COPP_THEAC
ID COPP_THEAC Reviewed; 328 AA.
AC Q9HIY2;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 107.
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=Ta1194;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL445066; CAC12319.1; -; Genomic_DNA.
DR RefSeq; WP_010901601.1; NC_002578.1.
DR AlphaFoldDB; Q9HIY2; -.
DR SMR; Q9HIY2; -.
DR STRING; 273075.Ta1194; -.
DR PRIDE; Q9HIY2; -.
DR EnsemblBacteria; CAC12319; CAC12319; CAC12319.
DR GeneID; 1456690; -.
DR KEGG; tac:Ta1194; -.
DR eggNOG; arCOG01221; Archaea.
DR HOGENOM; CLU_887399_0_0_2; -.
DR OMA; MIPRISH; -.
DR OrthoDB; 89644at2157; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000001024; 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; Reference proteome;
KW Transferase.
FT CHAIN 1..328
FT /note="Bifunctional phosphopantetheine
FT adenylyltransferase/NTP phosphatase"
FT /id="PRO_0000156329"
FT REGION 1..152
FT /note="Phosphopantetheine adenylyltransferase"
FT REGION 153..328
FT /note="Inosine/xanthosine triphosphatase"
SQ SEQUENCE 328 AA; 37722 MW; AE4613FB274502AC CRC64;
MITVVGGTFS KLHKGHKALL NTAIDTGNEV VIGLTSDEYV KKNKVYPAIP YSVRYRTLYN
YMIKRTNKFR IRQIDDRNGN APYEKDYEVI VVSPETYPRS LKINEIRISN GLPPLKIIRV
PYVLAQDLFP ISSTRIINGE IDTNGKRITP LKVGISTRNE AKIQAVEKFV RRLVKNYQIV
KNENYNLKTQ QPFGEETMEL ATQRAMEALK DNDYSVGIES GIIYESFSKK YYDVHYCVVI
DRFGNVTRGM SSGFEIPDHI VDRMKRDRTF SEAYSGYLNV QEIDQSEGII GKISEGKLRR
IDLIEESIRN AFILRLDPDF YDSTYTPP
