DGTP_SALAR
ID DGTP_SALAR Reviewed; 505 AA.
AC A9MPK1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00030};
DE Short=dGTP triphosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00030};
DE Short=dGTPase {ECO:0000255|HAMAP-Rule:MF_00030};
DE EC=3.1.5.1 {ECO:0000255|HAMAP-Rule:MF_00030};
GN Name=dgt {ECO:0000255|HAMAP-Rule:MF_00030}; OrderedLocusNames=SARI_02796;
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: dGTPase preferentially hydrolyzes dGTP over the other
CC canonical NTPs. {ECO:0000255|HAMAP-Rule:MF_00030}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dGTP + H2O = 2'-deoxyguanosine + H(+) + triphosphate;
CC Xref=Rhea:RHEA:15193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17172, ChEBI:CHEBI:18036, ChEBI:CHEBI:61429; EC=3.1.5.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00030};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00030};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00030}.
CC -!- SIMILARITY: Belongs to the dGTPase family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00030}.
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DR EMBL; CP000880; ABX22644.1; -; Genomic_DNA.
DR RefSeq; WP_000146442.1; NC_010067.1.
DR AlphaFoldDB; A9MPK1; -.
DR SMR; A9MPK1; -.
DR STRING; 41514.SARI_02796; -.
DR PRIDE; A9MPK1; -.
DR EnsemblBacteria; ABX22644; ABX22644; SARI_02796.
DR KEGG; ses:SARI_02796; -.
DR HOGENOM; CLU_028163_2_1_6; -.
DR OMA; ICYTIID; -.
DR OrthoDB; 370035at2; -.
DR Proteomes; UP000002084; Chromosome.
DR GO; GO:0008832; F:dGTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006203; P:dGTP catabolic process; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.3410.10; -; 1.
DR HAMAP; MF_00030; dGTPase_type1; 1.
DR InterPro; IPR023293; dGTP_triP_hydro_central_sf.
DR InterPro; IPR006261; dNTPase.
DR InterPro; IPR020779; dNTPase_1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR026875; PHydrolase_assoc_dom.
DR PANTHER; PTHR11373:SF32; PTHR11373:SF32; 1.
DR Pfam; PF01966; HD; 1.
DR Pfam; PF13286; HD_assoc; 1.
DR SMART; SM00471; HDc; 1.
DR TIGRFAMs; TIGR01353; dGTP_triPase; 1.
DR PROSITE; PS51831; HD; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Reference proteome.
FT CHAIN 1..505
FT /note="Deoxyguanosinetriphosphate triphosphohydrolase"
FT /id="PRO_1000074406"
FT DOMAIN 66..273
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 505 AA; 59392 MW; B0827D857B87E700 CRC64;
MASIDFRNKI NWHRRYRSPQ GVKTEHEILR IFESDRGRII NSPAIRRLQQ KTQVFPLERN
AAVRTRLTHS MEVQQVGRYI AKEILSRLKA QNLLEEYGLD ALTGPFESIV EMACLMHDIG
NPPFGHFGEA AINDWFRQRL YPEDAESQPL THDRCVVSSL RLQEGEESLN DIRRKVRQDI
CYFEGNAQGI RLVHTLMRMN LTWAQVGGIL KYTRPAWWRG PVPDSHRYLM KKPGYYLSEE
KYIARLRKEL QLAPYSRFPL TWIMEAADDI SYCVADLEDA VEKRIFSVEQ LYHHLYHAWG
HHEKDSLFEL VVGNAWEKSR ANTLSRSTEE QFFMYLRVNT LNKLVPYAAQ RFIDNLPQIF
AGTFNQALLE DASGFSRLLE LYKNVAVEHV FSHPDVEQLE LQGYRVISGL LDIYQPLLSM
SLNDFSELVE KERLKRFPIE SRLFQKLSTR HRLAYVEVVS KLPMDSAEYP VLEYYYRCRL
VQDYISGMTD LYAWDEYRRL MAVEQ