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UniProtKB - P0A6I6 (COAD_ECOLI)
Protein
Phosphopantetheine adenylyltransferase
Gene
coaD
Organism
Escherichia coli (strain K12)
Status
Functioni
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate (PubMed:10480925, PubMed:17873050).
CoA is not a substrate for the enzyme (PubMed:10480925).
UniRule annotation2 PublicationsMiscellaneous
The crystal structures in complex with substrates suggest the enzyme stabilizes the transition state but the functional groups of the enzyme are not directly involved in reaction catalysis.1 Publication
Caution
Was originally thought to have an essential function in lipopolysaccharide biosynthesis.1 Publication
Catalytic activityi
- (R)-4'-phosphopantetheine + ATP + H+ = 3'-dephospho-CoA + diphosphateUniRule annotation2 PublicationsEC:2.7.7.3UniRule annotation2 Publications
Cofactori
Mg2+1 PublicationNote: Crystallized in the absence of Mg2+, the catalytic metal is not bound by the protein but probably by non-esterified oxygen atoms from ATP and/or ordered H(2)O (PubMed:11812124).1 Publication
Activity regulationi
Feedback inhibited by CoA, which is competitive with ATP, 4'-phosphopantetheine and 3'-dephospho-CoA (PubMed:17873050, PubMed:10480925). Binds 0.5 CoA tightly per monomer in the same position as 3'-dephospho-CoA but in a different fashion (PubMed:12837781, PubMed:17873050). Is inhibited by the very potent and specific inhibitor PTX042695 dipeptide, with an IC50 of 6 nM, a compound which has no activity against porcine PPAT (PubMed:12750020). A series of pyrazoloquinolones were also characterized as ATP-competitive inhibitors of PPAT (PubMed:20486930).1 Publication4 Publications
Kineticsi
kcat is 1.37 sec(-1) for the forward reaction, with ATP and pantetheine 4'-phosphate as substrates (PubMed:17873050). kcat is 3.3 sec(-1) for the reverse reaction, with diphosphate and 3'-dephospho-CoA as substrates (PubMed:10480925). kcat is 1.37 sec(-1) for the reverse reaction, with diphosphate and 3'-dephospho-CoA as substrates (PubMed:17873050).2 Publications
- KM=7.0 µM for 3'-dephospho-CoA1 Publication
- KM=17.0 µM for 3'-dephospho-CoA1 Publication
- KM=0.22 mM for diphosphate1 Publication
- KM=0.23 mM for diphosphate1 Publication
- KM=220 µM for ATP1 Publication
- KM=4.7 µM for 4'-phosphopantetheine1 Publication
pH dependencei
Optimum pH is 6.9.1 Publication
: coenzyme A biosynthesis Pathwayi
This protein is involved in step 4 of the subpathway that synthesizes CoA from (R)-pantothenate.UniRule annotation This subpathway is part of the pathway coenzyme A biosynthesis, which is itself part of Cofactor biosynthesis.View all proteins of this organism that are known to be involved in the subpathway that synthesizes CoA from (R)-pantothenate, the pathway coenzyme A biosynthesis and in Cofactor biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 10 | SubstrateCombined sources2 Publications | 1 | |
Binding sitei | 18 | ATPCombined sources1 Publication | 1 | |
Sitei | 18 | Transition state stabilizer1 Publication | 1 | |
Binding sitei | 42 | SubstrateCombined sources2 Publications | 1 | |
Binding sitei | 74 | Substrate; via amide nitrogenCombined sources2 Publications | 1 | |
Binding sitei | 88 | SubstrateCombined sources1 Publication | 1 | |
Binding sitei | 99 | ATPCombined sources1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 7 – 11 | ATPCombined sources1 Publication | 5 | |
Nucleotide bindingi | 89 – 91 | ATPCombined sources1 Publication | 3 | |
Nucleotide bindingi | 124 – 130 | ATPCombined sources1 Publication | 7 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- identical protein binding Source: EcoCyc
- pantetheine-phosphate adenylyltransferase activity Source: EcoCyc
GO - Biological processi
- coenzyme A biosynthetic process Source: EcoCyc
Keywordsi
Molecular function | Nucleotidyltransferase, Transferase |
Biological process | Coenzyme A biosynthesis |
Ligand | ATP-binding, Magnesium, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:PANTEPADENYLYLTRAN-MONOMER |
BRENDAi | 2.7.7.3, 2026 |
SABIO-RKi | P0A6I6 |
UniPathwayi | UPA00241;UER00355 |
Names & Taxonomyi
Protein namesi | Recommended name: Phosphopantetheine adenylyltransferase1 PublicationUniRule annotation (EC:2.7.7.3UniRule annotation2 Publications)Alternative name(s): Dephospho-CoA pyrophosphorylaseUniRule annotation Pantetheine-phosphate adenylyltransferaseUniRule annotation Short name: PPAT1 PublicationUniRule annotation |
Gene namesi | Name:coaD1 PublicationUniRule annotation Synonyms:kdtB1 Publication, yicA Ordered Locus Names:b3634, JW3609 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000156204 | 1 – 159 | Phosphopantetheine adenylyltransferaseAdd BLAST | 159 |
Proteomic databases
jPOSTi | P0A6I6 |
PaxDbi | P0A6I6 |
PRIDEi | P0A6I6 |
Interactioni
Subunit structurei
Binary interactionsi
P0A6I6
With | #Exp. | IntAct |
---|---|---|
rplD [P60723] | 2 | EBI-553173,EBI-545597 |
GO - Molecular functioni
- identical protein binding Source: EcoCyc
Protein-protein interaction databases
BioGRIDi | 4263379, 238 interactors |
DIPi | DIP-35966N |
IntActi | P0A6I6, 10 interactors |
STRINGi | 511145.b3634 |
Chemistry databases
BindingDBi | P0A6I6 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A6I6 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A6I6 |
Family & Domainsi
Sequence similaritiesi
Belongs to the bacterial CoaD family.UniRule annotation
Phylogenomic databases
eggNOGi | COG0669, Bacteria |
HOGENOMi | CLU_100149_0_1_6 |
InParanoidi | P0A6I6 |
PhylomeDBi | P0A6I6 |
Family and domain databases
CDDi | cd02163, PPAT, 1 hit |
Gene3Di | 3.40.50.620, 1 hit |
HAMAPi | MF_00151, PPAT_bact, 1 hit |
InterProi | View protein in InterPro IPR004821, Cyt_trans-like IPR001980, PPAT IPR014729, Rossmann-like_a/b/a_fold |
PANTHERi | PTHR21342:SF1, PTHR21342:SF1, 1 hit |
Pfami | View protein in Pfam PF01467, CTP_transf_like, 1 hit |
PRINTSi | PR01020, LPSBIOSNTHSS |
TIGRFAMsi | TIGR01510, coaD_prev_kdtB, 1 hit TIGR00125, cyt_tran_rel, 1 hit |
i Sequence
Sequence statusi: Complete.
P0A6I6-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MQKRAIYPGT FDPITNGHID IVTRATQMFD HVILAIAASP SKKPMFTLEE
60 70 80 90 100
RVALAQQATA HLGNVEVVGF SDLMANFARN QHATVLIRGL RAVADFEYEM
110 120 130 140 150
QLAHMNRHLM PELESVFLMP SKEWSFISSS LVKEVARHQG DVTHFLPENV
HQALMAKLA
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M60670 Genomic DNA Translation: AAA24044.1 M86305 Genomic DNA Translation: AAA03746.1 U00039 Genomic DNA Translation: AAB18611.1 U00096 Genomic DNA Translation: AAC76658.1 AP009048 Genomic DNA Translation: BAE77658.1 |
PIRi | JU0468 |
RefSeqi | NP_418091.1, NC_000913.3 WP_001171866.1, NZ_STEB01000024.1 |
Genome annotation databases
EnsemblBacteriai | AAC76658; AAC76658; b3634 BAE77658; BAE77658; BAE77658 |
GeneIDi | 67417636 947386 |
KEGGi | ecj:JW3609 eco:b3634 |
PATRICi | fig|1411691.4.peg.3072 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M60670 Genomic DNA Translation: AAA24044.1 M86305 Genomic DNA Translation: AAA03746.1 U00039 Genomic DNA Translation: AAB18611.1 U00096 Genomic DNA Translation: AAC76658.1 AP009048 Genomic DNA Translation: BAE77658.1 |
PIRi | JU0468 |
RefSeqi | NP_418091.1, NC_000913.3 WP_001171866.1, NZ_STEB01000024.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1B6T | X-ray | 1.80 | A/B | 1-159 | [»] | |
1GN8 | X-ray | 1.83 | A/B | 1-159 | [»] | |
1H1T | X-ray | 1.78 | A/B | 1-159 | [»] | |
1QJC | X-ray | 1.63 | A/B | 2-159 | [»] | |
5JBN | X-ray | 1.45 | A/B | 1-159 | [»] | |
6B7A | X-ray | 1.99 | A/B | 1-159 | [»] | |
6B7B | X-ray | 1.98 | A/B | 1-159 | [»] | |
6B7C | X-ray | 1.56 | A/B | 1-159 | [»] | |
6B7D | X-ray | 1.80 | A/B | 1-159 | [»] | |
6B7E | X-ray | 2.10 | A/B | 1-159 | [»] | |
6B7F | X-ray | 2.56 | A/B | 1-159 | [»] | |
6CCK | X-ray | 1.61 | A/B | 1-159 | [»] | |
6CCL | X-ray | 1.77 | A/B | 1-159 | [»] | |
6CCM | X-ray | 1.79 | A/B | 1-159 | [»] | |
6CCN | X-ray | 1.87 | A/B | 1-159 | [»] | |
6CCO | X-ray | 1.82 | A/B | 1-159 | [»] | |
6CCQ | X-ray | 1.92 | A/B | 1-159 | [»] | |
6CCS | X-ray | 2.06 | A/B | 1-159 | [»] | |
6CHL | X-ray | 2.20 | A/B | 1-159 | [»] | |
6CHM | X-ray | 2.28 | A/B | 1-159 | [»] | |
6CHN | X-ray | 2.03 | A/B | 1-159 | [»] | |
6CHO | X-ray | 1.85 | A/B | 1-159 | [»] | |
6CHP | X-ray | 1.94 | A/B | 1-159 | [»] | |
6CHQ | X-ray | 1.79 | A/B | 1-159 | [»] | |
6CKW | X-ray | 2.06 | A/B | 1-159 | [»] | |
SMRi | P0A6I6 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263379, 238 interactors |
DIPi | DIP-35966N |
IntActi | P0A6I6, 10 interactors |
STRINGi | 511145.b3634 |
Chemistry databases
BindingDBi | P0A6I6 |
ChEMBLi | CHEMBL4523175 |
Proteomic databases
jPOSTi | P0A6I6 |
PaxDbi | P0A6I6 |
PRIDEi | P0A6I6 |
Genome annotation databases
EnsemblBacteriai | AAC76658; AAC76658; b3634 BAE77658; BAE77658; BAE77658 |
GeneIDi | 67417636 947386 |
KEGGi | ecj:JW3609 eco:b3634 |
PATRICi | fig|1411691.4.peg.3072 |
Organism-specific databases
EchoBASEi | EB1176 |
Phylogenomic databases
eggNOGi | COG0669, Bacteria |
HOGENOMi | CLU_100149_0_1_6 |
InParanoidi | P0A6I6 |
PhylomeDBi | P0A6I6 |
Enzyme and pathway databases
UniPathwayi | UPA00241;UER00355 |
BioCyci | EcoCyc:PANTEPADENYLYLTRAN-MONOMER |
BRENDAi | 2.7.7.3, 2026 |
SABIO-RKi | P0A6I6 |
Miscellaneous databases
EvolutionaryTracei | P0A6I6 |
PROi | PR:P0A6I6 |
Family and domain databases
CDDi | cd02163, PPAT, 1 hit |
Gene3Di | 3.40.50.620, 1 hit |
HAMAPi | MF_00151, PPAT_bact, 1 hit |
InterProi | View protein in InterPro IPR004821, Cyt_trans-like IPR001980, PPAT IPR014729, Rossmann-like_a/b/a_fold |
PANTHERi | PTHR21342:SF1, PTHR21342:SF1, 1 hit |
Pfami | View protein in Pfam PF01467, CTP_transf_like, 1 hit |
PRINTSi | PR01020, LPSBIOSNTHSS |
TIGRFAMsi | TIGR01510, coaD_prev_kdtB, 1 hit TIGR00125, cyt_tran_rel, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | COAD_ECOLI | |
Accessioni | P0A6I6Primary (citable) accession number: P0A6I6 Secondary accession number(s): P23875, Q2M7U8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 29, 2005 |
Last sequence update: | March 29, 2005 | |
Last modified: | February 23, 2022 | |
This is version 138 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families