(data stored in ACNUC7421 zone)

SWISSPROT: A0LF64_SYNFM

ID   A0LF64_SYNFM            Unreviewed;       418 AA.
AC   A0LF64;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 91.
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=Sfum_0366 {ECO:0000313|EMBL:ABK16066.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16066.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK16066.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00563}.
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DR   EMBL; CP000478; ABK16066.1; -; Genomic_DNA.
DR   RefSeq; WP_011697239.1; NC_008554.1.
DR   STRING; 335543.Sfum_0366; -.
DR   EnsemblBacteria; ABK16066; ABK16066; Sfum_0366.
DR   KEGG; sfu:Sfum_0366; -.
DR   eggNOG; ENOG4105C3E; Bacteria.
DR   eggNOG; COG0499; LUCA.
DR   HOGENOM; HOG000227987; -.
DR   KO; K01251; -.
DR   OMA; QPTHLCE; -.
DR   OrthoDB; 522981at2; -.
DR   BioCyc; SFUM335543:G1G7I-371-MONOMER; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000001784; 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; 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; 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; A0LF64.
DR   SWISS-2DPAGE; A0LF64.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00563};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00563,
KW   ECO:0000256|RuleBase:RU000548, ECO:0000313|EMBL:ABK16066.1};
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:UP000001784}.
FT   DOMAIN      185    346       AdoHcyase_NAD. {ECO:0000259|SMART:
FT                                SM00997}.
FT   NP_BIND     151    153       NAD. {ECO:0000256|HAMAP-Rule:MF_00563}.
FT   NP_BIND     214    219       NAD. {ECO:0000256|HAMAP-Rule:MF_00563}.
FT   NP_BIND     293    295       NAD. {ECO:0000256|HAMAP-Rule:MF_00563}.
FT   BINDING      53     53       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00563, ECO:0000256|PIRSR:PIRSR001109-
FT                                1}.
FT   BINDING     125    125       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00563, ECO:0000256|PIRSR:PIRSR001109-
FT                                1}.
FT   BINDING     150    150       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00563, ECO:0000256|PIRSR:PIRSR001109-
FT                                1}.
FT   BINDING     180    180       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00563, ECO:0000256|PIRSR:PIRSR001109-
FT                                1}.
FT   BINDING     184    184       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00563, ECO:0000256|PIRSR:PIRSR001109-
FT                                1}.
FT   BINDING     185    185       NAD. {ECO:0000256|HAMAP-Rule:MF_00563}.
FT   BINDING     237    237       NAD. {ECO:0000256|HAMAP-Rule:MF_00563}.
FT   BINDING     340    340       NAD. {ECO:0000256|HAMAP-Rule:MF_00563}.
SQ   SEQUENCE   418 AA;  45597 MW;  C22EBED82CA96847 CRC64;
     MEFDVKDPGL AEKGKLRIEW AAQSMPVLRS IHKRFAAEKP LQGTRIAACL HVTTETASLA
     QTLKAGGAEV RICASNPLST QDDVAASLVV NDSIPVFAIK GEDKDTYYRH INSALGHSPH
     ITMDDGADLV STLHSDRREL LQGILGGTEE TTTGVIRLRS MADKGVLQYP IIAVNDASTK
     HLFDNRYGTG QSTVDGIVRA TNRLLAGSGF VVSGYGWCGR GVAMRASGMG AKVIITEVDP
     LRALEAVMDG YQVMPMEQAA VVGDFFCTLT GDIHVIRREH FAVMKDGAIV CNSGHFNVEI
     DLDALASMAV ARREIRDFVE EFKLADGRRV YVLGEGRLIN LAAAEGHPSS VMDMSFANQA
     LCTEHMVKHH TTLKKQVYRV PMEIDKNIAK LKLASMNVDI DTLTPEQDAY LHSWEMGT
//

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