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Protein

Coenzyme A biosynthesis bifunctional protein CoaBC

Gene

coaBC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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 (PubMed:11278255). In the second the latter compound is decarboxylated to form 4'-phosphopantotheine (PubMed:10922366).2 Publications

Catalytic activityi

N-((R)-4'-phosphopantothenoyl)-L-cysteine = pantotheine 4'-phosphate + CO2.1 Publication
CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-((R)-4'-phosphopantothenoyl)-L-cysteine.1 Publication

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.1 Publication
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 sitei279CTPCombined sources1 Publication1
Binding sitei289CTPCombined sources1 Publication1
Binding sitei327CTP; via amide nitrogenCombined sources1 Publication1
Binding sitei341CTPCombined sources1 Publication1
Binding sitei345CTPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi273 – 275CTPCombined sources1 Publication3
Nucleotide bindingi308 – 311CTPCombined sources1 Publication4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDecarboxylase, Ligase, Lyase, Multifunctional enzyme
LigandFlavoprotein, FMN, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10004-MONOMER
MetaCyc:EG10004-MONOMER
BRENDAi6.3.2.5 2026
SABIO-RKiP0ABQ0
UniPathwayi
UPA00241;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:4.1.1.361 Publication)
Short name:
PPCDC
Alternative name(s):
CoaC
Phosphopantothenate--cysteine ligase (EC:6.3.2.51 Publication)
Alternative name(s):
CoaB
PPC synthetase
Short name:
PPCS
Phosphopantothenoylcysteine synthase
Gene namesi
Name:coaBC1 Publication
Synonyms:dfp1 Publication
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

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

Chemistry databases

DrugBankiDB03403 Cytidine-5'-Monophosphate
DB02431 Cytidine-5'-Triphosphate

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.

Binary interactionsi

Protein-protein interaction databases

BioGridi4261256, 26 interactors
DIPiDIP-48472N
IntActiP0ABQ0, 2 interactors
STRINGi316385.ECDH10B_3821

Structurei

Secondary structure

1406
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
OMAiWEHPATQ
PhylomeDBiP0ABQ0

Family and domain databases

Gene3Di3.40.50.10300, 1 hit
3.40.50.1950, 1 hit
InterProiView protein in InterPro
IPR035929 CoaB-like_sf
IPR005252 CoaBC
IPR007085 DNA/pantothenate-metab_flavo_C
IPR036551 Flavin_trans-like
IPR003382 Flavoprotein
PfamiView protein in Pfam
PF04127 DFP, 1 hit
PF02441 Flavoprotein, 1 hit
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
PATRICifig|1411691.4.peg.3067

Similar proteinsi

Entry informationi

Entry nameiCOABC_ECOLI
AccessioniPrimary (citable) accession number: P0ABQ0
Secondary accession number(s): P24285, P76718, Q2M7V3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 104 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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