ID   MTAD_THEKO              Reviewed;         424 AA.
AC   Q5JER0;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=TK1891;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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; AP006878; BAD86080.1; -; Genomic_DNA.
DR   RefSeq; WP_011250842.1; NC_006624.1.
DR   AlphaFoldDB; Q5JER0; -.
DR   SMR; Q5JER0; -.
DR   STRING; 69014.TK1891; -.
DR   EnsemblBacteria; BAD86080; BAD86080; TK1891.
DR   GeneID; 3235534; -.
DR   KEGG; tko:TK1891; -.
DR   PATRIC; fig|69014.16.peg.1849; -.
DR   eggNOG; arCOG00695; Archaea.
DR   HOGENOM; CLU_012358_2_1_2; -.
DR   InParanoid; Q5JER0; -.
DR   OMA; ALIGKVC; -.
DR   OrthoDB; 40873at2157; -.
DR   PhylomeDB; Q5JER0; -.
DR   Proteomes; UP000000536; 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..424
FT                   /note="5-methylthioadenosine/S-adenosylhomocysteine
FT                   deaminase"
FT                   /id="PRO_0000312487"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
SQ   SEQUENCE   424 AA;  46655 MW;  3C88F8DE8C03602F CRC64;
     MSILIKNGHV IYGENLDVVR ADVLIESNRI VSVERNINEA ADTVIDATGR VVSPGFINLH
     THSPMGLLRG LADDLPLMEW LQNHIWPREA KLTPEYVKVG AYLGALEMIR SGTTTFLDMY
     FHMDKVAEAV LDAGLRGYLS YGMIDLGDPD RTEKELKEAL REMEAIEKLN SERVHFVFGP
     HAPYTCSIAL LKEVRKLASE HNKLITIHVS ETMAEIGQIT ERYGKSPVVL LDDIGFLGND
     VIIAHGVWLD SRDIQILARH GVTVAHNPGS NMKLASGVMP LEKLLNAGVN IGLGTDGSAS
     NNNLDMLEEM KLAALLHKVH NLDPTIADAR TVFRMATQNG AKALRLNAGI IKEGYLADIA
     IINFNRPHLR PINDVISHLV YSANGNDVET TIVDGKILML DGEVLTLDEE KVISEAEKVS
     EKLA