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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei125 – 1251SubstrateBy similarity
Active sitei158 – 1581Proton donorCurated
Binding sitei279 – 2791CTP
Binding sitei289 – 2891CTP
Binding sitei341 – 3411CTP
Binding sitei345 – 3451CTP

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111G → D in Dfp-707; temperature-sensitive, impairs folding. 1 Publication
Mutagenesisi14 – 141G → S: No FMN binding. 1 Publication
Mutagenesisi15 – 151G → A: Less than 5% of wild-type activity. 1 Publication
Mutagenesisi16 – 161I → L: Severely reduced activity. 1 Publication
Mutagenesisi16 – 161I → V: Slightly reduced activity. 1 Publication
Mutagenesisi17 – 171A → D: Less than 5% of wild-type activity. 1 Publication
Mutagenesisi17 – 171A → G or S: Almost wild-type activity. 1 Publication
Mutagenesisi19 – 191Y → F: Almost wild-type activity. 1 Publication
Mutagenesisi19 – 191Y → L: Reduced activity. 1 Publication
Mutagenesisi20 – 201K → N or Q: Reduced activity. 1 Publication
Mutagenesisi20 – 201K → R: Almost wild-type activity. 1 Publication
Mutagenesisi46 – 461F → L: Reduced activity. 1 Publication
Mutagenesisi75 – 751H → N: Loss of activity. 1 Publication
Mutagenesisi89 – 891P → A: Binds FMN, but more loosely than wild-type. 1 Publication
Mutagenesisi89 – 891P → D: No FMN binding. 1 Publication
Mutagenesisi91 – 911T → V: Binds FMN. 1 Publication
Mutagenesisi124 – 1241M → L: No effect. 1 Publication
Mutagenesisi125 – 1251N → D or Q: Loss of activity. 2 Publications
Mutagenesisi128 – 1281M → L: Severely reduced activity. 1 Publication
Mutagenesisi158 – 1581C → A or S: Loss of activity.
Mutagenesisi194 – 1941T → V: Loss of dimerization. 1 Publication
Mutagenesisi198 – 1981T → V: Loss of dimerization. 1 Publication
Mutagenesisi203 – 2031D → N: Loss of dimerization. 1 Publication
Mutagenesisi210 – 2101N → D: Loss of activity, reaction intermediate detectable. 2 Publications
Mutagenesisi210 – 2101N → H or K: Loss of activity, reaction intermediate not detectable. 2 Publications
Mutagenesisi212 – 2121S → A: Small effect on activity. 1 Publication
Mutagenesisi215 – 2151K → Q: No effect. 1 Publication
Mutagenesisi275 – 2751A → V: Loss of dimerization. 2 Publications
Mutagenesisi289 – 2891K → Q: Loss of activity. 1 Publication
Mutagenesisi291 – 2911K → Q: Reduced activity. 1 Publication
Mutagenesisi292 – 2921K → Q: Small effect on activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 406405Coenzyme A biosynthesis bifunctional protein CoaBCPRO_0000182022Add
BLAST

Proteomic databases

EPDiP0ABQ0.
PaxDbiP0ABQ0.
PRIDEiP0ABQ0.

Interactioni

Subunit structurei

Homododecamer, the CoaB domains form homodimers.

Protein-protein interaction databases

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

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni185 – 1884Combined sources
Beta strandi190 – 1978Combined sources
Beta strandi199 – 21012Combined sources
Helixi215 – 22612Combined sources
Beta strandi230 – 2356Combined sources
Beta strandi246 – 2505Combined sources
Helixi254 – 26411Combined sources
Helixi265 – 2673Combined sources
Beta strandi269 – 2735Combined sources
Beta strandi279 – 2846Combined sources
Beta strandi299 – 3068Combined sources
Helixi310 – 3167Combined sources
Beta strandi318 – 3203Combined sources
Beta strandi323 – 33311Combined sources
Helixi334 – 34512Combined sources
Beta strandi348 – 3547Combined sources
Beta strandi364 – 37310Combined sources
Beta strandi376 – 3849Combined sources
Helixi385 – 40319Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 8-145, 181-405.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABQ0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 188187Phosphopantothenoylcysteine decarboxylaseAdd
BLAST
Regioni189 – 406218Phosphopantothenate--cysteine ligaseAdd
BLAST

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
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. Positions 8-145, 181-405.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48472N.
IntActiP0ABQ0. 2 interactions.
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: September 7, 2016
This is version 93 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.