位置:首页 > 蛋白库 > SAHH_METC4
SAHH_METC4
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   03-AUG-2022, entry version 73.
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=Mchl_4897;
OS   Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS   extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
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., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   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 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001298; ACK85662.1; -; Genomic_DNA.
DR   RefSeq; WP_003606448.1; NC_011757.1.
DR   AlphaFoldDB; B7KSJ4; -.
DR   SMR; B7KSJ4; -.
DR   EnsemblBacteria; ACK85662; ACK85662; Mchl_4897.
DR   KEGG; mch:Mchl_4897; -.
DR   HOGENOM; CLU_025194_2_1_5; -.
DR   OMA; NKYGCRE; -.
DR   BioCyc; MEXT440085:MCHL_RS23815-MON; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000002385; 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; -; 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_1000196670"
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024