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P24182 (ACCC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length449 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 + carboxy-biotin-[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 a 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

accBP0ABD86EBI-542308,EBI-542320

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449Biotin carboxylase
PRO_0000146791

Regions

Domain1 – 445445Biotin carboxylation
Domain120 – 317198ATP-grasp

Sites

Active site2921 Potential
Binding site1161ATP
Binding site2011ATP
Binding site2361ATP

Experimental info

Mutagenesis191R → E: Loss of homodimerization. No effect on ATP binding. Ref.10
Mutagenesis231E → R: Loss of homodimerization. No effect on ATP binding. Ref.10
Mutagenesis3631F → A: Loss of homodimerization. No effect on ATP binding. Ref.10
Mutagenesis3661R → E: Loss of homodimerization. No effect on ATP binding. Ref.10
Sequence conflict1361G → A Ref.7
Sequence conflict1601A → P Ref.7
Sequence conflict260 – 2612CA → SR Ref.2
Sequence conflict3131L → M in AAA23748. Ref.1

Secondary structure

................................................................................. 449
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24182 [UniParc].

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

FASTA44949,321
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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 277:1453-1462(1997) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJS0632.
RefSeqNP_417722.1. NC_000913.3.
YP_491438.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BNCX-ray2.40A/B1-449[»]
1DV1X-ray1.90A/B1-449[»]
1DV2X-ray2.50A/B1-449[»]
1K69model-A1-447[»]
2GPSX-ray2.80A/B1-449[»]
2GPWX-ray2.20A/B/C/D1-449[»]
2J9GX-ray2.05A/B1-449[»]
2V58X-ray2.10A/B1-449[»]
2V59X-ray2.40A/B1-449[»]
2V5AX-ray2.31A/B1-449[»]
2VR1X-ray2.60A/B1-449[»]
2W6MX-ray2.00A/B1-449[»]
2W6NX-ray1.87A/B1-449[»]
2W6OX-ray2.50A/C1-449[»]
2W6PX-ray1.85A/B1-449[»]
2W6QX-ray2.05A/B1-449[»]
2W6ZX-ray1.90A/B1-449[»]
2W70X-ray1.77A/B1-449[»]
2W71X-ray1.99A/C1-449[»]
3G8CX-ray2.00A/B1-444[»]
3G8DX-ray1.90A/B1-444[»]
3JZFX-ray2.13A/B1-449[»]
3JZIX-ray2.31A/B1-449[»]
3RUPX-ray1.99A/B1-449[»]
3RV3X-ray1.91A/B1-449[»]
3RV4X-ray1.98A1-449[»]
4HR7X-ray2.50A/C/E/F1-449[»]
ProteinModelPortalP24182.
SMRP24182. Positions 1-446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9035N.
IntActP24182. 20 interactions.
MINTMINT-1266968.
STRING511145.b3256.

Chemistry

BindingDBP24182.

Proteomic databases

PaxDbP24182.
PRIDEP24182.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76288; AAC76288; b3256.
BAE77297; BAE77297; BAE77297.
GeneID12933462.
947761.
KEGGecj:Y75_p3174.
eco:b3256.
PATRIC32121942. VBIEscCol129921_3355.

Organism-specific databases

EchoBASEEB0272.
EcoGeneEG10276. accC.

Phylogenomic databases

eggNOGCOG0439.
HOGENOMHOG000008988.
KOK01961.
OMAIRRMQNA.
OrthoDBEOG6CVV6Z.
PhylomeDBP24182.

Enzyme and pathway databases

BioCycEcoCyc:BIOTIN-CARBOXYL-MONOMER.
ECOL316407:JW3224-MONOMER.
MetaCyc:BIOTIN-CARBOXYL-MONOMER.
RETL1328306-WGS:GSTH-1922-MONOMER.
SABIO-RKP24182.
UniPathwayUPA00655; UER00711.

Gene expression databases

GenevestigatorP24182.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProIPR004549. Acetyl_CoA_COase_biotin_COase.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamPF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsTIGR00514. accC. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP24182.
PROP24182.

Entry information

Entry nameACCC_ECOLI
AccessionPrimary (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: July 9, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene