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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.

Pathwayi: 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 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)DescriptionActionsGraphical viewLength
Binding sitei116ATP1 Publication1
Binding sitei201ATP1 Publication1
Binding sitei236ATP1 Publication1
Active sitei292Sequence analysis1

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.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10276. accC.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi19R → E: Loss of homodimerization. No effect on ATP binding. 1 Publication1
Mutagenesisi23E → R: Loss of homodimerization. No effect on ATP binding. 1 Publication1
Mutagenesisi363F → A: Loss of homodimerization. No effect on ATP binding. 1 Publication1
Mutagenesisi366R → E: Loss of homodimerization. No effect on ATP binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001467911 – 449Biotin carboxylaseAdd BLAST449

Proteomic databases

EPDiP24182.
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

BioGridi4262456. 258 interactors.
DIPiDIP-9035N.
IntActiP24182. 20 interactors.
MINTiMINT-1266968.
STRINGi511145.b3256.

Chemistry databases

BindingDBiP24182.

Structurei

Secondary structure

1449
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 7Combined sources5
Helixi11 – 24Combined sources14
Beta strandi27 – 33Combined sources7
Helixi34 – 36Combined sources3
Helixi40 – 44Combined sources5
Beta strandi45 – 52Combined sources8
Helixi56 – 58Combined sources3
Turni59 – 61Combined sources3
Helixi63 – 73Combined sources11
Beta strandi77 – 79Combined sources3
Turni84 – 87Combined sources4
Helixi89 – 97Combined sources9
Beta strandi101 – 105Combined sources5
Helixi107 – 114Combined sources8
Helixi116 – 126Combined sources11
Helixi142 – 152Combined sources11
Beta strandi154 – 160Combined sources7
Turni165 – 168Combined sources4
Beta strandi170 – 172Combined sources3
Helixi175 – 193Combined sources19
Beta strandi198 – 202Combined sources5
Beta strandi208 – 216Combined sources9
Beta strandi218 – 220Combined sources3
Beta strandi222 – 234Combined sources13
Beta strandi237 – 244Combined sources8
Helixi250 – 267Combined sources18
Beta strandi271 – 280Combined sources10
Beta strandi283 – 290Combined sources8
Helixi297 – 304Combined sources8
Helixi308 – 317Combined sources10
Helixi325 – 327Combined sources3
Beta strandi332 – 340Combined sources9
Turni344 – 346Combined sources3
Beta strandi356 – 358Combined sources3
Beta strandi365 – 368Combined sources4
Beta strandi379 – 381Combined sources3
Beta strandi383 – 394Combined sources12
Helixi395 – 408Combined sources14
Beta strandi410 – 414Combined sources5
Helixi418 – 425Combined sources8
Helixi428 – 432Combined sources5
Helixi439 – 444Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24182.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 445Biotin carboxylationAdd BLAST445
Domaini120 – 317ATP-graspPROSITE-ProRule annotationAdd BLAST198

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CER. Bacteria.
COG0439. LUCA.
HOGENOMiHOG000008988.
InParanoidiP24182.
KOiK01961.
OMAiKGHAVEC.
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.
IPR005481. BC-like_N.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. Biotin_carb_N. 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)DescriptionActionsGraphical viewLength
Sequence conflicti136G → A (PubMed:2575489).Curated1
Sequence conflicti160A → P (PubMed:2575489).Curated1
Sequence conflicti260 – 261CA → SR (PubMed:1370469).Curated2
Sequence conflicti313L → M in AAA23748 (PubMed:1682920).Curated1

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.
WP_000884639.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76288; AAC76288; b3256.
BAE77297; BAE77297; BAE77297.
GeneIDi947761.
KEGGiecj:JW3224.
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.
WP_000884639.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262456. 258 interactors.
DIPiDIP-9035N.
IntActiP24182. 20 interactors.
MINTiMINT-1266968.
STRINGi511145.b3256.

Chemistry databases

BindingDBiP24182.

Proteomic databases

EPDiP24182.
PaxDbiP24182.
PRIDEiP24182.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76288; AAC76288; b3256.
BAE77297; BAE77297; BAE77297.
GeneIDi947761.
KEGGiecj:JW3224.
eco:b3256.
PATRICi32121942. VBIEscCol129921_3355.

Organism-specific databases

EchoBASEiEB0272.
EcoGeneiEG10276. accC.

Phylogenomic databases

eggNOGiENOG4105CER. Bacteria.
COG0439. LUCA.
HOGENOMiHOG000008988.
InParanoidiP24182.
KOiK01961.
OMAiKGHAVEC.
PhylomeDBiP24182.

Enzyme and pathway databases

UniPathwayiUPA00655; UER00711.
BioCyciEcoCyc:BIOTIN-CARBOXYL-MONOMER.
ECOL316407:JW3224-MONOMER.
MetaCyc:BIOTIN-CARBOXYL-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.
IPR005481. BC-like_N.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. Biotin_carb_N. 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...

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: November 2, 2016
This is version 166 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

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 one 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.