERL51139.1, ECO:0000313|Proteomes:UP000019113};
RN   [1] {ECO:0000313|EMBL:ERL51139.1, ECO:0000313|Proteomes:UP000019113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BJGMM-B45 {ECO:0000313|EMBL:ERL51139.1,
RC   ECO:0000313|Proteomes:UP000019113};
RA   Miao C., Wan Y., Jin W.;
RT   "draft genome of Halomonas huanghegensis, strain BJGMM-B45T.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|RuleBase:RU000548};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00563,
CC         ECO:0000256|PIRSR:PIRSR001109-2, ECO:0000256|RuleBase:RU000548};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|HAMAP-Rule:MF_00563,
CC       ECO:0000256|PIRSR:PIRSR001109-2, ECO:0000256|RuleBase:RU000548};
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, ECO:0000256|RuleBase:RU000548}.
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERL51139.1}.
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DR   EMBL; AVBC01000033; ERL51139.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1N6J9; -.
DR   STRING; 1178482.AR456_01440; -.
DR   PATRIC; fig|1178482.3.peg.2098; -.
DR   eggNOG; COG0499; Bacteria.
DR   OrthoDB; 9802717at2; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000019113; Unassembled WGS sequence.
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; 3.
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, ECO:0000256|RuleBase:RU000548};
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}; Reference proteome {ECO:0000313|Proteomes:UP000019113}.
FT   DOMAIN          209..392
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         175..177
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         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         209
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         238..243
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         240..245
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         261
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         309
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         330..332
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         386
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         393
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ   SEQUENCE   480 AA;  52999 MW;  1DD9E66932A8C43F CRC64;
     MTSVPPSHCH TSQLTAVDPS YDDFRVMDMS LAEWGRREIR IAETEMPALM AIRARYRDEQ
     PLKDARIAGC IHMTIQTAVL IETLIDLGAS VRWSSCNIFS TQDHAAAAIA AAQIPVFAWK
     GESEEEFWWC IEQTIEGPDG WTPNLVLDDG GDLTLVLHER YPQLLAAIHG ISEETTTGVH
     RLLDMARSGE LKVPAINVND AVTKSKNDNR YGCRHSLNDA IKRALDHLLA GKQALVMGYG
     DVGKGSAASL RQEGMIVRIA EIDPICAMQA CMDGYEVVSP HRNGINQGEA SVDRDLLGRI
     DLVVTATGNV SACDAAMLEA LKNGAVVCNI GHFDSEIDTA FMRREWHWEE VKPQVHRVYR
     DIVPGGDFDP ASRNVIYLLS EGRLVNLGNA TGHPSRVMDG SFANQVLAQM HLYTQRFADL
     PQEQRSAAIA VTVLPRQLDE EVARYMVEGF GGVITQLTAE QAEYCGVAPE GPYKPEHYRY
//
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