P67733 (COABC_MYCTU) Reviewed, UniProtKB/Swiss-Prot

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. Phosphopantothenoylcysteine decarboxylase
   Short name=PPCDC
   EC=4.1.1.36
   Alternative name(s):
   CoaC
2. Phosphopantothenate--cysteine ligase
   EC=6.3.2.5
   Alternative name(s):
   CoaB
   PPC synthetase
   Short name=PPCS
   Phosphopantothenoylcysteine synthase

Gene names

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

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	418 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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; CoA from (R)-pantothenate: step 2/5. Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5.
Subunit structure	Homododecamer, the CoaB domains form homodimers.
Miscellaneous	Was identified as a high-confidence drug target.
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.

Ontologies

Keywords
Ligand	FMN Flavoprotein
Molecular function	Decarboxylase Ligase Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	coenzyme A biosynthetic process Inferred from direct assay. Source: MTBBASE growth Inferred from mutant phenotype. Source: MTBBASE pantothenate catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	plasma membrane Inferred from direct assay. Source: MTBBASE
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 direct assay. Source: MTBBASE
Complete GO annotation...

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	1	CTP By similarity
	Binding site	295	1	CTP By similarity
	Binding site	354	1	CTP By similarity
	Binding site	358	1	CTP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P67733 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 48BD95E536595506	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

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. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., 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. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis." Raman K., Yeturu K., Chandra N. BMC Syst. Biol. 2:109-109(2008) [PubMed: 19099550] [Abstract] Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842576 Genomic DNA. Translation: CAB02174.1. AE000516 Genomic DNA. Translation: AAK45701.1.
PIR	E70899.
RefSeq	NP_215907.1. NC_000962.2. NP_335887.1. NC_002755.2.
3D structure databases
ProteinModelPortal	P67733.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000001175; EBMYCP00000001175; EBMYCG00000001175. EBMYCT00000071608; EBMYCP00000069667; EBMYCG00000071603.
GeneID	886749. 924547.
GenomeReviews	Gene locus MT1436 in contig AE000516_GR. Gene locus Rv1391 in contig AL123456_GR.
KEGG	mtc:MT1436. mtu:Rv1391.
PATRIC	18124926. VBIMycTub22151_1577.
TIGR	MT1436.
Organism-specific databases
TubercuList	Rv1391.
Phylogenomic databases
GeneTree	EBGT00050000017596.
HOGENOM	HBG523890.
OMA	VTSGPTH.
PhylomeDB	P67733.
ProtClustDB	PRK05579.
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.
KO	K13038.
Pfam	PF04127. DFP. 1 hit. PF02441. Flavoprotein. 1 hit. [Graphical view]
SUPFAM	SSF102645. DNA/pantothenate-metab_flavo_C. 1 hit. SSF52507. Flavoprotein. 1 hit.
TIGRFAMs	TIGR00521. CoaBC_dfp. 1 hit.
ProtoNet	Search...

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:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program