MTAD_ALKHC
ID MTAD_ALKHC Reviewed; 438 AA.
AC Q9KC82;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=5-methylthioadenosine/S-adenosylhomocysteine deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE Short=MTA/SAH deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE EC=3.5.4.28 {ECO:0000255|HAMAP-Rule:MF_01281};
DE EC=3.5.4.31 {ECO:0000255|HAMAP-Rule:MF_01281};
GN Name=mtaD {ECO:0000255|HAMAP-Rule:MF_01281}; OrderedLocusNames=BH1692;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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:0000255|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:0000255|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:0000255|HAMAP-
CC Rule:MF_01281};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01281};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01281};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC MTA/SAH deaminase family. {ECO:0000255|HAMAP-Rule:MF_01281}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB05411.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000004; BAB05411.1; ALT_INIT; Genomic_DNA.
DR PIR; D83861; D83861.
DR RefSeq; WP_041820494.1; NC_002570.2.
DR AlphaFoldDB; Q9KC82; -.
DR SMR; Q9KC82; -.
DR STRING; 272558.10174309; -.
DR EnsemblBacteria; BAB05411; BAB05411; BAB05411.
DR KEGG; bha:BH1692; -.
DR eggNOG; COG0402; Bacteria.
DR HOGENOM; CLU_012358_2_0_9; -.
DR OMA; ALIGKVC; -.
DR OrthoDB; 1592010at2; -.
DR Proteomes; UP000001258; Chromosome.
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 Gene3D; 2.30.40.10; -; 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 Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..438
FT /note="5-methylthioadenosine/S-adenosylhomocysteine
FT deaminase"
FT /id="PRO_0000312446"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
SQ SEQUENCE 438 AA; 48874 MW; E148C0DB981AA472 CRC64;
MGTIVKNVSI VTGQAEAPFI RHGYFKFADG VIVSVAEGTP SPEEIDRVEV IDGKGKWVMP
GMINTHGHLG MSLLRGHSDD LPLQSWLTEK MWPFEGKMDR EAVHHARQLA MAEMIKSGTT
TFLEMYHLYM DDLAEAVVEQ GPRAVLMRSM IGLCSESEQR EKLKEAVTFA TTWNGDGNGR
ITTMMAPHAP YTCPPSFIEM IVDEADRIDL PLHTHMAETQ REVEEHRKTY GVHPLVHFEQ
LGFLKDRHWL LAHCVHLGEE ELDILEQHPS VHVSHNPMSN LKLGSGIANV QSMLERGINI
CLGTDSVASN NHLDLVEEMR IAALLQKGAV LDPTAIPAET AIAMATKNGA KALRLPQVGT
IEAGKRADFI MIDPQCLHLQ PHEHVMSHLV YALKGADVQD VFVEGAPLML NKELKTFDEE
KLQFEANAHY QRICEKLK
