SAHH_BRUO2
ID SAHH_BRUO2 Reviewed; 466 AA.
AC A5VT52;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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}; OrderedLocusNames=BOV_2015;
OS Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=444178;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT range and tissue tropism.";
RL PLoS ONE 4:E5519-E5519(2009).
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; CP000708; ABQ61286.1; -; Genomic_DNA.
DR RefSeq; WP_006014498.1; NC_009505.1.
DR AlphaFoldDB; A5VT52; -.
DR SMR; A5VT52; -.
DR EnsemblBacteria; ABQ61286; ABQ61286; BOV_2015.
DR GeneID; 45125349; -.
DR KEGG; bov:BOV_2015; -.
DR HOGENOM; CLU_025194_2_0_5; -.
DR OMA; NKYGCRE; -.
DR PhylomeDB; A5VT52; -.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000006383; Chromosome I.
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_1000024713"
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; 50777 MW; 5F25EDD0E3480F6A CRC64;
MTASQDFVVK DISLADWGRK ELDIAETEMP GLMAAREEFG KSQPLKGARI SGSLHMTIQT
AVLIETLKVL GAEVRWASCN IFSTQDHAAA AIAATGTPVF AVKGETLEEY WTYTDQIFQW
PDGEPSNMIL DDGGDATMYI LIGARAEAGE DVLSNPQSEE EEVLFAQIKK RMAATPGFFT
KQRAAIKGVT EETTTGVNRL YQLQKKGLLP FPAINVNDSV TKSKFDNKYG CKESLVDGVR
RGTDVMMAGK VAVVCGYGDV GKGSAQSLAG AGARVKVTEV DPICALQAAM DGFEVVTLDD
AASTADIVVT TTGNKDVITI DHMRKMKDMC IVGNIGHFDN EIQVAALRNL KWTNVKPQVD
LIEFPDGKRL ILLSEGRLLN LGNATGHPSF VMSASFTNQV LGQIELFTRT DAYKNEVYVL
PKHLDEKVAR LHLDKLGAKL TVLSEEQAAY IGVTPQGPFK SEHYRY
