MTAD_CALS4
ID MTAD_CALS4 Reviewed; 433 AA.
AC Q8R9L4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=TTE1593;
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE008691; AAM24797.1; -; Genomic_DNA.
DR RefSeq; WP_011025828.1; NC_003869.1.
DR AlphaFoldDB; Q8R9L4; -.
DR SMR; Q8R9L4; -.
DR STRING; 273068.TTE1593; -.
DR EnsemblBacteria; AAM24797; AAM24797; TTE1593.
DR KEGG; tte:TTE1593; -.
DR eggNOG; COG0402; Bacteria.
DR HOGENOM; CLU_012358_2_1_9; -.
DR OMA; ALIGKVC; -.
DR OrthoDB; 1592010at2; -.
DR Proteomes; UP000000555; 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..433
FT /note="5-methylthioadenosine/S-adenosylhomocysteine
FT deaminase"
FT /id="PRO_0000312464"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 143
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 298
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
SQ SEQUENCE 433 AA; 48350 MW; 53FF2F25463AB8C5 CRC64;
MNLLIKNVNL LSMEEDKVLE GVNVYVEGDT IKHIGELLPD VKVDVVIEGK DKLAMPGLIN
AHTHLGMSLF RNYANDVPLF DWLTKYIWPL EARLTAEDVY WGSLLSMIEM IYSGTTTYCD
MYFFMEEVAK ATEEIGIRGV ISRGIIEEQD AKVNEEKLKD TENLYNAWNG KAEGRIKVMV
GPHAPYTCGP TYLKEILDLA KRLGTGIHIH VSETKREVEE SLEKYGKTPV QHLKDLGIFE
VPTVAAHCVH LTDEDIEVLK EMKVSPVYNP TSNLKLASGF APVEKMLKKG INVALGTDGP
ASNNNLNMFE EIHFAATINK ALNEDALSVP AFEALKMATV SGARALLWER EIGTIEVGKK
ADVILIDLNK PHLHPKNDLI SALAYSVQGS DVDTVIVNGK VIMEKREIKT VDVERVYYEV
EKRAQNLIRG EIS
