ID   MTAD_SYNWW              Reviewed;         431 AA.
AC   Q0AYV2;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=Swol_0781;
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen;
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI68102.1; -; Genomic_DNA.
DR   RefSeq; WP_011640207.1; NC_008346.1.
DR   AlphaFoldDB; Q0AYV2; -.
DR   SMR; Q0AYV2; -.
DR   STRING; 335541.Swol_0781; -.
DR   EnsemblBacteria; ABI68102; ABI68102; Swol_0781.
DR   KEGG; swo:Swol_0781; -.
DR   eggNOG; COG0402; Bacteria.
DR   HOGENOM; CLU_012358_2_1_9; -.
DR   OMA; ALIGKVC; -.
DR   OrthoDB; 1592010at2; -.
DR   Proteomes; UP000001968; 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; Reference proteome; Zinc.
FT   CHAIN           1..431
FT                   /note="5-methylthioadenosine/S-adenosylhomocysteine
FT                   deaminase"
FT                   /id="PRO_0000312461"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         210
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         299
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         299
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
SQ   SEQUENCE   431 AA;  47578 MW;  B69D18133551F1F5 CRC64;
     MRILLDNISI IPVSGSNSFI EKGYLLIEDV FIKELGTGKA PEGEFDHIID GENQVLLPGF
     INAHTHAAMT LLRGYADDLP LMEWLENKIW PLEAKLTPED IYWGTMLAIV EMIKSGTTTF
     NDMYFCMDEV ARAVELSGMR AVLARGMVGV GPESEQAIED SRELIGKWQG QAGGRISFRL
     GPHAPYTCPP AYLERVMQLS DELQAGIHIH VAETRVEYED ILKQYGKTPV SHLESLGLFQ
     GRQVLAAHCV HLNEEEIGIL HQYQVGVAHN PESNMKLASG IAPVPRMLES GIAVALGTDG
     ASSNNNLDML QEMRSSSFLH KVNTMDPMVL PAYQALEMAT ANGAISLGMG NELGRLEPGY
     RADMIIMNLK EAHMTPRYDL LANIVYSAQA SDVNSVIIDG KIVMENREIK TFDEQEVLAK
     ARETARKLVG K