ID A0A160T3W7_9CHLR Unreviewed; 670 AA.
AC A0A160T3W7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 2.
DT 27-MAR-2024, entry version 26.
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 ECO:0000313|EMBL:CUS04514.2};
GN ORFNames=CFX0092_A2636 {ECO:0000313|EMBL:CUS04514.2};
OS Candidatus Promineifilum breve.
OC Bacteria; Chloroflexota; Ardenticatenia; Candidatus Promineifilales;
OC Candidatus Promineifilaceae; Candidatus Promineifilum.
OX NCBI_TaxID=1806508 {ECO:0000313|EMBL:CUS04514.2, ECO:0000313|Proteomes:UP000215027};
RN [1] {ECO:0000313|EMBL:CUS04514.2, ECO:0000313|Proteomes:UP000215027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cfx-K {ECO:0000313|EMBL:CUS04514.2,
RC ECO:0000313|Proteomes:UP000215027};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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: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}.
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DR EMBL; LN890655; CUS04514.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A160T3W7; -.
DR KEGG; pbf:CFX0092_A2636; -.
DR OrthoDB; 9807210at2; -.
DR Proteomes; UP000215027; Chromosome i.
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; 2.40.320.10; Hypothetical Protein Pfu-838710-001; 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; IPR033469; CYTH-like_dom_sf.
DR InterPro; IPR023577; CYTH_domain.
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; SSF55154; CYTH-like phosphatases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS51707; CYTH; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01281, ECO:0000313|EMBL:CUS04514.2};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01281};
KW Reference proteome {ECO:0000313|Proteomes:UP000215027};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01281}.
FT DOMAIN 466..660
FT /note="CYTH"
FT /evidence="ECO:0000259|PROSITE:PS51707"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
SQ SEQUENCE 670 AA; 74527 MW; FE12F8B57A7D81B7 CRC64;
MPEQVDILLR GGTVVTMNGK YEVFEDGAVA IRGDAIIAVG PTDEITRAYA ATETVECADT
VIMPGLVNAH THIPMTLMRG LNDDLRLDVW LGYLMPVERE FVTPDFVKLG ARVACAEMIR
SGVTTFADMF YYEEAIAEQV AEIGMRALLG QTILVFPAPD AETFEDALLL CRRFIEHWNG
HPLIQPAVAP HAWYTATPEL LLACADLARA FDVPLHTHVS ETRLEADNSV NQNHMSVVTW
LEQHGILDTK LLAAHCVHID EEDMFSLRRA GAGVAHCPSS NLKLASGIAP IPQMLKLGLK
VGVGTDGPAS NNDLDMVEEM RLASFIAKIA AQNPTALPAR QTLEIATIGG ARAVHMGAIT
GSLEPGKRAD IAVLDMSGIH NQPHFHNHPD AVYSRIVYAG KSADVSHVIC NGRWLMRDRA
LLTVDEAAAR TDALRVAADI DAFVMERESS PYNKLVLLSG VQRQESFEVQ VKVPMADDTA
LQMLLESSAI TTTRYAHYRQ YDHYFLFDQG DPDANRLRYR EDEFINEAGD VTQVRARLTL
IGEGGREEFP NAVMMSRSRW LAAADRSLRF YQEYFAPARE LRVHKDRHRW HILYKATDFA
INLDKVLEPE LPGYFLEIKS RTWSRSDAQR KAGLIAELVA QCGLDFDRAE RREYAEIATS
ANYEKDTTPG
//
