COAD_ENTFA
ID COAD_ENTFA Reviewed; 163 AA.
AC Q831P9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000303|PubMed:17077496, ECO:0000303|PubMed:21912874};
DE EC=2.7.7.3 {ECO:0000255|HAMAP-Rule:MF_00151};
DE AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00151};
DE AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151};
DE Short=PPAT {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000303|PubMed:21912874};
GN Name=coaD {ECO:0000255|HAMAP-Rule:MF_00151}; OrderedLocusNames=EF_2451;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2]
RP SUBUNIT.
RC STRAIN=ATCC 700802 / V583;
RX PubMed=17077496; DOI=10.1107/s1744309106041108;
RA Kang J.Y., Lee H.H., Yoon H.J., Kim H.S., Suh S.W.;
RT "Overexpression, crystallization and preliminary X-ray crystallographic
RT analysis of phosphopantetheine adenylyltransferase from Enterococcus
RT faecalis.";
RL Acta Crystallogr. F 62:1131-1133(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP ATP OR PANTETHEINE.
RC STRAIN=ATCC 700802 / V583;
RX PubMed=21912874; DOI=10.1007/s10059-011-0102-y;
RA Yoon H.J., Kang J.Y., Mikami B., Lee H.H., Suh S.W.;
RT "Crystal structure of phosphopantetheine adenylyltransferase from
RT Enterococcus faecalis in the ligand-unbound state and in complex with ATP
RT and pantetheine.";
RL Mol. Cells 32:431-435(2011).
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_00151}.
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_00151};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00151};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00151}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00151,
CC ECO:0000269|PubMed:17077496}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00151}.
CC -!- SIMILARITY: Belongs to the bacterial CoaD family. {ECO:0000255|HAMAP-
CC Rule:MF_00151}.
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DR EMBL; AE016830; AAO82169.1; -; Genomic_DNA.
DR RefSeq; NP_816099.1; NC_004668.1.
DR RefSeq; WP_002356693.1; NZ_KE136528.1.
DR PDB; 3ND5; X-ray; 2.30 A; A/B/C/D/E/F=1-163.
DR PDB; 3ND6; X-ray; 2.30 A; A/B/C/D/E/F=1-163.
DR PDB; 3ND7; X-ray; 2.40 A; A/B/C/D/E/F=1-163.
DR PDBsum; 3ND5; -.
DR PDBsum; 3ND6; -.
DR PDBsum; 3ND7; -.
DR AlphaFoldDB; Q831P9; -.
DR SMR; Q831P9; -.
DR STRING; 226185.EF_2451; -.
DR BindingDB; Q831P9; -.
DR EnsemblBacteria; AAO82169; AAO82169; EF_2451.
DR KEGG; efa:EF2451; -.
DR PATRIC; fig|226185.45.peg.1094; -.
DR eggNOG; COG0669; Bacteria.
DR HOGENOM; CLU_100149_0_1_9; -.
DR OMA; EFQMALM; -.
DR UniPathway; UPA00241; UER00355.
DR EvolutionaryTrace; Q831P9; -.
DR Proteomes; UP000001415; 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 CDD; cd02163; PPAT; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00151; PPAT_bact; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR001980; PPAT.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR21342:SF1; PTHR21342:SF1; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR PRINTS; PR01020; LPSBIOSNTHSS.
DR TIGRFAMs; TIGR01510; coaD_prev_kdtB; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Magnesium;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..163
FT /note="Phosphopantetheine adenylyltransferase"
FT /id="PRO_0000156207"
FT BINDING 10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:21912874,
FT ECO:0007744|PDB:3ND6"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000305|PubMed:21912874, ECO:0007744|PDB:3ND7"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 90..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6"
FT BINDING 125..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6"
FT SITE 18
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:3ND5"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:3ND5"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:3ND5"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:3ND5"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:3ND5"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:3ND5"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:3ND5"
FT HELIX 94..110
FT /evidence="ECO:0007829|PDB:3ND5"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:3ND5"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3ND5"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:3ND5"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:3ND5"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:3ND5"
SQ SEQUENCE 163 AA; 18675 MW; 32A28D9691CD6769 CRC64;
MRKIALFPGS FDPMTNGHLN LIERSAKLFD EVIIGVFINT SKQTLFTPEE KKYLIEEATK
EMPNVRVIMQ ETQLTVESAK SLGANFLIRG IRNVKDYEYE KDIAKMNQHL APEIETVFLL
AEEPYAHVSS SLLKEVLRFG GDVSDYLPPN IYHALKQKKN DWS
