COAD_PSEAE
ID COAD_PSEAE Reviewed; 159 AA.
AC Q9I6D1;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151};
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};
GN Name=coaD {ECO:0000255|HAMAP-Rule:MF_00151}; OrderedLocusNames=PA0363;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG03752.1; -; Genomic_DNA.
DR PIR; A83600; A83600.
DR RefSeq; NP_249054.1; NC_002516.2.
DR RefSeq; WP_003084466.1; NZ_QZGE01000016.1.
DR PDB; 5X6F; X-ray; 2.59 A; A/B/C/D/E/F=1-159.
DR PDBsum; 5X6F; -.
DR AlphaFoldDB; Q9I6D1; -.
DR SMR; Q9I6D1; -.
DR STRING; 287.DR97_3329; -.
DR PaxDb; Q9I6D1; -.
DR PRIDE; Q9I6D1; -.
DR EnsemblBacteria; AAG03752; AAG03752; PA0363.
DR GeneID; 879847; -.
DR KEGG; pae:PA0363; -.
DR PATRIC; fig|208964.12.peg.382; -.
DR PseudoCAP; PA0363; -.
DR HOGENOM; CLU_100149_0_1_6; -.
DR InParanoid; Q9I6D1; -.
DR OMA; EFQMALM; -.
DR PhylomeDB; Q9I6D1; -.
DR BioCyc; PAER208964:G1FZ6-366-MON; -.
DR BRENDA; 2.7.7.3; 5087.
DR UniPathway; UPA00241; UER00355.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008771; F:[citrate (pro-3S)-lyase] ligase activity; IEA:InterPro.
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; IPR013166; Citrate_lyase_ligase_C.
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 SMART; SM00764; Citrate_ly_lig; 1.
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_0000156258"
FT BINDING 9..10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
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 BINDING 41
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 17
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:5X6F"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:5X6F"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:5X6F"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:5X6F"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:5X6F"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:5X6F"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:5X6F"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:5X6F"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:5X6F"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:5X6F"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:5X6F"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:5X6F"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:5X6F"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:5X6F"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:5X6F"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:5X6F"
SQ SEQUENCE 159 AA; 17771 MW; E0B0293D1B007B69 CRC64;
MNRVLYPGTF DPITKGHGDL IERASRLFDH VIIAVAASPK KNPLFSLEQR VALAQEVTKH
LPNVEVVGFS TLLAHFVKEQ KANVFLRGLR AVSDFEYEFQ LANMNRQLAP DVESMFLTPS
EKYSFISSTL VREIAALGGD ISKFVHPAVA DALAERFKR
