COAD_THEGJ
ID COAD_THEGJ Reviewed; 159 AA.
AC C5A3G3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=TGAM_0273;
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
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; CP001398; ACS32775.1; -; Genomic_DNA.
DR RefSeq; WP_015857894.1; NC_012804.1.
DR AlphaFoldDB; C5A3G3; -.
DR SMR; C5A3G3; -.
DR STRING; 593117.TGAM_0273; -.
DR PaxDb; C5A3G3; -.
DR PRIDE; C5A3G3; -.
DR EnsemblBacteria; ACS32775; ACS32775; TGAM_0273.
DR GeneID; 7988929; -.
DR KEGG; tga:TGAM_0273; -.
DR PATRIC; fig|593117.10.peg.276; -.
DR eggNOG; arCOG01223; Archaea.
DR HOGENOM; CLU_035272_5_0_2; -.
DR OMA; FDTLHSG; -.
DR OrthoDB; 93412at2157; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000001488; 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 3: Inferred from homology;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Nucleotide-binding;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..159
FT /note="Phosphopantetheine adenylyltransferase"
FT /id="PRO_1000212388"
SQ SEQUENCE 159 AA; 18179 MW; 218AEC412C24F697 CRC64;
MRKPYRKVVV GGTFDRLHLG HKALLRKAFE VGRYVYVGLT SDEMIRNKPY AEKILPYELR
LMDLLKFFEV NGYTNYRIIK INTAIGFADR IKSLEAIVVS EETYKGALLV NRAREERGLK
PLEIVTIKLV KSRIGPKISS TLIRAGLIDP FGNPLKKDN
