ID U3ABV0_9EURY Unreviewed; 429 AA.
AC U3ABV0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=MBEHAL_1018 {ECO:0000313|EMBL:GAD52258.1};
OS Halarchaeum acidiphilum MH1-52-1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae.
OX NCBI_TaxID=1261545 {ECO:0000313|EMBL:GAD52258.1, ECO:0000313|Proteomes:UP000016986};
RN [1] {ECO:0000313|EMBL:GAD52258.1, ECO:0000313|Proteomes:UP000016986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16109 {ECO:0000313|EMBL:GAD52258.1,
RC ECO:0000313|Proteomes:UP000016986};
RA Shimane Y., Minegishi H., Nishi S., Echigo A., Shuto A., Konishi M.,
RA Ito T., Ohkuma M., Ohta Y., Nagano Y., Tsubouchi T., Mori K., Usui K.,
RA Kamekura M., Usami R., Takaki Y., Hatada Y.;
RT "Whole genome sequencing of Halarchaeum acidiphilum strain MH1-52-1.";
RL Submitted (SEP-2013) 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}.
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:GAD52258.1}.
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DR EMBL; BATA01000018; GAD52258.1; -; Genomic_DNA.
DR RefSeq; WP_021779982.1; NZ_BATA01000018.1.
DR AlphaFoldDB; U3ABV0; -.
DR eggNOG; arCOG00695; Archaea.
DR OrthoDB; 372084at2157; -.
DR Proteomes; UP000016986; 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; 2.
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 51..398
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
SQ SEQUENCE 429 AA; 45419 MW; 730C3E58A0CD5E6C CRC64;
MATLRIAGGR VLHPDLSVTE GDVLVDDESG EIVAVGDTGD GDETLDAAGC LVMPGLVNAH
CHAAMTLLRG YADDKPLETW LREDVWPVEA ELTDDDIRAG TELALVELLK SGTTAFADMY
FSMPEVAEAV ADAGLRARLG HGVVGVGKDE DDARADHEES LAFAREYDGY ADGRVQTMYT
PHSLTTVDEA LLREYVPAAR EAGVPLHFHA NETRDEVDPI VDERGERPLE YADDVGMLGE
SDFVAHGVHS DAAEIALIAE RGTAVVHCPA SNMKLASGAA PIPAYRREGV TVALGTDGAA
SNNDLDLFDE MRDAAMLGKH AANDASAVPA EAVVEMATAG GADALGFDAG RIAAGKKADL
AVVDFEAAHL TPTHDAVSNL AYATRGSDVK HTVCDGDVLV RDREVLTLDE DAVRERATER
ARDLVARAE
//
