ID A0A1Y2RBT8_9BACT Unreviewed; 442 AA.
AC A0A1Y2RBT8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=CAP36_13745 {ECO:0000313|EMBL:OSZ77444.1};
OS Chitinophagaceae bacterium IBVUCB2.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae.
OX NCBI_TaxID=1985174 {ECO:0000313|EMBL:OSZ77444.1, ECO:0000313|Proteomes:UP000194400};
RN [1] {ECO:0000313|EMBL:OSZ77444.1, ECO:0000313|Proteomes:UP000194400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBVUCB2 {ECO:0000313|EMBL:OSZ77444.1,
RC ECO:0000313|Proteomes:UP000194400};
RA Orr R.J.;
RT "Draft genome sequences of novel bacteria, isolated from environmental
RT samples.";
RL Submitted (MAY-2017) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00563}.
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:OSZ77444.1}.
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DR EMBL; NFUV01000002; OSZ77444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2RBT8; -.
DR STRING; 1985174.CAP36_13745; -.
DR InParanoid; A0A1Y2RBT8; -.
DR OrthoDB; 9802717at2; -.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000194400; 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; 2.
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; 2.
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:UP000194400}.
FT DOMAIN 201..362
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 167..169
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 196
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT BINDING 230..235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT BINDING 232..237
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 253
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..311
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 356
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 363
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 442 AA; 48000 MW; 2D2FB3F4964AE4AF CRC64;
MSTLSKTSID FSLAYKVADI SLAEWGRKEI RLAEAEMPGL MAIRKEYGPS QPLKGARVAG
CLHMTIQTAV LIETLTALGA EVKWSSCNIF STQDHAAAAI AAAGIGVFAW KGQSQAEADW
CIEQTLFFGS ADKPLNMILD DGGDLTNMVL DTYPELIQHV KGISEETTTG VHRLYERVAK
GTLPMPAINV NDSVTKSKFD NKYGCKESLV DSIRRATDVM LAGKVAVVGG YGDVGKGSAA
SLAGAGCRVI VTEIDPICAL QAAMDGFEVK KMIDAVKEAD IVVTASGCRD LITGAHFKAM
KDKAIVCNIG HFDIEIDIAW LNDNYGSTKD TIKPQVDIYN VEGKDIIILA EGRLVNLGCA
TGHPSFVMSN SFSNQTLAQI ELWLNHKNYE NKVYVLPKHL DEKVARLHLE KIGVVLEELT
TAQAEYLGIS KEGPFKSDLY RY
//
