ID Q7NZ90_CHRVO Unreviewed; 439 AA.
AC Q7NZ90;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=5-methylthioadenosine/S-adenosylhomocysteine deaminase {ECO:0000256|HAMAP-Rule:MF_01281};
DE Short=MTA/SAH deaminase {ECO:0000256|HAMAP-Rule:MF_01281};
DE EC=3.5.4.28 {ECO:0000256|HAMAP-Rule:MF_01281};
DE EC=3.5.4.31 {ECO:0000256|HAMAP-Rule:MF_01281};
GN Name=mtaD {ECO:0000256|HAMAP-Rule:MF_01281};
GN OrderedLocusNames=CV_1032 {ECO:0000313|EMBL:AAQ58707.1};
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365 {ECO:0000313|EMBL:AAQ58707.1, ECO:0000313|Proteomes:UP000001424};
RN [1] {ECO:0000313|EMBL:AAQ58707.1, ECO:0000313|Proteomes:UP000001424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 /
RC NCTC 9757 {ECO:0000313|Proteomes:UP000001424};
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Almeida F.C., de Almeida L.G.P.,
RA de Almeida R., Goncalves J.A.A., Andrade E.M., Antonio R.V., Araripe J.,
RA de Araujo M.F.F., Filho S.A., Azevedo V., Batista A.J., Bataus L.A.M.,
RA Batista J.S., Belo A., vander Berg C., Blamey J., Bogo M., Bonato S.,
RA Bordignon J., Brito C.A., Brocchi M., Burity H.A., Camargo A.A.,
RA Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B.,
RA Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Pasa T.B.C., Duran N.,
RA Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S.,
RA Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A.,
RA Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Guimaraes C.T., Hanna E.S., Hungria M.,
RA Jardim S.N., Laurino J., Leoi L.C.T., Fassarella L., Lima A.,
RA Loureiro M.F., Lyra M.C.P., Macedo M., Madeira H.M.F., Manfio G.P.,
RA Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B.,
RA Meissner R.D.V., Menck C.F.M., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.J.D., Perreira J.O., Perreira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Neto C.E.R., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., dos Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
RN [2] {ECO:0007829|PDB:4F0R}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC.
RA Kim J., Vetting M.W., Sauder J.M., Burley S.K., Raushel F.M., Bonanno J.B.,
RA Almo S.C.;
RT "Crystal structure of an adenosine deaminase homolog from Chromobacterium
RT violaceum (target NYSGRC-019589) bound Zn and 5'-Methylthioadenosine
RT (unproductive complex).";
RL Submitted (MAY-2012) to the PDB data bank.
RN [3] {ECO:0007829|PDB:4F0S}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH INOSINE.
RA Kim J., Vetting M.W., Sauder J.M., Burley S.K., Raushel F.M., Bonanno J.B.,
RA Almo S.C.;
RT "Crystal structure of an adenosine deaminase homolog from Chromobacterium
RT violaceum (target NYSGRC-019589) with bound inosine.";
RL Submitted (MAY-2012) to the PDB data bank.
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:0000256|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:0000256|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:0000256|HAMAP-
CC Rule:MF_01281};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01281};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01281};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ATZ/TRZ family. {ECO:0000256|ARBA:ARBA00006745}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC MTA/SAH deaminase family. {ECO:0000256|HAMAP-Rule:MF_01281}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01281}.
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DR EMBL; AE016825; AAQ58707.1; -; Genomic_DNA.
DR RefSeq; WP_011134587.1; NC_005085.1.
DR PDB; 4F0R; X-ray; 1.80 A; A=1-439.
DR PDB; 4F0S; X-ray; 1.85 A; A=1-439.
DR PDBsum; 4F0R; -.
DR PDBsum; 4F0S; -.
DR AlphaFoldDB; Q7NZ90; -.
DR SMR; Q7NZ90; -.
DR STRING; 243365.CV_1032; -.
DR KEGG; cvi:CV_1032; -.
DR eggNOG; COG0402; Bacteria.
DR HOGENOM; CLU_012358_2_1_4; -.
DR OrthoDB; 9807210at2; -.
DR Proteomes; UP000001424; Chromosome.
DR GO; GO:0090614; F:5'-methylthioadenosine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004000; F:adenosine deaminase activity; IDA:CACAO.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050270; F:S-adenosylhomocysteine deaminase activity; IEA:UniProtKB-UniRule.
DR CDD; cd01298; ATZ_TRZ_like; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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 PANTHER; PTHR43794:SF11; AMIDOHYDRO-REL DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43794; AMINOHYDROLASE SSNA-RELATED; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4F0R, ECO:0007829|PDB:4F0S};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01281, ECO:0000313|EMBL:AAQ58707.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01281, ECO:0007829|PDB:4F0R};
KW Reference proteome {ECO:0000313|Proteomes:UP000001424};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01281, ECO:0007829|PDB:4F0R}.
FT DOMAIN 61..410
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281,
FT ECO:0007829|PDB:4F0R"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281,
FT ECO:0007829|PDB:4F0R"
FT BINDING 96
FT /ligand="inosine"
FT /ligand_id="ChEBI:CHEBI:17596"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4F0S"
FT BINDING 99
FT /ligand="inosine"
FT /ligand_id="ChEBI:CHEBI:17596"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4F0S"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 192
FT /ligand="inosine"
FT /ligand_id="ChEBI:CHEBI:17596"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4F0S"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281,
FT ECO:0007829|PDB:4F0R"
FT BINDING 219
FT /ligand="inosine"
FT /ligand_id="ChEBI:CHEBI:17596"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4F0S"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 256
FT /ligand="inosine"
FT /ligand_id="ChEBI:CHEBI:17596"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4F0S"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281,
FT ECO:0007829|PDB:4F0R"
FT BINDING 307
FT /ligand="inosine"
FT /ligand_id="ChEBI:CHEBI:17596"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4F0S"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 353
FT /ligand="inosine"
FT /ligand_id="ChEBI:CHEBI:17596"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4F0S"
FT BINDING 356
FT /ligand="inosine"
FT /ligand_id="ChEBI:CHEBI:17596"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4F0S"
FT BINDING 358
FT /ligand="inosine"
FT /ligand_id="ChEBI:CHEBI:17596"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4F0S"
SQ SEQUENCE 439 AA; 47381 MW; 9A140112B8566188 CRC64;
MPQSRYEKII SARWIITVET DGEVLENHAI AIRDGKIAAI IPAADAAGLE ADERLELPDH
VLMPGLINLH GHSAMSLLRG LADDKALMDW LTNYIWPTEG KHVHDDFVFD GSLLAMGEMI
RGGTTTINDM YFYNAAVARA GLASGMRTFV GCSILEFPTN YASNADDYIA KGMAERSQFL
GEDLLTFTLA PHAPYTVSDD TFRKVVTLAE QEDMLIHCHI HETADEVNNS VKEHGQRPLA
RLQRLGLLSP RLVAAHMVHL NDAEVELAAR HGLSTAHNPA SNMKLASGIS PVSKLMDAGV
AVGIGTDGAA SNNKLDMLAE TRLAALLAKV GTLDPTSVPA AAAIRMATLN GARALGIADK
VGSVKVGKQA DLIALDLAQL ETAPAFDPIS HVVYAAGREQ VSHVWVKGRA LMRERKLTTL
DESDLKARAG DWRNRILAK
//
