COAD_ARCFU
ID COAD_ARCFU Reviewed; 148 AA.
AC O28077;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, 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=AF_2206;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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}.
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; AE000782; AAB89047.1; -; Genomic_DNA.
DR PIR; F69525; F69525.
DR RefSeq; WP_010879695.1; NC_000917.1.
DR PDB; 3DO8; X-ray; 1.60 A; A/B=1-148.
DR PDBsum; 3DO8; -.
DR AlphaFoldDB; O28077; -.
DR SMR; O28077; -.
DR STRING; 224325.AF_2206; -.
DR DNASU; 1485435; -.
DR EnsemblBacteria; AAB89047; AAB89047; AF_2206.
DR GeneID; 24795955; -.
DR KEGG; afu:AF_2206; -.
DR eggNOG; arCOG01223; Archaea.
DR HOGENOM; CLU_035272_5_0_2; -.
DR OMA; FDTLHSG; -.
DR OrthoDB; 93412at2157; -.
DR PhylomeDB; O28077; -.
DR UniPathway; UPA00241; -.
DR EvolutionaryTrace; O28077; -.
DR Proteomes; UP000002199; 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 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..148
FT /note="Phosphopantetheine adenylyltransferase"
FT /id="PRO_0000156318"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:3DO8"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:3DO8"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:3DO8"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:3DO8"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:3DO8"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:3DO8"
FT TURN 78..84
FT /evidence="ECO:0007829|PDB:3DO8"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:3DO8"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:3DO8"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:3DO8"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:3DO8"
SQ SEQUENCE 148 AA; 16883 MW; 27AD2A950588D9B5 CRC64;
MKVALGGTFE PLHEGHKKLI DVAIKLGGRD ITIGVTSDRM ARARIRSVLP FAIRAENVKR
YVMRKYGFEP EIVKITNPYG KTLDVDFEYL VVSPETYEMA LKINQKREEL GKRKITIVKV
DWMMAEDGKP ISSTRIKRGE IDRYGGII
