ID   COAD_PYRAE              Reviewed;         155 AA.
AC   Q8ZY96;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 100.
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=PAE0887;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00647}.
CC   -!- SIMILARITY: Belongs to the eukaryotic CoaD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00647}.
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DR   EMBL; AE009441; AAL63100.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZY96; -.
DR   SMR; Q8ZY96; -.
DR   STRING; 178306.PAE0887; -.
DR   EnsemblBacteria; AAL63100; AAL63100; PAE0887.
DR   KEGG; pai:PAE0887; -.
DR   PATRIC; fig|178306.9.peg.652; -.
DR   eggNOG; arCOG01223; Archaea.
DR   HOGENOM; CLU_035272_5_0_2; -.
DR   InParanoid; Q8ZY96; -.
DR   OMA; FDTLHSG; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000002439; 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..155
FT                   /note="Phosphopantetheine adenylyltransferase"
FT                   /id="PRO_0000156325"
SQ   SEQUENCE   155 AA;  17478 MW;  C2CA115BB0D97040 CRC64;
     MKYKFRNVVL GGTFDTLHSG HVKLLATATL IGDRILIGLT SDSFASTYKQ YKVRPFSVRL
     ANLRNLMSLI APEREVAYVE IHDPYGPAVF DPRLEAIVAS IETAPRALQI NDERAKRGLR
     PMEVFIISTV RDGYGHTLSS TYIRRVLERP ESKQS