Biotin carboxyl carrier protein of acetyl-CoA carboxylase

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Reviewed, UniProtKB/Swiss-Prot P0ABD8 (BCCP_ECOLI)

Last modified June 16, 2009. Version 35. 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:
Biotin carboxyl carrier protein of acetyl-CoA carboxylase
Short name=BCCP

Gene names

Name:	accB
Synonyms:	fabE
Ordered Locus Names:	b3255, JW3223

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	156 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subunit structure	Homodimer.
Sequence similarities	Contains 1 biotinyl-binding domain.

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Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Ligand	Biotin
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	acetyl-CoA carboxylase complex Inferred from electronic annotation. Source: InterPro
Molecular function	acetyl-CoA carboxylase activity Inferred from electronic annotation. Source: InterPro biotin binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 156

156

Biotin carboxyl carrier protein of acetyl-CoA carboxylase

PRO_0000146805

Regions

Domain

81 – 155

Biotinyl-binding

Amino acid modifications

Modified residue

122

N6-biotinyllysine

Experimental info

Sequence conflict

113

D → N Ref.2

Secondary structure

156

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0ABD8-1 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 05FFDCB912A683A3
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FASTA

156

16,687

        10         20         30         40         50         60 
MDIRKIKKLI ELVEESGISE LEISEGEESV RISRAAPAAS FPVMQQAYAA PMMQQPAQSN 

        70         80         90        100        110        120 
AAAPATVPSM EAPAAAEISG HIVRSPMVGT FYRTPSPDAK AFIEVGQKVN VGDTLCIVEA 

       130        140        150 
MKMMNQIEAD KSGTVKAILV ESGQPVEFDE PLVVIE

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the fabE gene and flanking regions containing a bent DNA sequence of Escherichia coli." Muramatsu S., Mizuno T. Nucleic Acids Res. 17:3982-3982(1989) [PubMed: 2660106] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"A rapid procedure for cloning genes from lambda libraries by complementation of E. coli defective mutants: application to the fabE region of the E. coli chromosome." Alix J.-H. DNA 8:779-789(1989) [PubMed: 2575489] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase." Li S.-J., Cronan J.E. Jr. J. Biol. Chem. 267:855-863(1992) [PubMed: 1370469] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[4]	"Cloning and characterization of the E. coli fabEG operon encoding subunits of acetyl-CoA carboxylase." Best E.A., Knauf V.C. Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis." Li S.-J., Cronan J.E. Jr. J. Bacteriol. 175:332-340(1993) [PubMed: 7678242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
[8]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed: 9600841] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-4. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]	"Amino acid sequence of Escherichia coli biotin carboxyl carrier protein (9100)." Sutton M.R., Fall R.R., Nervi A.M., Alberts A.W., Vagelos P.R., Bradshaw R.A. J. Biol. Chem. 252:3934-3940(1977) [PubMed: 324999] [Abstract] Cited for: PROTEIN SEQUENCE OF 75-156.
[10]	"Acetyl-CoA carboxylase from Escherichia coli: gene organization and nucleotide sequence of the biotin carboxylase subunit." Kondo H., Shiratsuchi K., Yoshimoto T., Masuda T., Kitazono A., Tsuru D., Anai M., Sekiguchi M., Tanabe T. Proc. Natl. Acad. Sci. U.S.A. 88:9730-9733(1991) [PubMed: 1682920] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-156. Strain: K12.
[11]	"Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing." Athappilly F.K., Hendrickson W.A. Structure 3:1407-1419(1995) [PubMed: 8747466] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 77-156.
[12]	"Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase." Yao X., Wei D., Soden C. Jr., Summers M.F., Beckett D. Biochemistry 36:15089-15100(1997) [PubMed: 9398236] [Abstract] Cited for: STRUCTURE BY NMR OF 70-156.
[13]	"Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy." Roberts E.L., Shu N., Howard M.J., Broadhurst R.W., Chapman-Smith A., Wallace J.C., Morris T., Cronan J.E. Jr., Perham R.N. Biochemistry 38:5045-5053(1999) [PubMed: 10213607] [Abstract] Cited for: STRUCTURE BY NMR OF 77-156.

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Cross-references

Sequence databases

X14825 Genomic DNA. Translation: CAA32933.1.
M80458 Genomic DNA. Translation: AAA23408.1.
M32214 Genomic DNA. Translation: AAA23744.1.
M83198 Genomic DNA. Translation: AAA23745.1.
U18997 Genomic DNA. Translation: AAA58058.1.
U00096 Genomic DNA. Translation: AAC76287.1.
AP009048 Genomic DNA. Translation: BAE77296.1.
S52932 mRNA. Translation: AAB24892.1.
M79446 Genomic DNA. No translation available.

PIR

BKEC9. A93687.

RefSeq

AP_003795.1.
NP_417721.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A6X	NMR	-	A	70-156	[»]
1BDO	X-ray	1.80	A	77-156	[»]
1K67	model	-	B	77-155	[»]
1K69	model	-	B	77-156	[»]
2BDO	NMR	-	A	77-156	[»]
3BDO	NMR	-	A	75-156	[»]

DisProt

DP00415.

ModBase

Search...

2-D gel databases

SWISS-2DPAGE

P0ABD8.

Genome annotation databases

GeneID

947758.

GenomeReviews

Gene locus JW3223 in contig AP009048_GR.
Gene locus b3255 in contig U00096_GR.

KEGG

ecj:JW3223.
eco:b3255.

Organism-specific databases

EchoBASE

EB0271.

EcoGene

EG10275. accB.

CMR

Search...

Phylogenomic databases

HOGENOM

P0ABD8.

OMA

P0ABD8. ALCIVEA.

Enzyme and pathway databases

BioCyc

EcoCyc:BCCP-MON.

Family and domain databases

InterPro

IPR001249. AcCoA_biotinCC.
IPR001882. Biotin_BS.
IPR000089. Biotin_lipoyl.
[Graphical view]

Pfam

PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]

PRINTS

PR01071. ACOABIOTINCC.

TIGRFAMs

TIGR00531. BCCP. 1 hit.

PROSITE

PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

BCCP_ECOLI

Accession

Primary (citable) accession number: P0ABD8
Secondary accession number(s): P02905, Q2M8W0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 25, 2005
Last modified:	June 16, 2009
This is version 35 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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