ID   COAD_THEKO              Reviewed;         165 AA.
AC   Q5JHE8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00647, ECO:0000303|PubMed:31337720};
DE            EC=2.7.7.3 {ECO:0000255|HAMAP-Rule:MF_00647};
DE   AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00647};
DE   AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00647};
DE            Short=PPAT {ECO:0000255|HAMAP-Rule:MF_00647, ECO:0000303|PubMed:31337720};
GN   Name=coaD {ECO:0000255|HAMAP-Rule:MF_00647}; OrderedLocusNames=TK2128;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
RN   [2]
RP   PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=31337720; DOI=10.1128/mbio.01146-19;
RA   Shimosaka T., Makarova K.S., Koonin E.V., Atomi H.;
RT   "Identification of dephospho-coenzyme A (dephospho-CoA) kinase in
RT   Thermococcus kodakarensis and elucidation of the entire CoA biosynthesis
RT   pathway in archaea.";
RL   MBio 10:E01146-E01146(2019).
CC   -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-
CC       phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_00647}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00647};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00647, ECO:0000269|PubMed:31337720}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00647}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the gene results in CoA auxotrophy.
CC       {ECO:0000269|PubMed:31337720}.
CC   -!- SIMILARITY: Belongs to the eukaryotic CoaD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00647}.
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DR   EMBL; AP006878; BAD86317.1; -; Genomic_DNA.
DR   RefSeq; WP_011251078.1; NC_006624.1.
DR   AlphaFoldDB; Q5JHE8; -.
DR   SMR; Q5JHE8; -.
DR   STRING; 69014.TK2128; -.
DR   EnsemblBacteria; BAD86317; BAD86317; TK2128.
DR   GeneID; 3234848; -.
DR   KEGG; tko:TK2128; -.
DR   PATRIC; fig|69014.16.peg.2084; -.
DR   eggNOG; arCOG01223; Archaea.
DR   HOGENOM; CLU_035272_5_0_2; -.
DR   InParanoid; Q5JHE8; -.
DR   OMA; FDTLHSG; -.
DR   OrthoDB; 93412at2157; -.
DR   PhylomeDB; Q5JHE8; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004140; F:dephospho-CoA kinase activity; IBA:GO_Central.
DR   GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00647; PPAT_arch; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR023540; PPAT_arch.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..165
FT                   /note="Phosphopantetheine adenylyltransferase"
FT                   /id="PRO_0000156328"
SQ   SEQUENCE   165 AA;  18777 MW;  6F245BE6FE845B95 CRC64;
     MRKKYRKVVV GGTFDRLHLG HKALLRKAFE VGKIVYIGLT SDEMVRNKPY AERILPYEHR
     LKDLLKFIEV NGYTNYRIIK IHTAIGFADS MKSLEAIVVS EETYKGALIV NRAREEKGLK
     PLDIVTIPII KSYLGDKISS SLIRAGLIDP FGRPLHWKGN SPKDV