Coenzyme A biosynthesis bifunctional protein coaBC

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Reviewed, UniProtKB/Swiss-Prot P67733 (COABC_MYCTU)

Last modified June 16, 2009. Version 34. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Coenzyme A biosynthesis bifunctional protein coaBC
Alternative name(s):
    DNA/pantothenate metabolism flavoprotein
Including the following 2 domains:
    1- Recommended name:
            Phosphopantothenoylcysteine decarboxylase
                Short name=PPCDC
              EC=4.1.1.36
        Alternative name(s):
            CoaC
    2- Recommended name:
            Phosphopantothenate--cysteine ligase
              EC=6.3.2.5
        Alternative name(s):
            Phosphopantothenoylcysteine synthase
            PPC synthetase
              Short name=PPCS
            CoaB

Gene names

Name:	coaBC
Synonyms:	dfp
Ordered Locus Names:	Rv1391, MT1436
ORF Names:	MTCY21B4.08

Organism

Mycobacterium tuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

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Protein attributes

Sequence length	418 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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General annotation (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. 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. Cofactor biosynthesis; coenzyme A biosynthesis; coenzyme A from pantothenate: step 3/5.
Subunit structure	Homododecamer, the coaB domains form homodimers.
Sequence similarities	In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily. In the C-terminal section; belongs to the PPC synthetase family.

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Ontologies

Keywords
Ligand	FMN Flavoprotein
Molecular function	Decarboxylase Ligase Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	coenzyme A biosynthetic process Inferred from electronic annotation. Source: InterPro pantothenate catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro phosphopantothenate--cysteine ligase activity Inferred from electronic annotation. Source: EC phosphopantothenoylcysteine decarboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 418

418

Coenzyme A biosynthesis bifunctional protein coaBC

PRO_0000232694

Regions

Region

1 – 193

193

Phosphopantothenoylcysteine decarboxylase

Region

194 – 418

225

Phosphopantothenate--cysteine ligase

Sites

Binding site

285

CTP By similarity

Binding site

295

CTP By similarity

Binding site

354

CTP By similarity

Binding site

358

CTP By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P67733-1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 48BD95E536595506
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FASTA

418

43,577

        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

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References

[1]

"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.

Barrell B.G.
Nature 393:537-544(1998) [PubMed: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.

[2]

"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R.

Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.

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Cross-references

Sequence databases
	BX842576 Genomic DNA. Translation: CAB02174.1. AE000516 Genomic DNA. Translation: AAK45701.1.
PIR	E70899.
RefSeq	NP_215907.1. NP_335887.1.
3D structure databases
HSSP	HSSP built from PDB template 1MVN based on UniProtKB Q9SWE5.
ModBase	Search...
Genome annotation databases
GeneID	886749. 924547.
GenomeReviews	Gene locus MT1436 in contig AE000516_GR. Gene locus Rv1391 in contig AL123456_GR.
KEGG	mtc:MT1436. mtu:Rv1391.
TIGR	MT1436.
Organism-specific databases
TubercuList	Rv1391.
Phylogenomic databases
HOGENOM	P67733.
OMA	P67733. VTSGPTH.
Enzyme and pathway databases
BRENDA	4.1.1.36. 809. 6.3.2.5. 809.
Family and domain databases
InterPro	IPR005252. Bifunc_COABC. IPR007085. DNA/pantothenate-metab_flavo_C. IPR003382. Flavoprotein. [Graphical view]
Gene3D	G3DSA:3.40.50.10300. DNA/pantothenate-metab_flavo_C. 1 hit. G3DSA:3.40.50.1950. Flavoprotein. 1 hit.
Pfam	PF04127. DFP. 1 hit. PF02441. Flavoprotein. 1 hit. [Graphical view]
TIGRFAMs	TIGR00521. coaBC_dfp. 1 hit.
ProtoNet	Search...

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Entry information

Entry name

COABC_MYCTU

Accession

Primary (citable) accession number: P67733
Secondary accession number(s): P71661

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	June 16, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents