ID   MTAD2_SYNAS             Reviewed;         445 AA.
AC   Q2LUH4;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=5-methylthioadenosine/S-adenosylhomocysteine deaminase 2 {ECO:0000255|HAMAP-Rule:MF_01281};
DE            Short=MTA/SAH deaminase 2 {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=mtaD2 {ECO:0000255|HAMAP-Rule:MF_01281};
GN   OrderedLocusNames=SYNAS_18510; ORFNames=SYN_01991;
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC   Syntrophus.
OX   NCBI_TaxID=56780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB;
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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; CP000252; ABC77730.1; -; Genomic_DNA.
DR   RefSeq; WP_011417752.1; NC_007759.1.
DR   AlphaFoldDB; Q2LUH4; -.
DR   SMR; Q2LUH4; -.
DR   STRING; 56780.SYN_01991; -.
DR   EnsemblBacteria; ABC77730; ABC77730; SYN_01991.
DR   KEGG; sat:SYN_01991; -.
DR   eggNOG; COG0402; Bacteria.
DR   HOGENOM; CLU_012358_2_1_7; -.
DR   OMA; CYEVSDR; -.
DR   OrthoDB; 1592010at2; -.
DR   Proteomes; UP000001933; 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..445
FT                   /note="5-methylthioadenosine/S-adenosylhomocysteine
FT                   deaminase 2"
FT                   /id="PRO_0000312463"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         222
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         310
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         310
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
SQ   SEQUENCE   445 AA;  49005 MW;  5764CEE2B4861158 CRC64;
     MAKTELDLLI RGSVLLTMRE EEAVIENPVV GIRNGKIVLI MQNDLFTEEE YTARKVLDRS
     NTLIMPGLVN THTHLAMSCF RGLADDLPLM AWLHEYIFPA EARHVNPEMV YAGSLLAMAE
     MILSGTTTFC DGYFFVDQVA RAAKDAGMRA VVCQGFIDFP TPDTSDPSRQ METAERFIGT
     WKDASPLIQP ALFCHSPYTC SPETLVRIKE AARREKILYV LHLSETREEV SLIQDCYGKR
     PALHLHNLDV LDPDTLAVHC VWLDEEEQGV LADCGVRVSH TPQSNMKLAA GIAPVPAMQA
     MGISVSLGTD GSASNNDLDL FREMDSTAKI HKVATGNPAV MDAARVVRMA TSEGAGALGL
     QDRIGSLEVG KAADLIILDL NQPHLTPMYH PFSHLVYAAS GADVLTTVID GNVVMENRKI
     LSFDLEAIMR EVEKIAEKIR KSCRK