Reviewed, UniProtKB/Swiss-Prot P0A508 (BCCA_MYCTU)

Names and origin

Protein names

Recommended name:
    Acetyl-/propionyl-coenzyme A carboxylase alpha chain
Including the following 2 domains:
    1- Recommended name:
            Biotin carboxylase
              EC=6.3.4.14
    2- Recommended name:
            Biotin carboxyl carrier protein
                Short name=BCCP

Gene names

Name:	accA1
Synonyms:	bccA
Ordered Locus Names:	Rv2501c, MT2576
ORF Names:	MTCY07A7.07c

Organism

Mycobacterium tuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	654 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	This protein carries two functions: biotin carboxyl carrier protein and biotin carboxyltransferase By similarity.
Catalytic activity	ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein.
Cofactor	Biotin.
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subunit structure	Multimer comprised of 2 different subunits, the larger one (63/64 kDa) has biotin carboxylase and biotin carrier functions, while the smaller subunit possesses carboxyltransferase and substrate binding activity By similarity.
Sequence similarities	Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain. Contains 1 biotinyl-binding domain.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Ligand	ATP-binding Biotin Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW biotin binding Inferred from electronic annotation. Source: InterPro biotin carboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 654	654	Acetyl-/propionyl-coenzyme A carboxylase alpha chain		PRO_0000146798
Regions
	Domain	1 – 448	448	Biotin carboxylation
	Domain	120 – 319	200	ATP-grasp
	Domain	586 – 652	67	Biotinyl-binding
Sites
	Active site	294	1	By similarity
	Binding site	116	1	ATP By similarity
	Binding site	200	1	ATP By similarity
	Binding site	235	1	ATP By similarity
Amino acid modifications
	Modified residue	620	1	N6-biotinyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A508-1 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: FAA0A1A46432CABF	FASTA	654	70,592
	10 20 30 40 50 60 MFDTVLVANR GEIAVRVIRT LRRLGIRSVA VYSDPDVDAR HVLEADAAVR LGPAPARESY 70 80 90 100 110 120 LDIGKVLDAA ARTGAQAIHP GYGFLAENAD FAAACERARV VFLGPPARAI EVMGDKIAAK 130 140 150 160 170 180 NAVAAFDVPV VPGVARAGLT DDALVTAAAE VGYPVLIKPS AGGGGKGMRL VQDPARLPEA 190 200 210 220 230 240 LVSARREAMS SFGDDTLFLE RFVLRPRHIE VQVLADAHGN VVHLGERECS LQRRHQKVIE 250 260 270 280 290 300 EAPSPLLDPQ TRERIGVAAC NTARCVDYVG AGTVEFIVSA QRPDEFFFME MNTRLQVEHP 310 320 330 340 350 360 VTEAITGLDL VEWQLRVGAG EKLGFAQNDI ELRGHAIEAR VYAEDPAREF LPTGGRVLAV 370 380 390 400 410 420 FEPAGPGVRV DSSLLGGTVV GSDYDPLLTK VIAHGADREE ALDRLDQALA RTAVLGVQTN 430 440 450 460 470 480 VEFLRFLLAD ERVRVGDLDT AVLDERSADF TARPAPDDVL AAGGLYRQWA LARRAQGDLW 490 500 510 520 530 540 AAPSGWRGGG HMAPVRTAMR TPLRSETVSV WGPPESAQVQ VGDGEIDCAS VQVTREQMSV 550 560 570 580 590 600 TISGLRRDYR WAEADRHLWI ADERGTWHLR EAEEHKIHRA VGARPAEVVS PMPGSVIAVQ 610 620 630 640 650 VESGSQISAG DVVVVVEAMK MEHSLEAPVS GRVQVLVSVG DQVKVEQVLA RIKD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Lipid synthesis in mycobacteria: characterization of the biotin carboxyl carrier protein genes from Mycobacterium leprae and M. tuberculosis." Norman E., de Smet K.A.L., Stoker N.G., Ratledge C., Wheeler P.R., Dale J.W. J. Bacteriol. 176:2525-2531(1994) [PubMed: 7909542] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Isolate 50410.
[2]	"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.
[3]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z19549 Genomic DNA. Translation: CAA79609.1. BX842580 Genomic DNA. Translation: CAB08919.1. AE000516 Genomic DNA. Translation: AAK46880.1.
PIR	B55579.
RefSeq	NP_217017.1. NP_337066.1.
3D structure databases
HSSP	HSSP built from PDB template 1BNC based on UniProtKB P24182.
ModBase	Search...
Genome annotation databases
GeneID	887309. 925752.
GenomeReviews	Gene locus MT2576 in contig AE000516_GR. Gene locus Rv2501c in contig AL123456_GR.
KEGG	mtc:MT2576. mtu:Rv2501c.
TIGR	MT2576.
Organism-specific databases
TubercuList	Rv2501c.
Phylogenomic databases
HOGENOM	P0A508.
OMA	TWHIREA.
Enzyme and pathway databases
BRENDA	6.3.4.14. 809.
Family and domain databases
InterPro	IPR011761. ATP-grasp. IPR013816. ATP_grasp_subdomain_2. IPR011764. BC. IPR001882. Biotin_BS. IPR005482. Biotin_COase_C. IPR000089. Biotin_lipoyl. IPR005479. CarbamoylP_synth_lsu_ATP-bd. IPR005481. CarbamoylP_synth_lsu_N. IPR013817. Pre-ATP_grasp. [Graphical view]
Gene3D	G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
Pfam	PF02785. Biotin_carb_C. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF00289. CPSase_L_chain. 1 hit. PF02786. CPSase_L_D2. 1 hit. [Graphical view]
PROSITE	PS50975. ATP_GRASP. 1 hit. PS50979. BC. 1 hit. PS00188. BIOTIN. 1 hit. PS50968. BIOTINYL_LIPOYL. 1 hit. PS00866. CPSASE_1. 1 hit. PS00867. CPSASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BCCA_MYCTU

Accession

Primary (citable) accession number: P0A508
Secondary accession number(s): P46401

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	November 3, 2009
This is version 31 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)