COAD_BURP1
ID COAD_BURP1 Reviewed; 166 AA.
AC Q3JW91;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000303|PubMed:21904046};
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, ECO:0000303|PubMed:21904046};
DE Short=PPAT {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000303|PubMed:21904046};
GN Name=coaD {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000303|PubMed:21904046};
GN OrderedLocusNames=BURPS1710b_0748;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEXES WITH 3'-DEPHOSPHO-COA;
RP 4'-DIPHOSPHOPANTETHEINE AND ADENINE, AND SUBUNIT.
RC STRAIN=1710b;
RX PubMed=21904046; DOI=10.1107/s1744309111004349;
RA Edwards T.E., Leibly D.J., Bhandari J., Statnekov J.B., Phan I.,
RA Dieterich S.H., Abendroth J., Staker B.L., Van Voorhis W.C., Myler P.J.,
RA Stewart L.J.;
RT "Structures of phosphopantetheine adenylyltransferase from Burkholderia
RT pseudomallei.";
RL Acta Crystallogr. F 67:1032-1037(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:21904046}.
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; CP000124; ABA49742.1; -; Genomic_DNA.
DR RefSeq; WP_004195249.1; NC_007434.1.
DR PDB; 3K9W; X-ray; 1.60 A; A=1-166.
DR PDB; 3PXU; X-ray; 2.10 A; A=1-166.
DR PDBsum; 3K9W; -.
DR PDBsum; 3PXU; -.
DR AlphaFoldDB; Q3JW91; -.
DR SMR; Q3JW91; -.
DR EnsemblBacteria; ABA49742; ABA49742; BURPS1710b_0748.
DR GeneID; 56593817; -.
DR GeneID; 66545995; -.
DR KEGG; bpm:BURPS1710b_0748; -.
DR HOGENOM; CLU_100149_0_1_4; -.
DR OMA; EFQMALM; -.
DR OrthoDB; 1846503at2; -.
DR BRENDA; 2.7.7.3; 1031.
DR UniPathway; UPA00241; UER00355.
DR EvolutionaryTrace; Q3JW91; -.
DR Proteomes; UP000002700; Chromosome I.
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; Transferase.
FT CHAIN 1..166
FT /note="Phosphopantetheine adenylyltransferase"
FT /id="PRO_1000011110"
FT BINDING 6..10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:21904046,
FT ECO:0007744|PDB:3PXU"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000305|PubMed:21904046, ECO:0007744|PDB:3PXU"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000305|PubMed:21904046, ECO:0007744|PDB:3K9W,
FT ECO:0007744|PDB:3PXU"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000305|PubMed:21904046, ECO:0007744|PDB:3K9W,
FT ECO:0007744|PDB:3PXU"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000305|PubMed:21904046, ECO:0007744|PDB:3K9W,
FT ECO:0007744|PDB:3PXU"
FT BINDING 88..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000305|PubMed:21904046, ECO:0007744|PDB:3PXU"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000305|PubMed:21904046, ECO:0007744|PDB:3PXU"
FT BINDING 123..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000305|PubMed:21904046"
FT SITE 17
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3K9W"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:3K9W"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:3K9W"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:3K9W"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:3K9W"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:3K9W"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:3K9W"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:3K9W"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:3K9W"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:3K9W"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3K9W"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:3K9W"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:3K9W"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:3K9W"
SQ SEQUENCE 166 AA; 18530 MW; C9CDDE2E32564B58 CRC64;
MVVAVYPGTF DPLTRGHEDL VRRASSIFDT LVVGVADSRA KKPFFSLEER LKIANEVLGH
YPNVKVMGFT GLLKDFVRAN DARVIVRGLR AVSDFEYEFQ MAGMNRYLLP DVETMFMTPS
DQYQFISGTI VREIAQLGGD VSKFVFPSVE KWLTEKVAAM AQGPSA
