ID   MTAD_BACC3              Reviewed;         435 AA.
AC   C1EPN0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=5-methylthioadenosine/S-adenosylhomocysteine deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE            Short=MTA/SAH deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE            EC=3.5.4.28 {ECO:0000255|HAMAP-Rule:MF_01281};
DE            EC=3.5.4.31 {ECO:0000255|HAMAP-Rule:MF_01281};
GN   Name=mtaD {ECO:0000255|HAMAP-Rule:MF_01281}; OrderedLocusNames=BCA_1873;
OS   Bacillus cereus (strain 03BB102).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=572264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03BB102;
RA   Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C.,
RA   Tapia R., Han C., Sutton G., Sims D.;
RT   "Genome sequence of Bacillus cereus 03BB102.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the deamination of 5-methylthioadenosine and S-
CC       adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-
CC       homocysteine, respectively. Is also able to deaminate adenosine.
CC       {ECO:0000255|HAMAP-Rule:MF_01281}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:20716, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:57985; EC=3.5.4.28; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01281};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-
CC         thioinosine; Xref=Rhea:RHEA:25025, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:48595; EC=3.5.4.31; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01281};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01281};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01281};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       MTA/SAH deaminase family. {ECO:0000255|HAMAP-Rule:MF_01281}.
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DR   EMBL; CP001407; ACO28993.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1EPN0; -.
DR   SMR; C1EPN0; -.
DR   EnsemblBacteria; ACO28993; ACO28993; BCA_1873.
DR   KEGG; bcx:BCA_1873; -.
DR   OMA; ALIGKVC; -.
DR   Proteomes; UP000002210; Chromosome.
DR   GO; GO:0090614; F:5'-methylthioadenosine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050270; F:S-adenosylhomocysteine deaminase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.40.10; -; 1.
DR   HAMAP; MF_01281; MTA_SAH_deamin; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR023512; Deaminase_MtaD/DadD.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..435
FT                   /note="5-methylthioadenosine/S-adenosylhomocysteine
FT                   deaminase"
FT                   /id="PRO_1000165238"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         216
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         304
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
SQ   SEQUENCE   435 AA;  48077 MW;  584DABD4753F1FA1 CRC64;
     MKTTYVNATI VTMNEQNEVI ENGYIIVEND KIIDVNSGEF ASDFEVDEVI DMKGKWVLPG
     LVNTHTHVVM SLLRGIGDDM LLQPWLETRI WPLESQFTSQ IAVASTELGL LEMVKSGTTS
     FSDMFNPIGV DQDAIMETVS RSGMRAAVSR TLFSFGTKED EKKAIEEAEK YVKRYYNESG
     MLTTMVAPHS PYTCSTELLE ECARIAVENQ TMVHIHLSET EREVRDIEAQ YGKRPVEYAA
     SCGLFKRSTV IAHGVVLNDN ERAFLAEHDV RVAHNPNSNL KLGSGIANVK AMLEAGIKVG
     IATDSVASNN NLDMFEEMRI ATLLQKGIHQ DATALPVETA LTLATKGAAE VIGMKQTGSL
     EVGKCADFIT IDPSNKPHLQ PADEVLSHLV YAASGKDISD VIINGKRVVW NGECKTLDEE
     RIIFEASRYK RGLQR