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SAHH_BRUA1
ID   SAHH_BRUA1              Reviewed;         466 AA.
AC   B2S994;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=BAbS19_I19640;
OS   Brucella abortus (strain S19).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=430066;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S19;
RX   PubMed=18478107; DOI=10.1371/journal.pone.0002193;
RA   Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S.,
RA   Bricker B., Yu G., Du L., Sobral B.W.;
RT   "Genome sequence of Brucella abortus vaccine strain S19 compared to
RT   virulent strains yields candidate virulence genes.";
RL   PLoS ONE 3:E2193-E2193(2008).
CC   -!- FUNCTION: May play a key role in the regulation of the intracellular
CC       concentration of adenosylhomocysteine. {ECO:0000255|HAMAP-
CC       Rule:MF_00563}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine;
CC         Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.3.1.1;
CC         Evidence={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-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}.
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DR   EMBL; CP000887; ACD73446.1; -; Genomic_DNA.
DR   RefSeq; WP_002965162.1; NC_010742.1.
DR   AlphaFoldDB; B2S994; -.
DR   SMR; B2S994; -.
DR   EnsemblBacteria; ACD73446; ACD73446; BAbS19_I19640.
DR   GeneID; 45053024; -.
DR   GeneID; 55591665; -.
DR   KEGG; bmc:BAbS19_I19640; -.
DR   HOGENOM; CLU_025194_2_0_5; -.
DR   OMA; NKYGCRE; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000002565; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00401; SAHH; 1.
DR   Gene3D; 3.40.50.1480; -; 1.
DR   HAMAP; MF_00563; AdoHcyase; 1.
DR   InterPro; IPR042172; Adenosylhomocyst_ase-like_sf.
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; 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;
KW   Cytoplasm; Hydrolase; NAD; One-carbon metabolism.
FT   CHAIN           1..466
FT                   /note="Adenosylhomocysteinase"
FT                   /id="PRO_1000129272"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         193..195
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         227
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         256..261
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         279
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         314
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         335..337
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         380
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
SQ   SEQUENCE   466 AA;  50791 MW;  6AB3B4B1C2F0BE41 CRC64;
     MTASQDFVVK DISLADWGRK ELDIAETEMP GLMAAREEFG KSQPLKGARI SGSLHMTIQT
     AVLIETLKVL GAEVRWASCN IFSTQDHAAA AIAATGTPVF AVKGETLEEY WTYTDQIFQW
     PDGEPSNMIL DDGGDATMYI LIGARAEAGE DVLSNPQSEE EEVLFAQIKK RMAATPGFFT
     KQRAAIKGVT EETTTGVNRL YQLQKKGLLP FPAINVNDSV TKSKFDNKYG CKESLVDGIR
     RGTDVMMAGK VAVVCGYGDV GKGSAQSLAG AGARVKVTEV DPICALQAAM DGFEVVTLDD
     AASTADIVVT TTGNKDVITI DHMRKMKDMC IVGNIGHFDN EIQVAALRNL KWTNVKPQVD
     LIEFPDGKRL ILLSEGRLLN LGNATGHPSF VMSASFTNQV LGQIELFTRT DAYKNEVYVL
     PKHLDEKVAR LHLDKLGAKL TVLSEEQAAY IGVTPQGPFK SEHYRY
 
 
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