SAHH_METEP
ID SAHH_METEP Reviewed; 468 AA.
AC A9VYP7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Adenosylhomocysteinase {ECO:0000255|HAMAP-Rule:MF_00563};
DE EC=3.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00563};
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000255|HAMAP-Rule:MF_00563};
DE Short=AdoHcyase {ECO:0000255|HAMAP-Rule:MF_00563};
GN Name=ahcY {ECO:0000255|HAMAP-Rule:MF_00563}; OrderedLocusNames=Mext_4433;
OS Methylorubrum extorquens (strain PA1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=419610;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Marx C., Richardson P.;
RT "Complete sequence of Methylobacterium extorquens PA1.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a key role in the regulation of the intracellular
CC concentration of adenosylhomocysteine. {ECO:0000255|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=3.3.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00563};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00563};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00563};
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00563}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00563}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00563}.
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DR EMBL; CP000908; ABY32801.1; -; Genomic_DNA.
DR RefSeq; WP_003606448.1; NC_010172.1.
DR AlphaFoldDB; A9VYP7; -.
DR SMR; A9VYP7; -.
DR STRING; 419610.Mext_4433; -.
DR EnsemblBacteria; ABY32801; ABY32801; Mext_4433.
DR KEGG; mex:Mext_4433; -.
DR eggNOG; COG0499; Bacteria.
DR HOGENOM; CLU_025194_2_1_5; -.
DR OMA; NKYGCRE; -.
DR BioCyc; MEXT419610:MEXT_RS22280-MON; -.
DR UniPathway; UPA00314; UER00076.
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; -; 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 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 Cytoplasm; Hydrolase; NAD; One-carbon metabolism.
FT CHAIN 1..468
FT /note="Adenosylhomocysteinase"
FT /id="PRO_1000129287"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 195..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 258..263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 281
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 316
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 337..339
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 382
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
SQ SEQUENCE 468 AA; 51024 MW; EC7463AF4D3425D0 CRC64;
MAVANDYIVK DIGLADYGRK EISIAETEMP GLMSTRAEYG ASQPLKGAKI AGSLHMTIQT
AVLIETLKAL GADIRWVSCN IYSTQDHAAA AIAAAGIPVF AVKGETLTEY WDYTSKLFDW
HDGGMPNMIL DDGGDATMFV HLGLRAENGD TAFLDKPESE EEEVFFALLK KKLAEKPKGW
FAGLADSIKG VSEETTTGVH RLYNLAKEGK LLFPAINVND SVTKSKFDNL YGCKESLVDG
IRRGTDVMMA GKVAMVAGFG DVGKGSAASL RNAGCRVLVS EIDPICALQA AMEGYEVVTM
EDAAPRADIF VTATGNKDII TIEHMRAMKD RAIVCNIGHF DNEIQVAGLK NLKWQNIKPQ
VDEIEFADGH RIILLSEGRL VNLGNATGHP SFVMSASFTN QTLAQIELWT NPGKYERQVY
TLPKALDEKV AALHLEKIGV KLSKLRPDQA AYIGVSQTGP FKPEHYRY
