ID   COAD_PYRAB              Reviewed;         157 AA.
AC   Q9UYT0; G8ZHN5;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 3.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00647};
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};
GN   Name=coaD {ECO:0000255|HAMAP-Rule:MF_00647}; OrderedLocusNames=PYRAB14270;
GN   ORFNames=PAB0944;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=12756245; DOI=10.1074/jbc.m301891200;
RA   Armengaud J., Fernandez B., Chaumont V., Rollin-Genetet F., Finet S.,
RA   Marchetti C., Myllykallio H., Vidaud C., Pellequer J.-L., Gribaldo S.,
RA   Forterre P., Gans P.;
RT   "Identification, purification, and characterization of an eukaryotic-like
RT   phosphopantetheine adenylyltransferase (coenzyme A biosynthetic pathway) in
RT   the hyperthermophilic archaeon Pyrococcus abyssi.";
RL   J. Biol. Chem. 278:31078-31087(2003).
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}.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00647}.
CC   -!- SIMILARITY: Belongs to the eukaryotic CoaD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00647, ECO:0000305}.
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DR   EMBL; AJ248287; CAB50332.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70872.1; -; Genomic_DNA.
DR   PIR; G75054; G75054.
DR   AlphaFoldDB; Q9UYT0; -.
DR   SMR; Q9UYT0; -.
DR   STRING; 272844.PAB0944; -.
DR   EnsemblBacteria; CAB50332; CAB50332; PAB0944.
DR   KEGG; pab:PAB0944; -.
DR   PATRIC; fig|272844.11.peg.1517; -.
DR   eggNOG; arCOG01223; Archaea.
DR   HOGENOM; CLU_035272_5_0_2; -.
DR   BioCyc; MetaCyc:MON-21897; -.
DR   BRENDA; 2.7.7.3; 5242.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   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   1: Evidence at protein level;
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Nucleotide-binding;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..157
FT                   /note="Phosphopantetheine adenylyltransferase"
FT                   /id="PRO_0000156324"
SQ   SEQUENCE   157 AA;  17965 MW;  D89BE90EFEC59F29 CRC64;
     MMKFKKVVVG GTFDRLHLGH KALLRKAFEV GKIVYIGLTS DDMVKNKPYA EKILPYERRL
     KDLIEFLEVN NFRRYRIIKI NNAIGFTTRI RSLEAIVVSE ETYKGALLVN RAREEVGLRP
     LEIIVIPIIK SKLGDKISSS LIRAGLIDPF GNPIKRE