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Protein

Biotin carboxylase

Gene

accC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

ATP + biotin-[carboxyl-carrier-protein] + HCO3- = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].
ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.

Pathway: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.
Proteins known to be involved in this subpathway in this organism are:
  1. Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (accD), Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA), Biotin carboxylase (accC), Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (accD)
This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161ATP1 Publication
Binding sitei201 – 2011ATP1 Publication
Binding sitei236 – 2361ATP1 Publication
Active sitei292 – 2921Sequence Analysis

GO - Molecular functioni

GO - Biological processi

  • fatty acid biosynthetic process Source: EcoCyc
  • malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
  • negative regulation of fatty acid biosynthetic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Biotin, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:BIOTIN-CARBOXYL-MONOMER.
ECOL316407:JW3224-MONOMER.
MetaCyc:BIOTIN-CARBOXYL-MONOMER.
RETL1328306-WGS:GSTH-1922-MONOMER.
BRENDAi6.3.4.14. 2026.
SABIO-RKP24182.
UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin carboxylase (EC:6.3.4.14)
Alternative name(s):
Acetyl-CoA carboxylase subunit A (EC:6.4.1.2)
Short name:
ACC
Gene namesi
Name:accC
Synonyms:fabG
Ordered Locus Names:b3256, JW3224
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10276. accC.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191R → E: Loss of homodimerization. No effect on ATP binding. 1 Publication
Mutagenesisi23 – 231E → R: Loss of homodimerization. No effect on ATP binding. 1 Publication
Mutagenesisi363 – 3631F → A: Loss of homodimerization. No effect on ATP binding. 1 Publication
Mutagenesisi366 – 3661R → E: Loss of homodimerization. No effect on ATP binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449Biotin carboxylasePRO_0000146791Add
BLAST

Proteomic databases

PaxDbiP24182.
PRIDEiP24182.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
accBP0ABD86EBI-542308,EBI-542320

Protein-protein interaction databases

DIPiDIP-9035N.
IntActiP24182. 20 interactions.
MINTiMINT-1266968.
STRINGi511145.b3256.

Structurei

Secondary structure

1
449
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Helixi11 – 2414Combined sources
Beta strandi27 – 337Combined sources
Helixi34 – 363Combined sources
Helixi40 – 445Combined sources
Beta strandi45 – 528Combined sources
Helixi56 – 583Combined sources
Turni59 – 613Combined sources
Helixi63 – 7311Combined sources
Beta strandi77 – 793Combined sources
Turni84 – 874Combined sources
Helixi89 – 979Combined sources
Beta strandi101 – 1055Combined sources
Helixi107 – 1148Combined sources
Helixi116 – 12611Combined sources
Helixi142 – 15211Combined sources
Beta strandi154 – 1607Combined sources
Turni165 – 1684Combined sources
Beta strandi170 – 1723Combined sources
Helixi175 – 19319Combined sources
Beta strandi198 – 2025Combined sources
Beta strandi208 – 2169Combined sources
Beta strandi218 – 2203Combined sources
Beta strandi222 – 23413Combined sources
Beta strandi237 – 2448Combined sources
Helixi250 – 26718Combined sources
Beta strandi271 – 28010Combined sources
Beta strandi283 – 2908Combined sources
Helixi297 – 3048Combined sources
Helixi308 – 31710Combined sources
Helixi325 – 3273Combined sources
Beta strandi332 – 3409Combined sources
Turni344 – 3463Combined sources
Beta strandi356 – 3583Combined sources
Beta strandi365 – 3684Combined sources
Beta strandi379 – 3813Combined sources
Beta strandi383 – 39412Combined sources
Helixi395 – 40814Combined sources
Beta strandi410 – 4145Combined sources
Helixi418 – 4258Combined sources
Helixi428 – 4325Combined sources
Helixi439 – 4446Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP24182.
SMRiP24182. Positions 1-446.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24182.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 445445Biotin carboxylationAdd
BLAST
Domaini120 – 317198ATP-graspPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
Contains 1 biotin carboxylation domain.Curated

Phylogenomic databases

eggNOGiCOG0439.
HOGENOMiHOG000008988.
InParanoidiP24182.
KOiK01961.
OMAiERCANAC.
OrthoDBiEOG6CVV6Z.
PhylomeDBiP24182.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR004549. 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]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR00514. accC. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P24182-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLDKIVIANR GEIALRILRA CKELGIKTVA VHSSADRDLK HVLLADETVC
60 70 80 90 100
IGPAPSVKSY LNIPAIISAA EITGAVAIHP GYGFLSENAN FAEQVERSGF
110 120 130 140 150
IFIGPKAETI RLMGDKVSAI AAMKKAGVPC VPGSDGPLGD DMDKNRAIAK
160 170 180 190 200
RIGYPVIIKA SGGGGGRGMR VVRGDAELAQ SISMTRAEAK AAFSNDMVYM
210 220 230 240 250
EKYLENPRHV EIQVLADGQG NAIYLAERDC SMQRRHQKVV EEAPAPGITP
260 270 280 290 300
ELRRYIGERC AKACVDIGYR GAGTFEFLFE NGEFYFIEMN TRIQVEHPVT
310 320 330 340 350
EMITGVDLIK EQLRIAAGQP LSIKQEEVHV RGHAVECRIN AEDPNTFLPS
360 370 380 390 400
PGKITRFHAP GGFGVRWESH IYAGYTVPPY YDSMIGKLIC YGENRDVAIA
410 420 430 440
RMKNALQELI IDGIKTNVDL QIRIMNDENF QHGGTNIHYL EKKLGLQEK
Length:449
Mass (Da):49,321
Last modified:February 1, 1994 - v2
Checksum:i68C55F10ACB4F170
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361G → A (PubMed:2575489).Curated
Sequence conflicti160 – 1601A → P (PubMed:2575489).Curated
Sequence conflicti260 – 2612CA → SR (PubMed:1370469).Curated
Sequence conflicti313 – 3131L → M in AAA23748 (PubMed:1682920).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJS0632.
RefSeqiNP_417722.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76288; AAC76288; b3256.
BAE77297; BAE77297; BAE77297.
GeneIDi947761.
KEGGiecj:Y75_p3174.
eco:b3256.
PATRICi32121942. VBIEscCol129921_3355.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJS0632.
RefSeqiNP_417722.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP24182.
SMRiP24182. Positions 1-446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9035N.
IntActiP24182. 20 interactions.
MINTiMINT-1266968.
STRINGi511145.b3256.

Chemistry

BindingDBiP24182.

Proteomic databases

PaxDbiP24182.
PRIDEiP24182.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76288; AAC76288; b3256.
BAE77297; BAE77297; BAE77297.
GeneIDi947761.
KEGGiecj:Y75_p3174.
eco:b3256.
PATRICi32121942. VBIEscCol129921_3355.

Organism-specific databases

EchoBASEiEB0272.
EcoGeneiEG10276. accC.

Phylogenomic databases

eggNOGiCOG0439.
HOGENOMiHOG000008988.
InParanoidiP24182.
KOiK01961.
OMAiERCANAC.
OrthoDBiEOG6CVV6Z.
PhylomeDBiP24182.

Enzyme and pathway databases

UniPathwayiUPA00655; UER00711.
BioCyciEcoCyc:BIOTIN-CARBOXYL-MONOMER.
ECOL316407:JW3224-MONOMER.
MetaCyc:BIOTIN-CARBOXYL-MONOMER.
RETL1328306-WGS:GSTH-1922-MONOMER.
BRENDAi6.3.4.14. 2026.
SABIO-RKP24182.

Miscellaneous databases

EvolutionaryTraceiP24182.
PROiP24182.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR004549. 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]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR00514. accC. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiACCC_ECOLI
AccessioniPrimary (citable) accession number: P24182
Secondary accession number(s): Q2M8V9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: February 1, 1994
Last modified: June 24, 2015
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.