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P24182

- ACCC_ECOLI

UniProt

P24182 - ACCC_ECOLI

Protein

Biotin carboxylase

Gene

accC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (01 Feb 1994)
      Previous versions | rss
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    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 – 1161ATP1 Publication
    Binding sitei201 – 2011ATP1 Publication
    Binding sitei236 – 2361ATP1 Publication
    Active sitei292 – 2921Sequence Analysis

    GO - Molecular functioni

    1. acetyl-CoA carboxylase activity Source: UniProtKB-EC
    2. ATP binding Source: UniProtKB-KW
    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

    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

    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.

    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.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 – 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.
    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.
    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

    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:
    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

    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: October 1, 2014
    This is version 150 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