Phosphopantothenoylcysteine decarboxylase
     (PPCDC)
     (EC 4.1.1.36)
     (CoaC)
Phosphopantothenate--cysteine ligase
     (EC 6.3.2.5)
     (Phosphopantothenoylcysteine synthase)
     (PPC synthetase)
     (PPCS)
     (CoaB)

Gene name

	Name:	coaBC
	Synonyms:	dfp
	OrderedLocusNames:	Mb1426

From

Mycobacterium bovis

[TaxID: 1765]

[HAMAP proteome]

Taxonomy

Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-935 / AF2122/97;
DOI=10.1073/pnas.1130426100; PubMed=12788972 [NCBI, ExPASy, EBI, Israel, Japan]
Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
"The complete genome sequence of Mycobacterium bovis.";
Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).

Comments

FUNCTION: 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 (By similarity).
CATALYTIC ACTIVITY: N-((R)-4'-phosphopantothenoyl)-L-cysteine = pantotheine 4'-phosphate + CO₂.
CATALYTIC ACTIVITY: CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + PPi + N-((R)-4'-phosphopantothenoyl)-L-cysteine.
COFACTOR: Binds 1 FMN per subunit (By similarity).
PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; coenzyme A from pantothenate: step 2/5 .
PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; coenzyme A from pantothenate: step 3/5 .
SUBUNIT: Homododecamer, the coaB domains form homodimers.
SIMILARITY: In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily.
SIMILARITY: In the C-terminal section; belongs to the PPC synthetase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BX248338; CAD94287.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_855078.1; -.

3D structure databases

HSSP

Q9SWE5; 1MVN. [HSSP ENTRY / PDB]

ModBase

P67734.

Ontologies

GO:0010181;	Molecular function: FMN binding (inferred from electronic annotation from InterPro).
GO:0004632;	Molecular function: phosphopantothenate--cysteine ligase activity (inferred from electronic annotation from InterPro).
GO:0004633;	Molecular function: phosphopantothenoylcysteine decarboxylase activity (inferred from electronic annotation from InterPro).
GO:0015937;	Biological process: coenzyme A biosynthetic process (inferred from electronic annotation from InterPro).
GO:0015941;	Biological process: pantothenate catabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR005252; COABC.
IPR007085; DNA/pantothenate-metab_flavo_C.
IPR003382; Flavoprotein.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.10300; DNA/pantothenate-metab_flavo_C; 1.
G3DSA:3.40.50.1950; Flavoprotein; 1.

Pfam

PF04127; DFP; 1.
PF02441; Flavoprotein; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00521; coaBC_dfp; 1.

ProtoNet

P67734.

Genome annotation databases

GeneID

1090715; -.

GenomeReviews

BX248333_GR; Mb1426.

KEGG

mbo:Mb1426; -.

Phylogenomic databases

HOGENOM

P67734; -.

Genome annotation databases

CMR

P67734; Mb1426.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Decarboxylase; Flavoprotein; FMN; Ligase; Lyase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 418`	`418`	`Coenzyme A biosynthesis bifunctional protein coaBC.`	`PRO_0000232695`
`REGION`	`1 193`	`193`	`Phosphopantothenoylcysteine decarboxylase.`
`REGION`	`194 418`	`225`	`Phosphopantothenate--cysteine ligase.`
`BINDING`	`285 285`		`CTP (By similarity).`
`BINDING`	`295 295`		`CTP (By similarity).`
`BINDING`	`354 354`		`CTP (By similarity).`
`BINDING`	`358 358`		`CTP (By similarity).`

Sequence information

Length: 418 AA [This is the length of the unprocessed precursor]

Molecular weight: 43577 Da [This is the MW of the unprocessed precursor]

CRC64: 48BD95E536595506 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVDHKRIPKQ VIVGVSGGIA AYKACTVVRQ LTEASHRVRV IPTESALRFV GAATFEALSG 

        70         80         90        100        110        120 
EPVCTDVFAD VPAVPHVHLG QQADLVVVAP ATADLLARAA AGRADDLLTA TLLTARCPVL 

       130        140        150        160        170        180 
FAPAMHTEMW LHPATVDNVA TLRRRGAVVL EPATGRLTGA DSGAGRLPEA EEITTLAQLL 

       190        200        210        220        230        240 
LERHDALPYD LAGRKLLVTA GGTREPIDPV RFIGNRSSGK QGYAVARVAA QRGADVTLIA 

       250        260        270        280        290        300 
GHTAGLVDPA GVEVVHVSSA QQLADAVSKH APTADVLVMA AAVADFRPAQ VATAKIKKGV 

       310        320        330        340        350        360 
EGPPTIELLR NDDVLAGVVR ARAHGQLPNM RAIVGFAAET GDANGDVLFH ARAKLRRKGC 

       370        380        390        400        410 
DLLVVNAVGE GRAFEVDSND GWLLASDGTE SALQHGSKTL MASRIVDAIV TFLAGCSS

P67734 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools