(data stored in ACNUC7421 zone)

SWISSPROT: SAHH_PSEAB

ID   SAHH_PSEAB              Reviewed;         469 AA.
AC   Q02TY0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 77.
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=PA14_05620;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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:
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-
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}.
DR   EMBL; CP000438; ABJ15399.1; -; Genomic_DNA.
DR   RefSeq; WP_004365056.1; NC_008463.1.
DR   ProteinModelPortal; Q02TY0; -.
DR   SMR; Q02TY0; -.
DR   PRIDE; Q02TY0; -.
DR   EnsemblBacteria; ABJ15399; ABJ15399; PA14_05620.
DR   KEGG; pau:PA14_05620; -.
DR   HOGENOM; HOG000227986; -.
DR   KO; K01251; -.
DR   OMA; TGNRDII; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
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; 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   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; Q02TY0.
DR   SWISS-2DPAGE; Q02TY0.
KW   Complete proteome; Cytoplasm; Hydrolase; NAD; One-carbon metabolism.
FT   CHAIN         1    469       Adenosylhomocysteinase.
FT                                /FTId=PRO_1000024748.
FT   NP_BIND     165    167       NAD. {ECO:0000255|HAMAP-Rule:MF_00563}.
FT   NP_BIND     228    233       NAD. {ECO:0000255|HAMAP-Rule:MF_00563}.
FT   NP_BIND     321    323       NAD. {ECO:0000255|HAMAP-Rule:MF_00563}.
FT   BINDING      63     63       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00563}.
FT   BINDING     139    139       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00563}.
FT   BINDING     164    164       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00563}.
FT   BINDING     194    194       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00563}.
FT   BINDING     198    198       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00563}.
FT   BINDING     199    199       NAD. {ECO:0000255|HAMAP-Rule:MF_00563}.
FT   BINDING     251    251       NAD. {ECO:0000255|HAMAP-Rule:MF_00563}.
FT   BINDING     300    300       NAD. {ECO:0000255|HAMAP-Rule:MF_00563}.
FT   BINDING     375    375       NAD. {ECO:0000255|HAMAP-Rule:MF_00563}.
SQ   SEQUENCE   469 AA;  51426 MW;  B545630AA4E47A9D CRC64;
     MSAVMTPAGF TDYKVADITL AAWGRRELII AESEMPALMG LRRKYAGQQP LKGAKILGCI
     HMTIQTGVLI ETLVALGAEV RWSSCNIFST QDQAAAAIAA AGIPVFAWKG ETEEEYEWCI
     EQTILKDGQP WDANMVLDDG GDLTEILHKK YPQMLERIHG ITEETTTGVH RLLDMLKNGT
     LKVPAINVND SVTKSKNDNK YGCRHSLNDA IKRGTDHLLS GKQALVIGYG DVGKGSSQSL
     RQEGMIVKVA EVDPICAMQA CMDGFEVVSP YKNGINDGTE ASIDAALLGK IDLIVTTTGN
     VNVCDANMLK ALKKRAVVCN IGHFDNEIDT AFMRKNWAWE EVKPQVHKIH RTGKDGFDAY
     NDDYLILLAE GRLVNLGNAT GHPSRIMDGS FANQVLAQIH LFEQKYADLP AAEKAKRLSV
     EVLPKKLDEE VALEMVKGFG GVVTQLTPKQ AEYIGVSVEG PFKPDTYRY
//

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