COPP_THEVO
ID COPP_THEVO Reviewed; 328 AA.
AC Q97BQ0;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Bifunctional phosphopantetheine adenylyltransferase/NTP phosphatase;
DE Includes:
DE RecName: Full=Phosphopantetheine adenylyltransferase;
DE EC=2.7.7.3;
DE AltName: Full=Dephospho-CoA pyrophosphorylase;
DE AltName: Full=Pantetheine-phosphate adenylyltransferase;
DE Short=PPAT;
DE Includes:
DE RecName: Full=Probable inosine/xanthosine triphosphatase {ECO:0000250|UniProtKB:P39411};
DE EC=3.6.1.73 {ECO:0000250|UniProtKB:P39411};
DE AltName: Full=Non-canonical purine NTP phosphatase {ECO:0000250|UniProtKB:P39411};
DE AltName: Full=Nucleoside-triphosphate phosphatase {ECO:0000250|UniProtKB:P39411};
DE Short=NTPase {ECO:0000250|UniProtKB:P39411};
GN Name=coaD; OrderedLocusNames=TV0405; ORFNames=TVG0394586;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
CC -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-
CC phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
CC {ECO:0000250}.
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:0000250|UniProtKB:P39411}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA +
CC diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328,
CC ChEBI:CHEBI:61723; EC=2.7.7.3;
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:0000250|UniProtKB:P39411};
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:0000250|UniProtKB:P39411};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P39411};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P39411};
CC Note=Binds 1 divalent metal cation per subunit; can use either Mg(2+)
CC or Mn(2+). {ECO:0000250|UniProtKB:P39411};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the eukaryotic CoaD
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the YjjX NTPase
CC family. {ECO:0000305}.
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DR EMBL; BA000011; BAB59547.1; -; Genomic_DNA.
DR RefSeq; WP_010916661.1; NC_002689.2.
DR AlphaFoldDB; Q97BQ0; -.
DR SMR; Q97BQ0; -.
DR STRING; 273116.14324620; -.
DR DNASU; 1440919; -.
DR EnsemblBacteria; BAB59547; BAB59547; BAB59547.
DR GeneID; 1440919; -.
DR KEGG; tvo:TVG0394586; -.
DR eggNOG; arCOG01221; Archaea.
DR HOGENOM; CLU_887399_0_0_2; -.
DR OMA; MIPRISH; -.
DR OrthoDB; 89644at2157; -.
DR PhylomeDB; Q97BQ0; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000001017; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0004595; F:pantetheine-phosphate adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.90.950.10; -; 1.
DR HAMAP; MF_00648; Non_canon_purine_NTPase_YjjX; 1.
DR HAMAP; MF_00647; PPAT_arch; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR029001; ITPase-like_fam.
DR InterPro; IPR002786; Non_canon_purine_NTPase.
DR InterPro; IPR026533; NTPase/PRRC1.
DR InterPro; IPR023540; PPAT_arch.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_like; 1.
DR Pfam; PF01931; NTPase_I-T; 1.
DR SUPFAM; SSF52972; SSF52972; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Multifunctional enzyme; Nucleotide metabolism;
KW Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT CHAIN 1..328
FT /note="Bifunctional phosphopantetheine
FT adenylyltransferase/NTP phosphatase"
FT /id="PRO_0000156330"
FT REGION 1..152
FT /note="Phosphopantetheine adenylyltransferase"
FT REGION 153..328
FT /note="Inosine/xanthosine triphosphatase"
SQ SEQUENCE 328 AA; 37665 MW; 48B3048F1EAF22E6 CRC64;
MITVVGGTFS KLHKGHKALL EKAIETGNEI VIGLTSDEYV KRNKVYPAIP YKERYRNLYN
YMVKKTNKFR IRPIDDRNGN APYERDYEII VVSPETYQRS LKINEIRIQN GLPPLKIIRV
PYVLAEDLFP ISSTRIINGE IDGNGRRLKP VKVAIATNNS AKLKATNDFF HKLMKNFDVI
QNTDYKLETQ QPFGEVTMNM ATKRAMQSLG DNDYAIGIES GIVYERFSRK YFDFHYCVVI
DRFGNVTRGS SSGFEVPDRI IDLIKRDMSF SQAYGKVIDT NGIDDSTGIV GKISNGRVRR
YDLIMECIRN AFIPRFDPDF YDTTYTPP
