ID X0QMJ3_9GAMM Unreviewed; 378 AA.
AC X0QMJ3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=8-oxo-dGTP diphosphatase {ECO:0000256|ARBA:ARBA00040794};
DE EC=3.6.1.55 {ECO:0000256|ARBA:ARBA00038905};
DE AltName: Full=7,8-dihydro-8-oxoguanine-triphosphatase {ECO:0000256|ARBA:ARBA00042798};
DE AltName: Full=Mutator protein MutT {ECO:0000256|ARBA:ARBA00041979};
DE AltName: Full=dGTP pyrophosphohydrolase {ECO:0000256|ARBA:ARBA00041592};
GN ORFNames=JCM18900_11290 {ECO:0000313|EMBL:GAF52757.1};
OS Psychrobacter sp. JCM 18900.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1298608 {ECO:0000313|EMBL:GAF52757.1, ECO:0000313|Proteomes:UP000019500};
RN [1] {ECO:0000313|EMBL:GAF52757.1, ECO:0000313|Proteomes:UP000019500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 18900 {ECO:0000313|EMBL:GAF52757.1,
RC ECO:0000313|Proteomes:UP000019500};
RA Kudo T., Kidera A., Kida M., Kawauchi A., Shimizu R., Nakahara T.,
RA Zhang X., Yamada A., Amano M., Hamada Y., Taniyama S., Arakawa O.,
RA Yoshida A., Oshima K., Suda W., Kuwahara H., Nogi Y., Kitamura K., Yuki M.,
RA Iida T., Moriya S., Inoue T., Hongo Y., Hattori M., Ohkuma M.;
RT "Draft Genome Sequences of Psychrobacter Strains JCM 18900, JCM 18901, JCM
RT 18902, and JCM 18903, Isolated Preferentially from Frozen Aquatic
RT Organisms.";
RL Genome Announc. 2:e00280-14(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-oxo-GTP + H2O = 8-oxo-GMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:67616, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:143553, ChEBI:CHEBI:145694;
CC Evidence={ECO:0000256|ARBA:ARBA00036904};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:31575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:63224, ChEBI:CHEBI:77896; EC=3.6.1.55;
CC Evidence={ECO:0000256|ARBA:ARBA00035861};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC {ECO:0000256|ARBA:ARBA00005582}.
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:GAF52757.1}.
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DR EMBL; BAWG01000004; GAF52757.1; -; Genomic_DNA.
DR AlphaFoldDB; X0QMJ3; -.
DR eggNOG; COG0352; Bacteria.
DR eggNOG; COG0494; Bacteria.
DR Proteomes; UP000019500; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd03425; MutT_pyrophosphohydrolase; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR047127; MutT-like.
DR InterPro; IPR029119; MutY_C.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR036206; ThiamineP_synth_sf.
DR InterPro; IPR022998; ThiamineP_synth_TenI.
DR PANTHER; PTHR47707; 8-OXO-DGTP DIPHOSPHATASE; 1.
DR PANTHER; PTHR47707:SF1; NUDIX HYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF14815; NUDIX_4; 1.
DR Pfam; PF02581; TMP-TENI; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR SUPFAM; SSF51391; Thiamin phosphate synthase; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}.
FT DOMAIN 26..163
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 378 AA; 41499 MW; BA7B6E16F3F9EA99 CRC64;
MLNGSNQQSE TKPESKTNSK AQTDKPSIVN VAVAVIHYKD QYLLGFRDST QHQGNRYEFV
GGKIEANESA AQALIREVAE ETGILLEDNT IVKLGRLHHD YGDKQVSLQV YKIELIAEQY
EQHKHREQGL EGQALTWVSK SQLLAGAYHL PAANKTILEW LKLPSKIAIT YPLAHFGTHT
DAAATWLQHH QEKLASESWV YIRLKDANSK HLAEQLITAR PDILAILPNG NEQLLDVEGS
LTANETEMGQ RIVAEHLTQT TLMQCFDKDG NPTALSQSLS KDDPLIVSCH DIASITAANQ
LASMRIQNAL PPVIGTFVSP VLATQTHPDD TPLGWEAWSA LANLADMPVI GLGGLEPAML
NQALQYGGIS VAGIRQFI
//
