ID   SAHH_BARHE              Reviewed;         465 AA.
AC   Q6G584;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Adenosylhomocysteinase;
DE            EC=3.3.1.1;
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase;
DE            Short=AdoHcyase;
GN   Name=ahcY; OrderedLocusNames=BH00310;
OS   Bartonella henselae (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=38323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = L-
CC       homocysteine + adenosine.
CC   -!- COFACTOR: Binds 1 NAD per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; homocysteine biosynthesis; L-
CC       homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
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DR   EMBL; BX897699; CAF26847.1; -; Genomic_DNA.
DR   RefSeq; YP_032900.1; -.
DR   GeneID; 2866066; -.
DR   GenomeReviews; BX897699_GR; BH00310.
DR   KEGG; bhe:BH00310; -.
DR   NMPDR; fig|283166.1.peg.28; -.
DR   HOGENOM; Q6G584; -.
DR   OMA; Q6G584; HMRAMKD.
DR   BioCyc; BHEN283166:BH00310-MON; -.
DR   BRENDA; 3.3.1.1; 277357.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:HAMAP.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon compound metabolic process; IEA:HAMAP.
DR   HAMAP; MF_00563; -; 1.
DR   InterPro; IPR000043; Ad_hcy_hydrolase.
DR   InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR   Gene3D; G3DSA:3.40.50.1480; Ad_hcy_hydrolase; 1.
DR   PANTHER; PTHR23420; Ad_hcy_hydrolase; 1.
DR   Pfam; PF05221; AdoHcyase; 1.
DR   Pfam; PF00670; AdoHcyase_NAD; 1.
DR   PIRSF; PIRSF001109; Ad_hcy_hydrolase; 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    465       Adenosylhomocysteinase.
FT                                /FTId=PRO_0000116944.
FT   REGION      218    383       NAD binding (By similarity).
FT   BINDING      56     56       Substrate (By similarity).
FT   BINDING     131    131       Substrate (By similarity).
FT   BINDING     191    191       Substrate (By similarity).
FT   BINDING     221    221       Substrate (By similarity).
FT   BINDING     225    225       Substrate (By similarity).
SQ   SEQUENCE   465 AA;  51029 MW;  45F2E7583A655434 CRC64;
     MTAQDYVVKD IALAAYGRKE LDIAETEMPG LMACREEFSS SQPLRGARIS GSLHMTIQTA
     VLIETLKAIG ANVRWSSSNI FSTQDHAAAA IAATGTPVFA VKGETLEEYW TYIDAIFQWP
     DGNPSNLILD DGADATNYIL MGSRAETNKD ILSHPKTEEE ELFFKQIQRR MEATPGFFTR
     QRAAIKGISE ETTTGVHRLH QLQKEGLLPF PAININDSVT KSKFDNKYGC RESLVDGIRR
     ATDVMIAGKT AIVCGYGDVG KGSAASLSGA GARVKVTEID PICALQAAMD GYEVVNLDDA
     ASSADIIITT TGNKDIVRLD HMRKVKDMCI LGNIGHFDNE IQVAALQNLP WTNIKPQVDM
     ITFPDGKRII LLSEGRLLNL GNATGHPSFV MSASFTNQVL AQIELFTRSG HYKNEVTVLP
     KYLDEKVARL HLDQLGIKLT TLSQEQAAYI GVTPQGPYKP DHYRY
//