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Database: UniProt
Entry: A0A1J5H164_9BACT
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ID   A0A1J5H164_9BACT        Unreviewed;       441 AA.
AC   A0A1J5H164;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   22-FEB-2023, entry version 15.
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   ORFNames=AUK17_02515 {ECO:0000313|EMBL:OIP78228.1};
OS   Parcubacteria group bacterium CG2_30_44_18.
OC   Bacteria.
OX   NCBI_TaxID=1805318 {ECO:0000313|EMBL:OIP78228.1, ECO:0000313|Proteomes:UP000182705};
RN   [1] {ECO:0000313|EMBL:OIP78228.1, ECO:0000313|Proteomes:UP000182705}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG2_30_44_18 {ECO:0000313|EMBL:OIP78228.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
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       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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OIP78228.1}.
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DR   EMBL; MNZG01000050; OIP78228.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J5H164; -.
DR   STRING; 1805318.AUK17_02515; -.
DR   Proteomes; UP000182705; Unassembled WGS sequence.
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   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   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01281};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01281};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01281}.
FT   DOMAIN          58..407
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT   BINDING         215
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT   BINDING         303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
SQ   SEQUENCE   441 AA;  49272 MW;  1C94AB64538326EC CRC64;
     MILIRNATIL TQDSKRQILK NAAICIKDGR ILDIGISHEL EKLYKKRAKK IIDGEGRVVM
     PGLINTHTHL AMTLLRGYAD DMPLKKWWFE KVFPFEGKLK AEDVYWGSLL GGLEMIESGT
     TCFVDGYFFA DAIVMAVEEL GLRANIGIPV LDFKCPEFES PDDALAAAEK ILTKPRGAEL
     IKFSIAPHML QSTSLETYRK CKKLADRYKI ILQTHLAETE AEVEYSRKKY KKTPVRLLVE
     NRILDKNSLV AHVCHLTDDD VVLLAKSRVN VSHCPVSNMK LVSGLMPLKK LLNKGVNIGL
     GTDGACSNNN LDMFEEMKLS ALVHKLAEKD PSAAEAQIIL DMATINAAKA IGEEKNLGSI
     ERGKAADIIL LNFQQPHLLP DYNILSNLVY SARGNDVETA IINGQIVMEN RKIQNVNENK
     ILKIIRERYN AYSSNLILCA L
//
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