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Database: UniProt
Entry: B7KSJ4
LinkDB: B7KSJ4
Original site: B7KSJ4 
ID   SAHH_METC4              Reviewed;         468 AA.
AC   B7KSJ4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   01-OCT-2014, entry version 36.
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};
GN   OrderedLocusNames=Mchl_4897;
OS   Methylobacterium extorquens (strain CM4 / NCIMB 13688)
OS   (Methylobacterium chloromethanicum).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=440085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM4 / NCIMB 13688;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Marx C., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium chloromethanicum
RT   CM4.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a key role in the regulation of the
CC       intracellular concentration of adenosylhomocysteine.
CC       {ECO:0000255|HAMAP-Rule:MF_00563}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = L-
CC       homocysteine + adenosine. {ECO:0000255|HAMAP-Rule:MF_00563}.
CC   -!- COFACTOR: Binds 1 NAD per subunit. {ECO:0000255|HAMAP-
CC       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; CP001298; ACK85662.1; -; Genomic_DNA.
DR   RefSeq; YP_002423590.1; NC_011757.1.
DR   ProteinModelPortal; B7KSJ4; -.
DR   SMR; B7KSJ4; 6-468.
DR   STRING; 440085.Mchl_4897; -.
DR   EnsemblBacteria; ACK85662; ACK85662; Mchl_4897.
DR   GeneID; 7114318; -.
DR   KEGG; mch:Mchl_4897; -.
DR   PATRIC; 22504084; VBIMetChl132133_4853.
DR   eggNOG; COG0499; -.
DR   HOGENOM; HOG000227986; -.
DR   KO; K01251; -.
DR   OMA; EAIMDGF; -.
DR   OrthoDB; EOG6F296M; -.
DR   BioCyc; MCHL440085:GCXT-4971-MONOMER; -.
DR   UniPathway; UPA00314; UER00076.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP.
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   TIGRFAMs; TIGR00936; ahcY; 1.
DR   PROSITE; PS00738; ADOHCYASE_1; 1.
DR   PROSITE; PS00739; ADOHCYASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Hydrolase; NAD; One-carbon metabolism.
FT   CHAIN         1    468       Adenosylhomocysteinase.
FT                                /FTId=PRO_1000196670.
FT   NP_BIND     195    197       NAD. {ECO:0000255|HAMAP-Rule:MF_00563}.
FT   NP_BIND     258    263       NAD. {ECO:0000255|HAMAP-Rule:MF_00563}.
FT   NP_BIND     337    339       NAD. {ECO:0000255|HAMAP-Rule:MF_00563}.
FT   BINDING      57     57       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00563}.
FT   BINDING     132    132       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00563}.
FT   BINDING     194    194       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00563}.
FT   BINDING     224    224       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00563}.
FT   BINDING     228    228       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00563}.
FT   BINDING     229    229       NAD. {ECO:0000255|HAMAP-Rule:MF_00563}.
FT   BINDING     281    281       NAD. {ECO:0000255|HAMAP-Rule:MF_00563}.
FT   BINDING     316    316       NAD. {ECO:0000255|HAMAP-Rule:MF_00563}.
FT   BINDING     382    382       NAD. {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
//
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