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P24182

- ACCC_ECOLI

UniProt

P24182 - ACCC_ECOLI

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Protein
Biotin carboxylase
Gene
accC, fabG, b3256, JW3224
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].
ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161ATP
Binding sitei201 – 2011ATP
Binding sitei236 – 2361ATP
Active sitei292 – 2921 Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. acetyl-CoA carboxylase activity Source: UniProtKB-EC
  3. biotin carboxylase activity Source: EcoliWiki
  4. metal ion binding Source: InterPro
  5. protein binding Source: IntAct

GO - Biological processi

  1. fatty acid biosynthetic process Source: EcoCyc
  2. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
  3. 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.
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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10276. accC.

Subcellular locationi

GO - Cellular componenti

  1. 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 carboxylase
PRO_0000146791Add
BLAST

Proteomic databases

PaxDbiP24182.
PRIDEiP24182.

Expressioni

Gene expression databases

GenevestigatoriP24182.

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.1 Publication

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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP24182.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 445445Biotin carboxylation
Add
BLAST
Domaini120 – 317198ATP-grasp
Add
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.

Phylogenomic databases

eggNOGiCOG0439.
HOGENOMiHOG000008988.
KOiK01961.
OMAiIRRMQNA.
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

MLDKIVIANR GEIALRILRA CKELGIKTVA VHSSADRDLK HVLLADETVC    50
IGPAPSVKSY LNIPAIISAA EITGAVAIHP GYGFLSENAN FAEQVERSGF 100
IFIGPKAETI RLMGDKVSAI AAMKKAGVPC VPGSDGPLGD DMDKNRAIAK 150
RIGYPVIIKA SGGGGGRGMR VVRGDAELAQ SISMTRAEAK AAFSNDMVYM 200
EKYLENPRHV EIQVLADGQG NAIYLAERDC SMQRRHQKVV EEAPAPGITP 250
ELRRYIGERC AKACVDIGYR GAGTFEFLFE NGEFYFIEMN TRIQVEHPVT 300
EMITGVDLIK EQLRIAAGQP LSIKQEEVHV RGHAVECRIN AEDPNTFLPS 350
PGKITRFHAP GGFGVRWESH IYAGYTVPPY YDSMIGKLIC YGENRDVAIA 400
RMKNALQELI IDGIKTNVDL QIRIMNDENF QHGGTNIHYL EKKLGLQEK 449
Length:449
Mass (Da):49,321
Last modified:February 1, 1994 - v2
Checksum:i68C55F10ACB4F170
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361G → A1 Publication
Sequence conflicti160 – 1601A → P1 Publication
Sequence conflicti260 – 2612CA → SR1 Publication
Sequence conflicti313 – 3131L → M in AAA23748. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_491438.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76288; AAC76288; b3256.
BAE77297; BAE77297; BAE77297.
GeneIDi12933462.
947761.
KEGGiecj:Y75_p3174.
eco:b3256.
PATRICi32121942. VBIEscCol129921_3355.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
PIRi JS0632.
RefSeqi NP_417722.1. NC_000913.3.
YP_491438.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
2W6M X-ray 2.00 A/B 1-449 [» ]
2W6N X-ray 1.87 A/B 1-449 [» ]
2W6O X-ray 2.50 A/C 1-449 [» ]
2W6P X-ray 1.85 A/B 1-449 [» ]
2W6Q X-ray 2.05 A/B 1-449 [» ]
2W6Z X-ray 1.90 A/B 1-449 [» ]
2W70 X-ray 1.77 A/B 1-449 [» ]
2W71 X-ray 1.99 A/C 1-449 [» ]
3G8C X-ray 2.00 A/B 1-444 [» ]
3G8D X-ray 1.90 A/B 1-444 [» ]
3JZF X-ray 2.13 A/B 1-449 [» ]
3JZI X-ray 2.31 A/B 1-449 [» ]
3RUP X-ray 1.99 A/B 1-449 [» ]
3RV3 X-ray 1.91 A/B 1-449 [» ]
3RV4 X-ray 1.98 A 1-449 [» ]
4HR7 X-ray 2.50 A/C/E/F 1-449 [» ]
ProteinModelPortali P24182.
SMRi P24182. Positions 1-446.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9035N.
IntActi P24182. 20 interactions.
MINTi MINT-1266968.
STRINGi 511145.b3256.

Chemistry

BindingDBi P24182.

Proteomic databases

PaxDbi P24182.
PRIDEi P24182.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76288 ; AAC76288 ; b3256 .
BAE77297 ; BAE77297 ; BAE77297 .
GeneIDi 12933462.
947761.
KEGGi ecj:Y75_p3174.
eco:b3256.
PATRICi 32121942. VBIEscCol129921_3355.

Organism-specific databases

EchoBASEi EB0272.
EcoGenei EG10276. accC.

Phylogenomic databases

eggNOGi COG0439.
HOGENOMi HOG000008988.
KOi K01961.
OMAi IRRMQNA.
OrthoDBi EOG6CVV6Z.
PhylomeDBi P24182.

Enzyme and pathway databases

UniPathwayi UPA00655 ; UER00711 .
BioCyci EcoCyc:BIOTIN-CARBOXYL-MONOMER.
ECOL316407:JW3224-MONOMER.
MetaCyc:BIOTIN-CARBOXYL-MONOMER.
RETL1328306-WGS:GSTH-1922-MONOMER.
SABIO-RK P24182.

Miscellaneous databases

EvolutionaryTracei P24182.
PROi P24182.

Gene expression databases

Genevestigatori P24182.

Family and domain databases

Gene3Di 3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProi IPR004549. 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 ]
Pfami PF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view ]
SMARTi SM00878. Biotin_carb_C. 1 hit.
[Graphical view ]
SUPFAMi SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsi TIGR00514. accC. 1 hit.
PROSITEi PS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 149 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

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