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Protein

Coenzyme A biosynthesis bifunctional protein CoaBC

Gene

coaBC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine.

Catalytic activityi

N-((R)-4'-phosphopantothenoyl)-L-cysteine = pantotheine 4'-phosphate + CO2.
CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-((R)-4'-phosphopantothenoyl)-L-cysteine.

Cofactori

Protein has several cofactor binding sites:
  • Mg2+
  • FMNNote: Binds 1 FMN per subunit.

Pathwayi: coenzyme A biosynthesis

This protein is involved in step 2 and 3 of the subpathway that synthesizes CoA from (R)-pantothenate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Pantothenate kinase (coaA)
  2. Coenzyme A biosynthesis bifunctional protein CoaBC (coaBC)
  3. Coenzyme A biosynthesis bifunctional protein CoaBC (coaBC)
  4. Phosphopantetheine adenylyltransferase (coaD)
  5. Dephospho-CoA kinase (coaE)
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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei125SubstrateBy similarity1
Active sitei158Proton donorCurated1
Binding sitei279CTP1
Binding sitei289CTP1
Binding sitei341CTP1
Binding sitei345CTP1

GO - Molecular functioni

  • FMN 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

Keywords - Molecular functioni

Decarboxylase, Ligase, Lyase

Keywords - Ligandi

Flavoprotein, FMN, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10004-MONOMER.
ECOL316407:JW5642-MONOMER.
MetaCyc:EG10004-MONOMER.
BRENDAi6.3.2.5. 2026.
SABIO-RKP0ABQ0.
UniPathwayiUPA00241; UER00353.
UPA00241; UER00354.

Names & Taxonomyi

Protein namesi
Recommended name:
Coenzyme A biosynthesis bifunctional protein CoaBC
Alternative name(s):
DNA/pantothenate metabolism flavoprotein
Including the following 2 domains:
Phosphopantothenoylcysteine decarboxylase (EC:4.1.1.36)
Short name:
PPCDC
Alternative name(s):
CoaC
Phosphopantothenate--cysteine ligase (EC:6.3.2.5)
Alternative name(s):
CoaB
PPC synthetase
Short name:
PPCS
Phosphopantothenoylcysteine synthase
Gene namesi
Name:coaBC
Synonyms:dfp
Ordered Locus Names:b3639, JW5642
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10004. dfp.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi11G → D in Dfp-707; temperature-sensitive, impairs folding. 1 Publication1
Mutagenesisi14G → S: No FMN binding. 1 Publication1
Mutagenesisi15G → A: Less than 5% of wild-type activity. 1 Publication1
Mutagenesisi16I → L: Severely reduced activity. 1 Publication1
Mutagenesisi16I → V: Slightly reduced activity. 1 Publication1
Mutagenesisi17A → D: Less than 5% of wild-type activity. 1 Publication1
Mutagenesisi17A → G or S: Almost wild-type activity. 1 Publication1
Mutagenesisi19Y → F: Almost wild-type activity. 1 Publication1
Mutagenesisi19Y → L: Reduced activity. 1 Publication1
Mutagenesisi20K → N or Q: Reduced activity. 1 Publication1
Mutagenesisi20K → R: Almost wild-type activity. 1 Publication1
Mutagenesisi46F → L: Reduced activity. 1 Publication1
Mutagenesisi75H → N: Loss of activity. 1 Publication1
Mutagenesisi89P → A: Binds FMN, but more loosely than wild-type. 1 Publication1
Mutagenesisi89P → D: No FMN binding. 1 Publication1
Mutagenesisi91T → V: Binds FMN. 1 Publication1
Mutagenesisi124M → L: No effect. 1 Publication1
Mutagenesisi125N → D or Q: Loss of activity. 2 Publications1
Mutagenesisi128M → L: Severely reduced activity. 1 Publication1
Mutagenesisi158C → A or S: Loss of activity. 1
Mutagenesisi194T → V: Loss of dimerization. 1 Publication1
Mutagenesisi198T → V: Loss of dimerization. 1 Publication1
Mutagenesisi203D → N: Loss of dimerization. 1 Publication1
Mutagenesisi210N → D: Loss of activity, reaction intermediate detectable. 2 Publications1
Mutagenesisi210N → H or K: Loss of activity, reaction intermediate not detectable. 2 Publications1
Mutagenesisi212S → A: Small effect on activity. 1 Publication1
Mutagenesisi215K → Q: No effect. 1 Publication1
Mutagenesisi275A → V: Loss of dimerization. 2 Publications1
Mutagenesisi289K → Q: Loss of activity. 1 Publication1
Mutagenesisi291K → Q: Reduced activity. 1 Publication1
Mutagenesisi292K → Q: Small effect on activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001820222 – 406Coenzyme A biosynthesis bifunctional protein CoaBCAdd BLAST405

Proteomic databases

EPDiP0ABQ0.
PaxDbiP0ABQ0.
PRIDEiP0ABQ0.

Interactioni

Subunit structurei

Homododecamer, the CoaB domains form homodimers.

Protein-protein interaction databases

DIPiDIP-48472N.
IntActiP0ABQ0. 2 interactors.
STRINGi511145.b3639.

Structurei

Secondary structure

1406
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni185 – 188Combined sources4
Beta strandi190 – 197Combined sources8
Beta strandi199 – 210Combined sources12
Helixi215 – 226Combined sources12
Beta strandi230 – 235Combined sources6
Beta strandi246 – 250Combined sources5
Helixi254 – 264Combined sources11
Helixi265 – 267Combined sources3
Beta strandi269 – 273Combined sources5
Beta strandi279 – 284Combined sources6
Beta strandi299 – 306Combined sources8
Helixi310 – 316Combined sources7
Beta strandi318 – 320Combined sources3
Beta strandi323 – 333Combined sources11
Helixi334 – 345Combined sources12
Beta strandi348 – 354Combined sources7
Beta strandi364 – 373Combined sources10
Beta strandi376 – 384Combined sources9
Helixi385 – 403Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U7UX-ray2.40A181-406[»]
1U7WX-ray2.50A/B/C181-406[»]
1U7ZX-ray2.30A/B/C181-406[»]
1U80X-ray2.85A/B/C181-406[»]
ProteinModelPortaliP0ABQ0.
SMRiP0ABQ0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABQ0.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 188Phosphopantothenoylcysteine decarboxylaseAdd BLAST187
Regioni189 – 406Phosphopantothenate--cysteine ligaseAdd BLAST218

Sequence similaritiesi

In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily.Curated
In the C-terminal section; belongs to the PPC synthetase family.Curated

Phylogenomic databases

eggNOGiENOG4105CJS. Bacteria.
COG0452. LUCA.
HOGENOMiHOG000037526.
InParanoidiP0ABQ0.
KOiK13038.
OMAiVVFAPAM.
PhylomeDBiP0ABQ0.

Family and domain databases

Gene3Di3.40.50.10300. 1 hit.
3.40.50.1950. 1 hit.
InterProiIPR005252. CoaBC.
IPR007085. DNA/pantothenate-metab_flavo_C.
IPR003382. Flavoprotein.
[Graphical view]
PfamiPF04127. DFP. 1 hit.
PF02441. Flavoprotein. 1 hit.
[Graphical view]
SUPFAMiSSF102645. SSF102645. 1 hit.
SSF52507. SSF52507. 1 hit.
TIGRFAMsiTIGR00521. coaBC_dfp. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0ABQ0-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:406
Mass (Da):43,438
Last modified:January 23, 2007 - v2
Checksum:iCBD11B9347E8C6AB
GO

Sequence cautioni

The sequence AAA61992 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.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.
RefSeqiNP_418096.4. NC_000913.3.
WP_000050139.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76663; AAC76663; b3639.
BAE77653; BAE77653; BAE77653.
GeneIDi949047.
KEGGiecj:JW5642.
eco:b3639.
PATRICi32122765. VBIEscCol129921_3759.

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.
RefSeqiNP_418096.4. NC_000913.3.
WP_000050139.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U7UX-ray2.40A181-406[»]
1U7WX-ray2.50A/B/C181-406[»]
1U7ZX-ray2.30A/B/C181-406[»]
1U80X-ray2.85A/B/C181-406[»]
ProteinModelPortaliP0ABQ0.
SMRiP0ABQ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48472N.
IntActiP0ABQ0. 2 interactors.
STRINGi511145.b3639.

Proteomic databases

EPDiP0ABQ0.
PaxDbiP0ABQ0.
PRIDEiP0ABQ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76663; AAC76663; b3639.
BAE77653; BAE77653; BAE77653.
GeneIDi949047.
KEGGiecj:JW5642.
eco:b3639.
PATRICi32122765. VBIEscCol129921_3759.

Organism-specific databases

EchoBASEiEB0004.
EcoGeneiEG10004. dfp.

Phylogenomic databases

eggNOGiENOG4105CJS. Bacteria.
COG0452. LUCA.
HOGENOMiHOG000037526.
InParanoidiP0ABQ0.
KOiK13038.
OMAiVVFAPAM.
PhylomeDBiP0ABQ0.

Enzyme and pathway databases

UniPathwayiUPA00241; UER00353.
UPA00241; UER00354.
BioCyciEcoCyc:EG10004-MONOMER.
ECOL316407:JW5642-MONOMER.
MetaCyc:EG10004-MONOMER.
BRENDAi6.3.2.5. 2026.
SABIO-RKP0ABQ0.

Miscellaneous databases

EvolutionaryTraceiP0ABQ0.
PROiP0ABQ0.

Family and domain databases

Gene3Di3.40.50.10300. 1 hit.
3.40.50.1950. 1 hit.
InterProiIPR005252. CoaBC.
IPR007085. DNA/pantothenate-metab_flavo_C.
IPR003382. Flavoprotein.
[Graphical view]
PfamiPF04127. DFP. 1 hit.
PF02441. Flavoprotein. 1 hit.
[Graphical view]
SUPFAMiSSF102645. SSF102645. 1 hit.
SSF52507. SSF52507. 1 hit.
TIGRFAMsiTIGR00521. coaBC_dfp. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCOABC_ECOLI
AccessioniPrimary (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: November 2, 2016
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.