Biotin carboxylase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P24182 (ACCC_ECOLI)

Last modified June 16, 2009. Version 101. History...

Clusters with 100%, 90%, 50% identity |

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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 carboxylase
    EC=6.3.4.14
Alternative name(s):
    Acetyl-CoA carboxylase subunit A
      Short name=ACC
    EC=6.4.1.2

Gene names

Name:	accC
Synonyms:	fabG
Ordered Locus Names:	b3256, JW3224

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	449 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.
Catalytic activity	ATP + biotin-carboxyl-carrier protein + CO₂ = ADP + phosphate + carboxybiotin-carboxyl-carrier protein. ATP + acetyl-CoA + HCO₃^- = ADP + phosphate + malonyl-CoA.
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subunit structure	Acetyl-CoA carboxylase is an heterohexamer of biotin carboxyl carrier protein, biotin carboxylase and the two subunits of carboxyl transferase in a 2:2 complex. Ref.10
Sequence similarities	Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain.

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Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Ligand	ATP-binding Biotin Nucleotide-binding
Molecular function	Ligase
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
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activity Inferred from electronic annotation. Source: EC biotin binding Inferred from electronic annotation. Source: InterPro biotin carboxylase 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 – 449

449

Biotin carboxylase

PRO_0000146791

Regions

Domain

1 – 445

445

Biotin carboxylation

Domain

120 – 317

198

ATP-grasp

Sites

Active site

292

Potential

Binding site

116

ATP

Binding site

201

ATP

Binding site

236

ATP

Experimental info

Mutagenesis

R → E: Loss of homodimerization. No effect on ATP binding. Ref.10

Mutagenesis

E → R: Loss of homodimerization. No effect on ATP binding. Ref.10

Mutagenesis

363

F → A: Loss of homodimerization. No effect on ATP binding. Ref.10

Mutagenesis

366

R → E: Loss of homodimerization. No effect on ATP binding. Ref.10

Sequence conflict

136

G → A Ref.7

Sequence conflict

160

A → P Ref.7

Sequence conflict

260 – 261

CA → SR Ref.2

Sequence conflict

313

L → M in AAA23748. Ref.1

Secondary structure

449

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P24182-1 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: 68C55F10ACB4F170
Show »

FASTA

449

49,321

        10         20         30         40         50         60 
MLDKIVIANR GEIALRILRA CKELGIKTVA VHSSADRDLK HVLLADETVC IGPAPSVKSY 

        70         80         90        100        110        120 
LNIPAIISAA EITGAVAIHP GYGFLSENAN FAEQVERSGF IFIGPKAETI RLMGDKVSAI 

       130        140        150        160        170        180 
AAMKKAGVPC VPGSDGPLGD DMDKNRAIAK RIGYPVIIKA SGGGGGRGMR VVRGDAELAQ 

       190        200        210        220        230        240 
SISMTRAEAK AAFSNDMVYM EKYLENPRHV EIQVLADGQG NAIYLAERDC SMQRRHQKVV 

       250        260        270        280        290        300 
EEAPAPGITP ELRRYIGERC AKACVDIGYR GAGTFEFLFE NGEFYFIEMN TRIQVEHPVT 

       310        320        330        340        350        360 
EMITGVDLIK EQLRIAAGQP LSIKQEEVHV RGHAVECRIN AEDPNTFLPS PGKITRFHAP 

       370        380        390        400        410        420 
GGFGVRWESH IYAGYTVPPY YDSMIGKLIC YGENRDVAIA RMKNALQELI IDGIKTNVDL 

       430        440 
QIRIMNDENF QHGGTNIHYL EKKLGLQEK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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], PARTIAL PROTEIN SEQUENCE. Strain: K12.
[2]	"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].
[3]	"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].
[4]	"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.
[5]	"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.
[6]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-12. Strain: K12 / EMG2.
[7]	"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] OF 1-160.
[8]	"Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase." Waldrop G.L., Rayment I., Holden H.M. Biochemistry 33:10249-10256(1994) [PubMed: 7915138] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[9]	"Movement of the biotin carboxylase B-domain as a result of ATP binding." Thoden J.B., Blanchard C.Z., Holden H.M., Waldrop G.L. J. Biol. Chem. 275:16183-16190(2000) [PubMed: 10821865] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ATP.
[10]	"Is dimerization required for the catalytic activity of bacterial biotin carboxylase?" Shen Y., Chou C.-Y., Chang G.-G., Tong L. Mol. Cell 22:807-818(2006) [PubMed: 16793549] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT, MUTAGENESIS OF ARG-19; GLU-23; PHE-363 AND ARG-366.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

M79446 Genomic DNA. Translation: AAA23748.1.
M80458 Genomic DNA. Translation: AAA23409.1.
M83198 Genomic DNA. Translation: AAA23746.1.
U18997 Genomic DNA. Translation: AAA58059.1.
U00096 Genomic DNA. Translation: AAC76288.1.
AP009048 Genomic DNA. Translation: BAE77297.1.
M32214 Genomic DNA. No translation available.

PIR

JS0632.

RefSeq

AP_003796.1.
NP_417722.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BNC	X-ray	2.40	A/B	1-449	[»]
1DV1	X-ray	1.90	A/B	1-449	[»]
1DV2	X-ray	2.50	A/B	1-449	[»]
1K69	model	-	A	1-447	[»]
2GPS	X-ray	2.80	A/B	1-449	[»]
2GPW	X-ray	2.20	A/B/C/D	1-449	[»]
2J9G	X-ray	2.05	A/B	1-449	[»]
2V58	X-ray	2.10	A/B	1-449	[»]
2V59	X-ray	2.40	A/B	1-449	[»]
2V5A	X-ray	2.31	A/B	1-449	[»]
2VR1	X-ray	2.60	A/B	1-449	[»]
3G8C	X-ray	2.00	A/B	1-444	[»]
3G8D	X-ray	1.90	A/B	1-444	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9035N.

Genome annotation databases

GeneID

947761.

GenomeReviews

Gene locus JW3224 in contig AP009048_GR.
Gene locus b3256 in contig U00096_GR.

KEGG

ecj:JW3224.
eco:b3256.

Organism-specific databases

EchoBASE

EB0272.

EcoGene

EG10276. accC.

CMR

Search...

Phylogenomic databases

HOGENOM

P24182.

OMA

P24182. HIRLMGD.

Enzyme and pathway databases

BioCyc

EcoCyc:BIOTIN-CARBOXYL-MON.
MetaCyc:BIOTIN-CARBOXYL-MON.

Family and domain databases

InterPro

IPR004549. Acetyl_CoA_COase_biotin_COase.
IPR011761. ATP-grasp.
IPR013816. ATP_grasp_subdomain_2.
IPR011764. BC.
IPR005482. Biotin_COase_C.
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.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00514. accC. 1 hit.

PROSITE

PS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

ACCC_ECOLI

Accession

Primary (citable) accession number: P24182
Secondary accession number(s): Q2M8V9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	February 1, 1994
Last modified:	June 16, 2009
This is version 101 of the entry and version 2 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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