ID   MTAD_PYRFU              Reviewed;         419 AA.
AC   Q8U0P7;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=PF1538;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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; AE009950; AAL81662.1; -; Genomic_DNA.
DR   RefSeq; WP_011012685.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U0P7; -.
DR   SMR; Q8U0P7; -.
DR   STRING; 186497.PF1538; -.
DR   EnsemblBacteria; AAL81662; AAL81662; PF1538.
DR   GeneID; 41713357; -.
DR   KEGG; pfu:PF1538; -.
DR   PATRIC; fig|186497.12.peg.1603; -.
DR   eggNOG; arCOG00695; Archaea.
DR   HOGENOM; CLU_012358_2_1_2; -.
DR   OMA; ALIGKVC; -.
DR   OrthoDB; 40873at2157; -.
DR   PhylomeDB; Q8U0P7; -.
DR   Proteomes; UP000001013; 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..419
FT                   /note="5-methylthioadenosine/S-adenosylhomocysteine
FT                   deaminase"
FT                   /id="PRO_0000312486"
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         294
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
SQ   SEQUENCE   419 AA;  46707 MW;  C2C88267288D9E33 CRC64;
     MIIKNGMIIY GDEFTIVRSD VLIEDGVIKE VGKNIRAPAD MVIDASSHLV IPGLINAHTH
     VSMVLLRGLA EDVPLQEWLQ NYIWPREREL KRKDIYWGTL LGLVEMARSG VTTFVDMYFH
     IEEVAKATIE VGLRGFLGYG MVDLENREKL EVEIKETEKF YEYVTKINSP LVNFVLAPHA
     PYTCSLECLK WVSKKANQWN VPVTIHLSET KKEVEEIRKK YGMTPTQLLD EVGLLNEKLI
     AAHGVWLSEE ELRMLSSANA TVVHCPASNM KLGSGVFPLR KALDLGVNVA LGTDGAASNN
     TLDMLREMRL ASLLQKVAHL NPAIVKSEEI LKMATVNPAK ALGLKSGVIK EGYIADLALI
     NLRRPHLLPL NSPTSLLIYS ARGGDVDTLF VNGEIVILDG EFLTVNEEKI LDKFLKVIE