ID   SAHH_BURTA              Reviewed;         473 AA.
AC   Q2STU0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 30.
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=BTH_I3165;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000086; ABC37731.1; -; Genomic_DNA.
DR   RefSeq; YP_443659.1; -.
DR   GeneID; 3849850; -.
DR   GenomeReviews; CP000086_GR; BTH_I3165.
DR   KEGG; bte:BTH_I3165; -.
DR   TIGR; BTH_I3165; -.
DR   HOGENOM; Q2STU0; -.
DR   OMA; Q2STU0; HMRAMKD.
DR   BioCyc; BTHA271848:BTH_I3165-MON; -.
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    473       Adenosylhomocysteinase.
FT                                /FTId=PRO_1000024720.
FT   REGION      226    391       NAD binding (By similarity).
FT   BINDING      64     64       Substrate (By similarity).
FT   BINDING     139    139       Substrate (By similarity).
FT   BINDING     199    199       Substrate (By similarity).
FT   BINDING     229    229       Substrate (By similarity).
FT   BINDING     233    233       Substrate (By similarity).
SQ   SEQUENCE   473 AA;  52160 MW;  F1198EAA912306C8 CRC64;
     MNAAVIDSNS AQDYVVADIA LAGWGRKELN IAETEMPGLV QIRDEYKAQQ PLKGARIAGS
     LHMTIQTGVL IETLKALGAD VRWASCNIFS TQDHAAAAIV EAGTPVFAFK GESLDEYWEF
     SHRIFEWPNG EFANMILDDG GDATLLLILG SKAEKDRSVI AKPTNEEEVA LFKSIERHLE
     IDGSWYSKRL AHIKGVTEET TTGVHRLYQM EKDGRLPFPA FNVNDSVTKS KFDNLYGCRE
     SLVDGIKRAT DVMIAGKIAV VAGYGDVGKG CAQSLRGLGA TVWVTEIDPI CALQAAMEGY
     RVVTMEYAAD KADIFVTATG NYHVINHDHM KAMRHNAIVC NIGHFDSEID VASTRQYQWE
     NIKPQVDHII FPDGKRVILL AEGRLVNLGC ATGHPSFVMS NSFTNQTLAQ IELFTRGGEY
     ANKVYVLPKH LDEKVARLHL ARIGAQLSEL SDDQAAYIGV PKAGPFKPDH YRY
//