UniProtKB - P9WPA5 (COAD_MYCTU)
Protein
Phosphopantetheine adenylyltransferase
Gene
coaD
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.UniRule annotation2 Publications
Catalytic activityi
- ATP + D-pantetheine 4'-phosphate + H+ = 3'-dephospho-CoA + diphosphateUniRule annotation2 PublicationsEC:2.7.7.3UniRule annotation2 Publications
Cofactori
Mg2+UniRule annotation
Activity regulationi
Regulated by Coenzyme A (CoA) through feedback inhibition.2 Publications
Kineticsi
kcat is 288.5 min(-1) for the reverse reaction, with diphosphate and 3'-dephospho-CoA as substrates, which is nearly identical to that of the forward reaction fitted to the Hill equation. The enzyme seems to utilize a nonrapid-equilibrium random bi-bi mechanism with a preferred pathway to the ternary complex. A sigmoidal response is observed when ATP was varied at different fixed concentrations of pantetheine 4'-phosphate. Also exhibits nonhyperbolic kinetics when pantetheine 4'-phosphate was varied at a fixed saturating concentration of ATP.1 Publication
- KM=6.7 µM for 3'-dephospho-CoA1 Publication
: coenzyme A biosynthesis Pathwayi
This protein is involved in step 4 of the subpathway that synthesizes CoA from (R)-pantothenate.UniRule annotationProteins known to be involved in the 5 steps of the subpathway in this organism are:
- Type III pantothenate kinase (coaX), Pantothenate kinase (coaA)
- Coenzyme A biosynthesis bifunctional protein CoaBC (coaBC)
- Coenzyme A biosynthesis bifunctional protein CoaBC (coaBC)
- Phosphopantetheine adenylyltransferase (coaD)
- Dephospho-CoA kinase (coaE)
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 | 9 | SubstrateUniRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 17 | ATPUniRule annotationCombined sources1 Publication1 Publication | 1 | |
Sitei | 17 | Transition state stabilizerUniRule annotation | 1 | |
Binding sitei | 41 | SubstrateUniRule annotation | 1 | |
Binding sitei | 73 | Substrate; via amide nitrogenUniRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 87 | SubstrateUniRule annotation | 1 | |
Binding sitei | 98 | ATPUniRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 105 | SubstrateCombined sources1 Publication | 1 | |
Binding sitei | 118 | ATPCombined sources1 Publication1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 9 – 10 | ATPUniRule annotationCombined sources1 Publication1 Publication | 2 | |
Nucleotide bindingi | 88 – 90 | ATPUniRule annotationCombined sources1 Publication1 Publication | 3 | |
Nucleotide bindingi | 122 – 128 | ATPUniRule annotationCombined sources1 Publication1 Publication | 7 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- pantetheine-phosphate adenylyltransferase activity Source: MTBBASE
GO - Biological processi
- coenzyme A biosynthetic process Source: MTBBASE
- protein hexamerization Source: MTBBASE
Keywordsi
Molecular function | Nucleotidyltransferase, Transferase |
Biological process | Coenzyme A biosynthesis |
Ligand | ATP-binding, Magnesium, Nucleotide-binding |
Enzyme and pathway databases
UniPathwayi | UPA00241;UER00355 |
Names & Taxonomyi
Protein namesi | Recommended name: Phosphopantetheine adenylyltransferase2 PublicationsUniRule annotation (EC:2.7.7.3UniRule annotation2 Publications)Alternative name(s): Dephospho-CoA pyrophosphorylaseUniRule annotation Pantetheine-phosphate adenylyltransferaseUniRule annotation Short name: PPAT2 PublicationsUniRule annotation |
Gene namesi | Name:coaDUniRule annotation Synonyms:kdtB1 Publication Ordered Locus Names:Rv2965c ORF Names:MTCY349.22, u0002e |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv2965c |
Subcellular locationi
- Cytoplasm UniRule annotation
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000156242 | 2 – 161 | Phosphopantetheine adenylyltransferaseAdd BLAST | 160 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylthreonineCombined sources | 1 |
Keywords - PTMi
AcetylationProteomic databases
PaxDbi | P9WPA5 |
PTM databases
iPTMneti | P9WPA5 |
Interactioni
Subunit structurei
Homohexamer; dimer of trimers.
UniRule annotation1 Publication1 PublicationProtein-protein interaction databases
STRINGi | 83332.Rv2965c |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P9WPA5 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the bacterial CoaD family.UniRule annotation
Phylogenomic databases
eggNOGi | COG0669, Bacteria |
OMAi | EFQMALM |
PhylomeDBi | P9WPA5 |
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.
: The displayed sequence is further processed into a mature form. Sequence processingi
P9WPA5-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTGAVCPGSF DPVTLGHVDI FERAAAQFDE VVVAILVNPA KTGMFDLDER
60 70 80 90 100
IAMVKESTTH LPNLRVQVGH GLVVDFVRSC GMTAIVKGLR TGTDFEYELQ
110 120 130 140 150
MAQMNKHIAG VDTFFVATAP RYSFVSSSLA KEVAMLGGDV SELLPEPVNR
160
RLRDRLNTER T
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00024 Genomic DNA Translation: AAA50946.1 AL123456 Genomic DNA Translation: CCP45769.1 |
PIRi | B70671 |
RefSeqi | NP_217481.1, NC_000962.3 WP_003414998.1, NZ_NVQJ01000015.1 |
Genome annotation databases
EnsemblBacteriai | CCP45769; CCP45769; Rv2965c |
GeneIDi | 23490791 888423 |
KEGGi | mtu:Rv2965c mtv:RVBD_2965c |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00024 Genomic DNA Translation: AAA50946.1 AL123456 Genomic DNA Translation: CCP45769.1 |
PIRi | B70671 |
RefSeqi | NP_217481.1, NC_000962.3 WP_003414998.1, NZ_NVQJ01000015.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1TFU | X-ray | 1.99 | A | 1-157 | [»] | |
3LCJ | X-ray | 2.10 | A | 1-161 | [»] | |
3NBA | X-ray | 2.68 | A/B/C/D | 1-157 | [»] | |
3NBK | X-ray | 1.58 | A/B/C/D | 1-157 | [»] | |
3PNB | X-ray | 2.11 | A/B/C/D | 1-157 | [»] | |
3RBA | X-ray | 1.59 | A | 1-157 | [»] | |
3RFF | X-ray | 1.76 | A | 1-157 | [»] | |
3RHS | X-ray | 1.59 | A | 1-157 | [»] | |
3UC5 | X-ray | 1.70 | A | 1-157 | [»] | |
4E1A | X-ray | 1.62 | A | 1-161 | [»] | |
4R0N | X-ray | 2.00 | A/C/E/G/I/K | 2-157 | [»] | |
6G6V | X-ray | 1.94 | A | 1-161 | [»] | |
6G7S | X-ray | 1.77 | A | 1-161 | [»] | |
6G7T | X-ray | 1.65 | A | 1-161 | [»] | |
6G7U | X-ray | 1.84 | A | 1-161 | [»] | |
6G7V | X-ray | 1.78 | A | 1-161 | [»] | |
6QMF | X-ray | 1.77 | A | 1-161 | [»] | |
6QMG | X-ray | 1.65 | A | 1-161 | [»] | |
6QMI | X-ray | 1.78 | A | 1-161 | [»] | |
SMRi | P9WPA5 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv2965c |
PTM databases
iPTMneti | P9WPA5 |
Proteomic databases
PaxDbi | P9WPA5 |
Genome annotation databases
EnsemblBacteriai | CCP45769; CCP45769; Rv2965c |
GeneIDi | 23490791 888423 |
KEGGi | mtu:Rv2965c mtv:RVBD_2965c |
Organism-specific databases
TubercuListi | Rv2965c |
Phylogenomic databases
eggNOGi | COG0669, Bacteria |
OMAi | EFQMALM |
PhylomeDBi | P9WPA5 |
Enzyme and pathway databases
UniPathwayi | UPA00241;UER00355 |
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 |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | COAD_MYCTU | |
Accessioni | P9WPA5Primary (citable) accession number: P9WPA5 Secondary accession number(s): L0TCR8 Q50452 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | December 2, 2020 | |
This is version 37 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, 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