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
//