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UniProtKB - P0ABQ0 (COABC_ECOLI)
Protein
Coenzyme A biosynthesis bifunctional protein CoaBC
Gene
coaBC
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine (PubMed:11278255, PubMed:12140293, PubMed:14686929).
In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine (PubMed:10922366, PubMed:11358972).
5 PublicationsCatalytic activityi
- H+ + N-[(R)-4-phosphopantothenoyl]-L-cysteine = (R)-4'-phosphopantetheine + CO2UniRule annotation2 PublicationsEC:4.1.1.36UniRule annotation2 Publications
- (R)-4'-phosphopantothenate + CTP + L-cysteine = CMP + diphosphate + H+ + N-[(R)-4-phosphopantothenoyl]-L-cysteineUniRule annotation3 PublicationsEC:6.3.2.5UniRule annotation3 Publications
Cofactori
Protein has several cofactor binding sites:- Mg2+UniRule annotation1 Publication
- FMNUniRule annotation3 PublicationsNote: Binds 1 FMN per subunit.UniRule annotation1 Publication
: coenzyme A biosynthesis Pathwayi
This protein is involved in step 2 and 3 of the subpathway that synthesizes CoA from (R)-pantothenate.UniRule annotation1 Publication 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 |
---|---|---|---|---|
Active sitei | 158 | Proton donorUniRule annotationCurated | 1 | |
Binding sitei | 279 | CTPUniRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 289 | CTPUniRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 327 | CTP; via amide nitrogenUniRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 341 | CTPUniRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 345 | CTPUniRule annotationCombined sources1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 273 – 275 | CTPUniRule annotationCombined sources1 Publication | 3 | |
Nucleotide bindingi | 308 – 311 | CTPUniRule annotationCombined sources1 Publication | 4 |
GO - Molecular functioni
- FMN binding Source: EcoCyc
- identical protein binding Source: EcoCyc
- metal ion binding Source: UniProtKB-KW
- phosphopantothenate--cysteine ligase activity Source: EcoCyc
- phosphopantothenoylcysteine decarboxylase activity Source: EcoCyc
GO - Biological processi
- coenzyme A biosynthetic process Source: EcoCyc
- pantothenate catabolic process Source: InterPro
Keywordsi
Molecular function | Decarboxylase, Ligase, Lyase, Multifunctional enzyme |
Ligand | Flavoprotein, FMN, Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10004-MONOMER |
BRENDAi | 6.3.2.5, 2026 |
SABIO-RKi | P0ABQ0 |
UniPathwayi | UPA00241;UER00353 UPA00241;UER00354 |
Names & Taxonomyi
Protein namesi | Recommended name: Coenzyme A biosynthesis bifunctional protein CoaBCUniRule annotationCuratedAlternative name(s): DNA/pantothenate metabolism flavoproteinUniRule annotationCurated Phosphopantothenoylcysteine synthetase/decarboxylaseUniRule annotation Short name: PPCS-PPCDCUniRule annotation Including the following 2 domains: Phosphopantothenoylcysteine decarboxylase1 PublicationUniRule annotation (EC:4.1.1.36UniRule annotation2 Publications) Short name: PPC decarboxylase1 PublicationUniRule annotation Short name: PPC-DC1 PublicationUniRule annotation Alternative name(s): CoaC1 PublicationUniRule annotation Phosphopantothenate--cysteine ligaseUniRule annotationCurated (EC:6.3.2.5UniRule annotation3 Publications) Alternative name(s): CoaB1 PublicationUniRule annotation Phosphopantothenoylcysteine synthetase1 PublicationUniRule annotation Short name: PPC synthetaseUniRule annotation Short name: PPC-S1 PublicationUniRule annotation |
Gene namesi | Name:coaBC1 PublicationUniRule annotation Synonyms:dfp1 Publication Ordered Locus Names:b3639, JW5642 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytosol
- cytosol Source: EcoCyc
Other locations
- phosphopantothenoylcysteine decarboxylase complex Source: GO_Central
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 11 | G → D in Dfp-707; temperature-sensitive, impairs folding. 1 Publication | 1 | |
Mutagenesisi | 14 | G → S: No FMN binding. 1 Publication | 1 | |
Mutagenesisi | 15 | G → A: Less than 5% of wild-type activity. 1 Publication | 1 | |
Mutagenesisi | 16 | I → L: Severely reduced activity. 1 Publication | 1 | |
Mutagenesisi | 16 | I → V: Slightly reduced activity. 1 Publication | 1 | |
Mutagenesisi | 17 | A → D: Less than 5% of wild-type activity. 1 Publication | 1 | |
Mutagenesisi | 17 | A → G or S: Almost wild-type activity. 1 Publication | 1 | |
Mutagenesisi | 19 | Y → F: Almost wild-type activity. 1 Publication | 1 | |
Mutagenesisi | 19 | Y → L: Reduced activity. 1 Publication | 1 | |
Mutagenesisi | 20 | K → N or Q: Reduced activity. 1 Publication | 1 | |
Mutagenesisi | 20 | K → R: Almost wild-type activity. 1 Publication | 1 | |
Mutagenesisi | 46 | F → L: Reduced activity. 1 Publication | 1 | |
Mutagenesisi | 75 | H → N: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 89 | P → A: Binds FMN, but more loosely than wild-type. 1 Publication | 1 | |
Mutagenesisi | 89 | P → D: No FMN binding. 1 Publication | 1 | |
Mutagenesisi | 91 | T → V: Binds FMN. 1 Publication | 1 | |
Mutagenesisi | 124 | M → L: No effect. 1 Publication | 1 | |
Mutagenesisi | 125 | N → D or Q: Loss of activity. 2 Publications | 1 | |
Mutagenesisi | 128 | M → L: Severely reduced activity. 1 Publication | 1 | |
Mutagenesisi | 158 | C → A or S: Loss of activity. | 1 | |
Mutagenesisi | 194 | T → V: Loss of dimerization. 1 Publication | 1 | |
Mutagenesisi | 198 | T → V: Loss of dimerization. 1 Publication | 1 | |
Mutagenesisi | 203 | D → N: Loss of dimerization. 1 Publication | 1 | |
Mutagenesisi | 210 | N → D: Loss of activity, reaction intermediate detectable. 2 Publications | 1 | |
Mutagenesisi | 210 | N → H or K: Loss of activity, reaction intermediate not detectable. 2 Publications | 1 | |
Mutagenesisi | 212 | S → A: Small effect on activity. 1 Publication | 1 | |
Mutagenesisi | 215 | K → Q: No effect. 1 Publication | 1 | |
Mutagenesisi | 275 | A → V: Loss of dimerization. 2 Publications | 1 | |
Mutagenesisi | 289 | K → Q: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 291 | K → Q: Reduced activity. 1 Publication | 1 | |
Mutagenesisi | 292 | K → Q: Small effect on activity. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB03403, Cytidine-5'-Monophosphate DB02431, Cytidine-5'-Triphosphate |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000182022 | 2 – 406 | Coenzyme A biosynthesis bifunctional protein CoaBCAdd BLAST | 405 |
Proteomic databases
jPOSTi | P0ABQ0 |
PaxDbi | P0ABQ0 |
PRIDEi | P0ABQ0 |
Interactioni
Subunit structurei
Binary interactionsi
GO - Molecular functioni
- identical protein binding Source: EcoCyc
Protein-protein interaction databases
BioGRIDi | 4261256, 26 interactors |
DIPi | DIP-48472N |
IntActi | P0ABQ0, 2 interactors |
STRINGi | 511145.b3639 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0ABQ0 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0ABQ0 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2 – 190 | Phosphopantothenoylcysteine decarboxylaseUniRule annotation1 PublicationAdd BLAST | 189 | |
Regioni | 191 – 406 | Phosphopantothenate--cysteine ligaseUniRule annotation1 PublicationAdd BLAST | 216 |
Sequence similaritiesi
In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily.UniRule annotationCurated
Phylogenomic databases
eggNOGi | COG0452, Bacteria |
HOGENOMi | CLU_033319_0_1_6 |
InParanoidi | P0ABQ0 |
PhylomeDBi | P0ABQ0 |
Family and domain databases
Gene3Di | 3.40.50.10300, 1 hit 3.40.50.1950, 1 hit |
HAMAPi | MF_02225, CoaBC, 1 hit |
InterProi | View protein in InterPro IPR035929, CoaB-like_sf IPR005252, CoaBC IPR007085, DNA/pantothenate-metab_flavo_C IPR036551, Flavin_trans-like IPR003382, Flavoprotein |
Pfami | View protein in Pfam PF04127, DFP, 1 hit PF02441, Flavoprotein, 1 hit |
SUPFAMi | SSF102645, SSF102645, 1 hit SSF52507, SSF52507, 1 hit |
TIGRFAMsi | TIGR00521, coaBC_dfp, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0ABQ0-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSLAGKKIVL GVSGGIAAYK TPELVRRLRD RGADVRVAMT EAAKAFITPL
60 70 80 90 100
SLQAVSGYPV SDSLLDPAAE AAMGHIELGK WADLVILAPA TADLIARVAA
110 120 130 140 150
GMANDLVSTI CLATPAPVAV LPAMNQQMYR AAATQHNLEV LASRGLLIWG
160 170 180 190 200
PDSGSQACGD IGPGRMLDPL TIVDMAVAHF SPVNDLKHLN IMITAGPTRE
210 220 230 240 250
PLDPVRYISN HSSGKMGFAI AAAAARRGAN VTLVSGPVSL PTPPFVKRVD
260 270 280 290 300
VMTALEMEAA VNASVQQQNI FIGCAAVADY RAATVAPEKI KKQATQGDEL
310 320 330 340 350
TIKMVKNPDI VAGVAALKDH RPYVVGFAAE TNNVEEYARQ KRIRKNLDLI
360 370 380 390 400
CANDVSQPTQ GFNSDNNALH LFWQDGDKVL PLERKELLGQ LLLDEIVTRY
DEKNRR
Sequence cautioni
The sequence AAA61992 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L10328 Genomic DNA Translation: AAA61992.1 Different initiation. U00096 Genomic DNA Translation: AAC76663.2 AP009048 Genomic DNA Translation: BAE77653.1 V01578 Genomic DNA No translation available. |
RefSeqi | NP_418096.4, NC_000913.3 WP_000050139.1, NZ_SSZK01000022.1 |
Genome annotation databases
EnsemblBacteriai | AAC76663; AAC76663; b3639 BAE77653; BAE77653; BAE77653 |
GeneIDi | 66672466 949047 |
KEGGi | ecj:JW5642 eco:b3639 |
PATRICi | fig|1411691.4.peg.3067 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L10328 Genomic DNA Translation: AAA61992.1 Different initiation. U00096 Genomic DNA Translation: AAC76663.2 AP009048 Genomic DNA Translation: BAE77653.1 V01578 Genomic DNA No translation available. |
RefSeqi | NP_418096.4, NC_000913.3 WP_000050139.1, NZ_SSZK01000022.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1U7U | X-ray | 2.40 | A | 181-406 | [»] | |
1U7W | X-ray | 2.50 | A/B/C | 181-406 | [»] | |
1U7Z | X-ray | 2.30 | A/B/C | 181-406 | [»] | |
1U80 | X-ray | 2.85 | A/B/C | 181-406 | [»] | |
SMRi | P0ABQ0 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261256, 26 interactors |
DIPi | DIP-48472N |
IntActi | P0ABQ0, 2 interactors |
STRINGi | 511145.b3639 |
Chemistry databases
DrugBanki | DB03403, Cytidine-5'-Monophosphate DB02431, Cytidine-5'-Triphosphate |
Proteomic databases
jPOSTi | P0ABQ0 |
PaxDbi | P0ABQ0 |
PRIDEi | P0ABQ0 |
Genome annotation databases
EnsemblBacteriai | AAC76663; AAC76663; b3639 BAE77653; BAE77653; BAE77653 |
GeneIDi | 66672466 949047 |
KEGGi | ecj:JW5642 eco:b3639 |
PATRICi | fig|1411691.4.peg.3067 |
Organism-specific databases
EchoBASEi | EB0004 |
Phylogenomic databases
eggNOGi | COG0452, Bacteria |
HOGENOMi | CLU_033319_0_1_6 |
InParanoidi | P0ABQ0 |
PhylomeDBi | P0ABQ0 |
Enzyme and pathway databases
UniPathwayi | UPA00241;UER00353 UPA00241;UER00354 |
BioCyci | EcoCyc:EG10004-MONOMER |
BRENDAi | 6.3.2.5, 2026 |
SABIO-RKi | P0ABQ0 |
Miscellaneous databases
EvolutionaryTracei | P0ABQ0 |
PROi | PR:P0ABQ0 |
Family and domain databases
Gene3Di | 3.40.50.10300, 1 hit 3.40.50.1950, 1 hit |
HAMAPi | MF_02225, CoaBC, 1 hit |
InterProi | View protein in InterPro IPR035929, CoaB-like_sf IPR005252, CoaBC IPR007085, DNA/pantothenate-metab_flavo_C IPR036551, Flavin_trans-like IPR003382, Flavoprotein |
Pfami | View protein in Pfam PF04127, DFP, 1 hit PF02441, Flavoprotein, 1 hit |
SUPFAMi | SSF102645, SSF102645, 1 hit SSF52507, SSF52507, 1 hit |
TIGRFAMsi | TIGR00521, coaBC_dfp, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | COABC_ECOLI | |
Accessioni | P0ABQ0Primary (citable) accession number: P0ABQ0 Secondary accession number(s): P24285, P76718, Q2M7V3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 8, 2005 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 125 of the entry and version 2 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