(data stored in SCRATCH zone)

SWISSPROT: Q2IMA1_ANADE

ID   Q2IMA1_ANADE            Unreviewed;       491 AA.
AC   Q2IMA1;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 107.
DE   RecName: Full=Adenosylhomocysteinase {ECO:0000256|HAMAP-Rule:MF_00563};
DE            EC=3.3.1.1 {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   OrderedLocusNames=Adeh_0156 {ECO:0000313|EMBL:ABC79933.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79933.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|EMBL:ABC79933.1, ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|EMBL:ABC79933.1,
RC   ECO:0000313|Proteomes:UP000001935};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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:0000256|HAMAP-Rule:MF_00563}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-
CC         homocysteine; Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16335, ChEBI:CHEBI:57856, ChEBI:CHEBI:58199;
CC         EC=3.3.1.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00563,
CC         ECO:0000256|RuleBase:RU000548};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00563, ECO:0000256|RuleBase:RU000548};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|HAMAP-Rule:MF_00563,
CC       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|HAMAP-Rule:MF_00563, ECO:0000256|RuleBase:RU004166}.
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DR   EMBL; CP000251; ABC79933.1; -; Genomic_DNA.
DR   RefSeq; WP_011419216.1; NC_007760.1.
DR   STRING; 290397.Adeh_0156; -.
DR   EnsemblBacteria; ABC79933; ABC79933; Adeh_0156.
DR   KEGG; ade:Adeh_0156; -.
DR   eggNOG; ENOG4105C3E; Bacteria.
DR   eggNOG; COG0499; LUCA.
DR   HOGENOM; HOG000227986; -.
DR   KO; K01251; -.
DR   OMA; QSTWDGI; -.
DR   BioCyc; ADEH290397:G1G5W-160-MONOMER; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000001935; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019510; P:S-adenosylhomocysteine catabolic process; IEA:InterPro.
DR   CDD; cd00401; SAHH; 1.
DR   HAMAP; MF_00563; AdoHcyase; 1.
DR   InterPro; IPR034373; Adenosylhomocysteinase.
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;
DR   PRODOM; Q2IMA1.
DR   SWISS-2DPAGE; Q2IMA1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00563};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00563,
KW   ECO:0000256|RuleBase:RU000548, ECO:0000313|EMBL:ABC79933.1};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00563, ECO:0000256|RuleBase:RU000548};
KW   One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00563,
KW   ECO:0000256|RuleBase:RU000548};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935}.
FT   DOMAIN      251    411       AdoHcyase_NAD. {ECO:0000259|SMART:
FT                                SM00997}.
FT   NP_BIND     217    219       NAD. {ECO:0000256|HAMAP-Rule:MF_00563}.
FT   NP_BIND     280    285       NAD. {ECO:0000256|HAMAP-Rule:MF_00563}.
FT   NP_BIND     359    361       NAD. {ECO:0000256|HAMAP-Rule:MF_00563}.
FT   BINDING      70     70       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00563, ECO:0000256|PIRSR:PIRSR001109-
FT                                1}.
FT   BINDING     154    154       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00563, ECO:0000256|PIRSR:PIRSR001109-
FT                                1}.
FT   BINDING     216    216       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00563, ECO:0000256|PIRSR:PIRSR001109-
FT                                1}.
FT   BINDING     246    246       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00563, ECO:0000256|PIRSR:PIRSR001109-
FT                                1}.
FT   BINDING     250    250       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00563, ECO:0000256|PIRSR:PIRSR001109-
FT                                1}.
FT   BINDING     251    251       NAD. {ECO:0000256|HAMAP-Rule:MF_00563}.
FT   BINDING     303    303       NAD. {ECO:0000256|HAMAP-Rule:MF_00563}.
FT   BINDING     338    338       NAD. {ECO:0000256|HAMAP-Rule:MF_00563}.
FT   BINDING     405    405       NAD. {ECO:0000256|HAMAP-Rule:MF_00563}.
SQ   SEQUENCE   491 AA;  53248 MW;  3B52C030253D75A8 CRC64;
     MAVSAAKKKP APSAPAPFEH KVKDLSLAGW GRKEIELAEK EMPGLMAVRR EYARQRPLAG
     QRITGSLHMT IQTAVLIETL VDLGADVRWA SCNIFSTQDH AAAAVVVGRD GTPEAPRGVP
     VFAWKGETLE EYWDCTERAL DFGGGKGPTQ IVDDGGDATL LIHKGAEYEK AGKVPPPSSA
     GSEELEVVLR LLAREQKKDA RRWTRVAKAC AGVTEETTTG VHRLYEMQKA GTLLFPAINV
     NDSVTKSKFD NLYGCRHSLV DGLNRAADVM LAGKLCVVCG YGDVGKGCAQ ALRGQGARVV
     VTEIDPINAL QASMEGYQVV RLEDVVEHAD VFVTATGNLD VVTVEHMKAM KDCAIVGNIG
     HFDNEIDMAG LRKAATRVNI KPQYDAFVFP DGHRVLVLAE GRLLNLGCAT GHPSFVMSNS
     FTNQTLAQIE LAVNRAAYAK QVYVLPKHLD EKVAALHLEQ IGARLTKLSK KQAAYIGVPQ
     SGPFKPEHYR Y
//

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