ID A0A140E431_9GAMM Unreviewed; 437 AA.
AC A0A140E431;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=JT25_001425 {ECO:0000313|EMBL:AMK75155.1};
OS Methylomonas denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=1538553 {ECO:0000313|EMBL:AMK75155.1, ECO:0000313|Proteomes:UP000030512};
RN [1] {ECO:0000313|EMBL:AMK75155.1, ECO:0000313|Proteomes:UP000030512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJG1 {ECO:0000313|EMBL:AMK75155.1,
RC ECO:0000313|Proteomes:UP000030512};
RX PubMed=25580993; DOI=10.1111/1462-2920.12772;
RA Kits K.D., Klotz M.G., Stein L.Y.;
RT "Methane oxidation coupled to nitrate reduction under hypoxia by the
RT Gammaproteobacterium Methylomonas denitrificans, sp. nov. type strain
RT FJG1.";
RL Environ. Microbiol. 17:3219-3232(2015).
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 ATZ/TRZ family. {ECO:0000256|ARBA:ARBA00006745}.
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; CP014476; AMK75155.1; -; Genomic_DNA.
DR RefSeq; WP_036272243.1; NZ_CP014476.1.
DR AlphaFoldDB; A0A140E431; -.
DR STRING; 1538553.JT25_001425; -.
DR KEGG; mdn:JT25_001425; -.
DR OrthoDB; 9787621at2; -.
DR Proteomes; UP000030512; 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 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, ECO:0000313|EMBL:AMK75155.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01281};
KW Reference proteome {ECO:0000313|Proteomes:UP000030512};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01281}.
FT DOMAIN 60..408
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
SQ SEQUENCE 437 AA; 47950 MW; EFC756830A49D4C0 CRC64;
MLVDLLIQAR WIIPVEPESA IHEHASLVID DGRIVDLLPT EQAVLQYQAR NVEVLDQHAL
IPGLINCHTH AAMSLLRGIA DDLHLMDWLQ NHIWPAEQKW VSEAFVRDGT DLAIAEMLRC
GTTCFNDMYF FPEIVAQQAI QHGIRANIGL IVFDFPTVWA ENADAYLTKG LALHEQLRHE
TLISTSFAPH APYTVSDGPL RNVITYADEM NLTVHMHLHE TAHEVDEQKA KNGQTPLQRL
HELGLLTPSF IAVHMTQLSS DDIRLYAETG GHIVHCPESN LKLASGFCPV AECLAAGINV
ALGTDGAASN NDLDMLSEMR TAALLGKGVA GDASAVSAVT ALQMATINGA KALGLDAEIG
SLAIGKAADV VAIDLSELET QPLFNPLAQI VYAAGRHQVS DVWVNGKQLL NKRQLKTLNL
EELRQKVNVW RERLESR
//
