ID Q24WB4_DESHY Unreviewed; 424 AA.
AC Q24WB4;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 01-MAY-2013, entry version 61.
DE RecName: Full=Adenosylhomocysteinase;
DE EC=3.3.1.1;
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase;
GN Name=ahcY; OrderedLocusNames=DSY1889;
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51;
RX PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
CC -!- FUNCTION: May play a key role in the regulation of the
CC intracellular concentration of adenosylhomocysteine (By
CC similarity).
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; L-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; AP008230; BAE83678.1; -; Genomic_DNA.
DR RefSeq; YP_518122.1; NC_007907.1.
DR ProteinModelPortal; Q24WB4; -.
DR STRING; 138119.DSY1889; -.
DR EnsemblBacteria; BAE83678; BAE83678; DSY1889.
DR GeneID; 3953596; -.
DR KEGG; dsy:DSY1889; -.
DR PATRIC; 21672320; VBIDesHaf65307_2107.
DR eggNOG; COG0499; -.
DR HOGENOM; HOG000227987; -.
DR KO; K01251; -.
DR OMA; TIGMALH; -.
DR ProtClustDB; PRK05476; -.
DR BioCyc; DHAF138119:GHT5-1890-MONOMER; -.
DR UniPathway; UPA00314; UER00076.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:HAMAP.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:HAMAP.
DR Gene3D; 3.40.50.720; -; 1.
DR HAMAP; MF_00563; AdoHcyase; 1; -.
DR InterPro; IPR000043; Adenosylhomocysteinase.
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 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 NP_BIND 158 160 NAD (By similarity).
FT NP_BIND 221 226 NAD (By similarity).
FT NP_BIND 300 302 NAD (By similarity).
FT BINDING 132 132 Substrate (By similarity).
FT BINDING 157 157 Substrate (By similarity).
FT BINDING 187 187 Substrate (By similarity).
FT BINDING 191 191 Substrate (By similarity).
FT BINDING 192 192 NAD (By similarity).
FT BINDING 244 244 NAD (By similarity).
FT BINDING 279 279 NAD (By similarity).
FT BINDING 347 347 NAD (By similarity).
SQ SEQUENCE 424 AA; 46612 MW; 1F5AEC4BF999F7A5 CRC64;
MTWLSQDNME STIRDIGLAP QGQLKIDWVQ AHMPVLNTLR EEFEKTQPFQ GKKVTICLHL
EAKTAYLAKV VQAGGAEVTV AASNPLSTQD DVVAALVAGG VHAHAWYGAT DEEYHQHLHK
ALDFEPDYII DDGGDLVSTL HKERRELLPK VLGGAEETTT GILRLRAMEK NGELAFPMMA
VNDAEMKYLF DNRYGTGQSV WDGIMRTTNL VVAGKTVCVV GYGWCGKGVA LRAKGLGARV
IICEVNPIKA NEAWMDGFEV MPMLAAAPLG DFFVTVTGNK NVISGEHFQV MKDGAILANA
GHFDVEVNKV QLAAMAQSCR EVRRNIEEYL LQDGRKIYLL AEGRLVNLAA GDGHPAEVMD
MTFALQALAL HYLATVKTPL EPKVYSVPTE MDMRVAELKL KTLGLSIDQL SEEQKSYLAS
WQHS
//
