MTAD_DESAP
ID MTAD_DESAP Reviewed; 430 AA.
AC B1I2P4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Daud_0651;
OS Desulforudis audaxviator (strain MP104C).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Candidatus Desulforudis.
OX NCBI_TaxID=477974;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP104C;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL Submitted (OCT-2007) 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; CP000860; ACA59185.1; -; Genomic_DNA.
DR RefSeq; WP_012301773.1; NC_010424.1.
DR AlphaFoldDB; B1I2P4; -.
DR SMR; B1I2P4; -.
DR STRING; 477974.Daud_0651; -.
DR EnsemblBacteria; ACA59185; ACA59185; Daud_0651.
DR KEGG; dau:Daud_0651; -.
DR eggNOG; COG0402; Bacteria.
DR HOGENOM; CLU_012358_2_1_9; -.
DR OMA; ALIGKVC; -.
DR OrthoDB; 1592010at2; -.
DR Proteomes; UP000008544; 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..430
FT /note="5-methylthioadenosine/S-adenosylhomocysteine
FT deaminase"
FT /id="PRO_1000214205"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
SQ SEQUENCE 430 AA; 46329 MW; F38EE462215C47A0 CRC64;
MRLLIRNAYV IPVAGSDFTG DVAVEEGRIV FAGPTGAVPG TFEADETIDA TGMVATPGLV
NCHTHAAMTL FRGYADDLPL MEWLTRKIWP VENLLTGDDI YWGSLLAGLE MLKSGTTTFA
DQYFEMDRVA QAVEEIGLRA SLCRGLIGVS EHAEKALAEG CEFVRRWHGA AAGRISAMLG
PHAPYTCPPA YLKKVVAASE ELDVGLHIHL SETRTEIEQI KAEYGCSPIA LMEETGLFHR
PVLAAHCVHL SEADIKILAR RGVGVAHNPQ SNMKLASGIA PVVRMLAAGV RVGIGTDGAA
SNNDLNMVEE MRTAALLQKV AQGDPTVLPA GLVLEMATAG GARVLGLEDR IGTLEVGKRA
DVVLWRVNQP HLCPAHNYQA HLVYSAGRAD VDTVIVDGHV VMRGRRVLTV DEETVLRQAE
RTARRLIESV
