COAD_COXBU
ID COAD_COXBU Reviewed; 159 AA.
AC Q83EM7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000303|PubMed:26033498};
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:26033498};
GN Name=coaD {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000303|PubMed:26033498};
GN OrderedLocusNames=CBU_0288;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=26033498; DOI=10.1002/prot.24841;
RA Franklin M.C., Cheung J., Rudolph M.J., Burshteyn F., Cassidy M., Gary E.,
RA Hillerich B., Yao Z.K., Carlier P.R., Totrov M., Love J.D.;
RT "Structural genomics for drug design against the pathogen Coxiella
RT burnetii.";
RL Proteins 83:2124-2136(2015).
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 -!- 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; AE016828; AAO89846.1; -; Genomic_DNA.
DR RefSeq; NP_819332.1; NC_002971.3.
DR RefSeq; WP_005771452.1; NZ_CDBG01000001.1.
DR PDB; 4F3R; X-ray; 2.25 A; A/B/C=1-159.
DR PDBsum; 4F3R; -.
DR AlphaFoldDB; Q83EM7; -.
DR SMR; Q83EM7; -.
DR STRING; 227377.CBU_0288; -.
DR EnsemblBacteria; AAO89846; AAO89846; CBU_0288.
DR GeneID; 1208170; -.
DR KEGG; cbu:CBU_0288; -.
DR PATRIC; fig|227377.7.peg.281; -.
DR eggNOG; COG0669; Bacteria.
DR HOGENOM; CLU_100149_0_1_6; -.
DR OMA; EFQMALM; -.
DR UniPathway; UPA00241; UER00355.
DR Proteomes; UP000002671; 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..159
FT /note="Phosphopantetheine adenylyltransferase"
FT /id="PRO_0000156200"
FT BINDING 10..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
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 BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 88..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 123..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
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:4F3R"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:4F3R"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:4F3R"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:4F3R"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:4F3R"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:4F3R"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:4F3R"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:4F3R"
FT HELIX 92..108
FT /evidence="ECO:0007829|PDB:4F3R"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:4F3R"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4F3R"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:4F3R"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:4F3R"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:4F3R"
SQ SEQUENCE 159 AA; 17967 MW; A87B74F77AA72525 CRC64;
MKPIAIYPGT FDPLTNGHVD IIERALPLFN KIIVACAPTS RKDPHLKLEE RVNLIADVLT
DERVEVLPLT GLLVDFAKTH QANFILRGLR AVSDFDYEFQ LAHMNYQLSP EIETIFLPAR
EGYSYVSGTM VREIVTLGGD VSPFVPPLVA RHLQKRREK
