ID   COAD_METJA              Reviewed;         147 AA.
AC   Q58436;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 112.
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=MJ1030;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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; L77117; AAB99034.1; -; Genomic_DNA.
DR   PIR; E64428; E64428.
DR   RefSeq; WP_010870543.1; NC_000909.1.
DR   AlphaFoldDB; Q58436; -.
DR   SMR; Q58436; -.
DR   STRING; 243232.MJ_1030; -.
DR   PRIDE; Q58436; -.
DR   EnsemblBacteria; AAB99034; AAB99034; MJ_1030.
DR   GeneID; 1451927; -.
DR   KEGG; mja:MJ_1030; -.
DR   eggNOG; arCOG01223; Archaea.
DR   HOGENOM; CLU_035272_5_0_2; -.
DR   InParanoid; Q58436; -.
DR   OMA; FDTLHSG; -.
DR   OrthoDB; 93412at2157; -.
DR   PhylomeDB; Q58436; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000000805; 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..147
FT                   /note="Phosphopantetheine adenylyltransferase"
FT                   /id="PRO_0000156320"
SQ   SEQUENCE   147 AA;  16669 MW;  999471C211B1B1C9 CRC64;
     MKVVVGGTFD ILHRGHKELL KFASSLGKLT IGITSDEFAK KYKTHKINDL KTRIENLKKF
     LDSIKADYEI KVINDAYGDA ITEDYDIIVV TQETLKNAEK INKIRESKGL KPLKIVIFKP
     ILAEDGKPIS TTRIRKGEID EEGRIIK