coaBC

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:

Pantothenate kinase (coaA)
Coenzyme A biosynthesis bifunctional protein CoaBC (coaBC)
Coenzyme A biosynthesis bifunctional protein CoaBC (coaBC)
Phosphopantetheine adenylyltransferase (coaD)
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 key	Position(s)	DescriptionActions	Length
Binding siteⁱ	125	SubstrateBy similarity	1
Active siteⁱ	158	Proton donorCurated	1
Binding siteⁱ	279	CTPCombined sources1 Publication	1
Binding siteⁱ	289	CTPCombined sources1 Publication	1
Binding siteⁱ	327	CTP; via amide nitrogenCombined sources1 Publication	1
Binding siteⁱ	341	CTPCombined sources1 Publication	1
Binding siteⁱ	345	CTPCombined sources1 Publication	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	273 – 275	CTPCombined sources1 Publication		3
Nucleotide bindingⁱ	308 – 311	CTPCombined sources1 Publication		4

GO - Molecular functionⁱ

FMN binding
Source: EcoCyc
Inferred from direct assayⁱ
- 10922366
- 2999089
metal ion binding Source: UniProtKB-KW
phosphopantothenate--cysteine ligase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 11278255
phosphopantothenoylcysteine decarboxylase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 10922366

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

coenzyme A biosynthetic process
Source: EcoCyc
Inferred from direct assayⁱ
- 11278255
pantothenate catabolic process Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Decarboxylase, Ligase, Lyase, Multifunctional enzyme
Ligand	Flavoprotein, FMN, Magnesium, Metal-binding

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10004-MONOMER MetaCyc: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 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
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10004 dfp

EcoGeneⁱ

EG10004 dfp

Subcellular locationⁱ

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 15911532
- 18304323

View the complete GO annotation on QuickGO ...

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	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

Drug and drug target database More...DrugBankⁱ	DB03403 Cytidine-5'-Monophosphate DB02431 Cytidine-5'-Triphosphate

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

EPDⁱ	P0ABQ0
PaxDbⁱ	P0ABQ0
PRIDEⁱ	P0ABQ0

Interactionⁱ

Subunit structureⁱ

Homododecamer, the CoaB domains form homodimers.

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
rplA	P0A7L0	2	EBI-548929,EBI-543771
rpoA	P0A7Z4	2	EBI-548929,EBI-544985

Protein-protein interaction databases

BioGridⁱ	4261256, 26 interactors
Database of interacting proteins More...DIPⁱ	DIP-48472N
IntActⁱ	P0ABQ0, 2 interactors
STRINGⁱ	316385.ECDH10B_3821

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	185 – 188	Combined sources	4
Beta strandⁱ	190 – 197	Combined sources	8
Beta strandⁱ	199 – 210	Combined sources	12
Helixⁱ	215 – 226	Combined sources	12
Beta strandⁱ	230 – 235	Combined sources	6
Beta strandⁱ	246 – 250	Combined sources	5
Helixⁱ	254 – 264	Combined sources	11
Helixⁱ	265 – 267	Combined sources	3
Beta strandⁱ	269 – 273	Combined sources	5
Beta strandⁱ	279 – 284	Combined sources	6
Beta strandⁱ	299 – 306	Combined sources	8
Helixⁱ	310 – 316	Combined sources	7
Beta strandⁱ	318 – 320	Combined sources	3
Beta strandⁱ	323 – 333	Combined sources	11
Helixⁱ	334 – 345	Combined sources	12
Beta strandⁱ	348 – 354	Combined sources	7
Beta strandⁱ	364 – 373	Combined sources	10
Beta strandⁱ	376 – 384	Combined sources	9
Helixⁱ	385 – 403	Combined sources	19

Show more details

3D structure databases

ProteinModelPortalⁱ	P0ABQ0
SMRⁱ	P0ABQ0
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P0ABQ0

EvolutionaryTraceⁱ

P0ABQ0

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	2 – 188	Phosphopantothenoylcysteine decarboxylaseAdd BLAST		187
Regionⁱ	189 – 406	Phosphopantothenate--cysteine ligaseAdd BLAST		218

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

eggNOGⁱ	ENOG4105CJS Bacteria COG0452 LUCA
HOGENOMⁱ	HOG000037526
InParanoidⁱ	P0ABQ0
KEGG Orthology (KO) More...KOⁱ	K13038
OMAⁱ	WEHPATQ
PhylomeDBⁱ	P0ABQ0

Family and domain databases

Gene3Dⁱ	3.40.50.10300, 1 hit 3.40.50.1950, 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
Pfam protein domain database More...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

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P0ABQ0-1 [UniParc]FASTA Add 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.
NCBI Reference Sequences More...RefSeqⁱ	NP_418096.4, NC_000913.3 WP_000050139.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76663; AAC76663; b3639 BAE77653; BAE77653; BAE77653
GeneIDⁱ	949047
KEGGⁱ	ecj:JW5642 eco:b3639
PATRICⁱ	fig\|1411691.4.peg.3067

Protein	Similar proteins		Species	Score	Length	Source
P0ABQ0	Coenzyme A biosynthesis bifunctional protein CoaBC		ECOL6		406	UniRef100_P0ABQ1
Coenzyme A biosynthesis bifunctional protein CoaBC		ECOLX		430
Coenzyme A biosynthesis bifunctional protein CoaBC		ECO57		430
Coenzyme A biosynthesis bifunctional protein CoaBC		Escherichia coli H386		430
Coenzyme A biosynthesis bifunctional protein CoaBC		SHIFL		430
+113

Protein	Similar proteins		Species	Score	Length	Source
P0ABQ0	Coenzyme A biosynthesis bifunctional protein CoaBC		ECOL6		406	UniRef90_P0ABQ1
Coenzyme A biosynthesis bifunctional protein CoaBC		ECOLX		430
Coenzyme A biosynthesis bifunctional protein CoaBC		ECO57		430
Coenzyme A biosynthesis bifunctional protein CoaBC		Escherichia coli H386		430
Coenzyme A biosynthesis bifunctional protein CoaBC		SHIFL		430
+242

Protein	Similar proteins		Species	Score	Length	Source
P0ABQ0	Coenzyme A biosynthesis bifunctional protein CoaBC		ECOL6		406	UniRef50_P0ABQ1
Coenzyme A biosynthesis bifunctional protein CoaBC		ECOLX		430
Coenzyme A biosynthesis bifunctional protein CoaBC		ECO57		430
Coenzyme A biosynthesis bifunctional protein CoaBC		Escherichia coli H386		430
Coenzyme A biosynthesis bifunctional protein CoaBC		SHIFL		430
+625

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:	March 28, 2018
	This is version 104 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, Complete proteome, Direct protein sequencing, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0ABQ0 (COABC_ECOLI)

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Coenzyme A biosynthesis bifunctional protein CoaBC

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: coenzyme A biosynthesis

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Sequence databases

Genome annotation databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Pathwayⁱ: coenzyme A biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ