ID A0A1G6LUY0_9BACL Unreviewed; 430 AA.
AC A0A1G6LUY0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN04488112_108138 {ECO:0000313|EMBL:SDC47030.1};
OS Melghirimyces thermohalophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Melghirimyces.
OX NCBI_TaxID=1236220 {ECO:0000313|EMBL:SDC47030.1, ECO:0000313|Proteomes:UP000199387};
RN [1] {ECO:0000313|EMBL:SDC47030.1, ECO:0000313|Proteomes:UP000199387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45514 {ECO:0000313|EMBL:SDC47030.1,
RC ECO:0000313|Proteomes:UP000199387};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FMZA01000008; SDC47030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6LUY0; -.
DR STRING; 1236220.SAMN04488112_108138; -.
DR OrthoDB; 9807210at2; -.
DR Proteomes; UP000199387; 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|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01281};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01281};
KW Reference proteome {ECO:0000313|Proteomes:UP000199387};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01281}.
FT DOMAIN 55..401
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
SQ SEQUENCE 430 AA; 47840 MW; 29BD71B56873F805 CRC64;
MKRLFVNAHI LTMREKDTLL EHAYLVTEDN CITEVGQGDP PVVYDEILDM KGKLLLPGFI
NTHGHAAMTL LRGYADDLPL KTWLEEKMWP IEGRFGPEQV RWGTALAMVE MIRGGTTCFA
DMYDHMDQVG ALVADAGMRA SLCRGVIGLG SQTEREAKRR EAVQFAQQWH REANGRITTM
MAPHAPYTCP PAYIESIVSD AERLHLPIHI HLSETRREVE QNVQDYGKRP VAHLDQLGVF
HRPALVAHAV HVTEDEIQLL AERGVKVSHN PGSNLKLASG IAPVLAMLKK GIRPSLGTDG
AASNNNLDLL EEIRLAALIH KGVGEDPEAI PAETALAMGT RFGAEALFLE EEIGTLEPGK
KADFVTMDIS RAHWQPTHDL LSHVVYSASA ADVQDVYVDG RPLMRNRELL TLDEERIRWE
TIRAFEKVSP
//
