NCPP_VIBCH
ID NCPP_VIBCH Reviewed; 183 AA.
AC Q9KU27;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Inosine/xanthosine triphosphatase {ECO:0000255|HAMAP-Rule:MF_00648};
DE Short=ITPase/XTPase {ECO:0000255|HAMAP-Rule:MF_00648};
DE EC=3.6.1.73 {ECO:0000255|HAMAP-Rule:MF_00648};
DE AltName: Full=Non-canonical purine NTP phosphatase {ECO:0000255|HAMAP-Rule:MF_00648};
DE AltName: Full=Non-standard purine NTP phosphatase {ECO:0000255|HAMAP-Rule:MF_00648};
DE AltName: Full=Nucleoside-triphosphate phosphatase {ECO:0000255|HAMAP-Rule:MF_00648};
DE Short=NTPase {ECO:0000255|HAMAP-Rule:MF_00648};
GN OrderedLocusNames=VC_0702;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=16498616; DOI=10.1002/prot.20919;
RA Ni S., Forouhar F., Bussiere D.E., Robinson H., Kennedy M.A.;
RT "Crystal structure of VC0702 at 2.0 A: conserved hypothetical protein from
RT Vibrio cholerae.";
RL Proteins 63:733-741(2006).
CC -!- FUNCTION: Phosphatase that hydrolyzes non-canonical purine nucleotides
CC such as XTP and ITP to their respective diphosphate derivatives.
CC Probably excludes non-canonical purines from DNA/RNA precursor pool,
CC thus preventing their incorporation into DNA/RNA and avoiding
CC chromosomal lesions. {ECO:0000255|HAMAP-Rule:MF_00648}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + XTP = H(+) + phosphate + XDP; Xref=Rhea:RHEA:28406,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:59884, ChEBI:CHEBI:61314; EC=3.6.1.73;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + ITP = H(+) + IDP + phosphate; Xref=Rhea:RHEA:28330,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58280, ChEBI:CHEBI:61402; EC=3.6.1.73;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00648};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00648};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00648};
CC Note=Binds 1 divalent metal cation per subunit; can use either Mg(2+)
CC or Mn(2+). {ECO:0000255|HAMAP-Rule:MF_00648};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00648}.
CC -!- SIMILARITY: Belongs to the YjjX NTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00648, ECO:0000305}.
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DR EMBL; AE003852; AAF93867.1; -; Genomic_DNA.
DR PIR; H82290; H82290.
DR RefSeq; NP_230351.1; NC_002505.1.
DR PDB; 1ZNO; X-ray; 2.00 A; A/B=1-183.
DR PDB; 1ZWY; X-ray; 1.90 A; A/B/C/D=1-183.
DR PDBsum; 1ZNO; -.
DR PDBsum; 1ZWY; -.
DR AlphaFoldDB; Q9KU27; -.
DR SMR; Q9KU27; -.
DR STRING; 243277.VC_0702; -.
DR DNASU; 2615706; -.
DR EnsemblBacteria; AAF93867; AAF93867; VC_0702.
DR KEGG; vch:VC_0702; -.
DR PATRIC; fig|243277.26.peg.672; -.
DR eggNOG; COG1986; Bacteria.
DR HOGENOM; CLU_087417_1_0_6; -.
DR OMA; ADYWVGI; -.
DR BioCyc; VCHO:VC0702-MON; -.
DR EvolutionaryTrace; Q9KU27; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0103023; F:ITPase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; ISS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006772; P:thiamine metabolic process; IBA:GO_Central.
DR Gene3D; 3.90.950.10; -; 1.
DR HAMAP; MF_00648; Non_canon_purine_NTPase_YjjX; 1.
DR InterPro; IPR029001; ITPase-like_fam.
DR InterPro; IPR002786; Non_canon_purine_NTPase.
DR InterPro; IPR026533; NTPase/PRRC1.
DR Pfam; PF01931; NTPase_I-T; 1.
DR SUPFAM; SSF52972; SSF52972; 1.
DR TIGRFAMs; TIGR00258; TIGR00258; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nucleotide metabolism; Nucleotide-binding; Reference proteome.
FT CHAIN 1..183
FT /note="Inosine/xanthosine triphosphatase"
FT /id="PRO_0000156350"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:1ZWY"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:1ZWY"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:1ZWY"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1ZWY"
FT HELIX 57..74
FT /evidence="ECO:0007829|PDB:1ZWY"
FT STRAND 79..89
FT /evidence="ECO:0007829|PDB:1ZWY"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:1ZWY"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:1ZWY"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:1ZWY"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:1ZWY"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:1ZWY"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:1ZWY"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:1ZWY"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:1ZWY"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1ZWY"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:1ZWY"
SQ SEQUENCE 183 AA; 20562 MW; 425531EDD8017C23 CRC64;
MPPIIKRRVM RKIIIASQNP AKVNAVRSAF STVFPDQEWE FIGVSVPSEV ADQPMSDEET
KQGALNRVRN AKQRHPGAEY YVGLEAGIEE NKTFAWMIVE SDQQRGESRS ACLMLPPLVL
ERLRQAKELG DVMDEVFGTE NIKQKGGAIG LLTRHHLTRS TVYHQALILA LIPFINPEHY
PSA
