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O34544

- ACCC2_BACSU

UniProt

O34544 - ACCC2_BACSU

Protein

Biotin carboxylase 2

Gene

accC2

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      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.By similarity

    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 – 1161ATPBy similarity
    Binding sitei200 – 2001ATPBy similarity
    Binding sitei235 – 2351ATPBy similarity
    Active sitei292 – 2921By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-KW
    2. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway

    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

    BioCyciBSUB:BSU18240-MONOMER.
    UniPathwayiUPA00655; UER00711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Biotin carboxylase 2 (EC:6.3.4.14)
    Alternative name(s):
    Acetyl-CoA carboxylase subunit A 2 (EC:6.4.1.2)
    Short name:
    ACC 2
    Gene namesi
    Name:accC2
    Synonyms:accC, yngH
    Ordered Locus Names:BSU18240
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU18240. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 444444Biotin carboxylase 2PRO_0000360841Add
    BLAST

    Proteomic databases

    PaxDbiO34544.

    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.By similarity

    Protein-protein interaction databases

    STRINGi224308.BSU18240.

    Structurei

    3D structure databases

    ProteinModelPortaliO34544.
    SMRiO34544. Positions 1-443.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 444444Biotin 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.
    OMAiAVILEFA.
    OrthoDBiEOG6CVV6Z.
    PhylomeDBiO34544.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    InterProiIPR011761. 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.
    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.

    O34544-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFTKVLIANR GEIAMRIIRT CSRLGIKTVA VYSEADKDAP HTKAATEAYL    50
    IGESRVSESY LNIERIIKTA KKAKADAIHP GYGLLSENSR FAERCKQENI 100
    VFIGPSPDII AKMGSKIEAR KAMEAAGVPV VPGVSESLGD IEAACRTASQ 150
    IGYPVMLKAS AGGGGIGMQR VENEEALKKA YEGNKKRAAD FFGDGSMYIE 200
    KVIEHARHIE VQLLADQHGH TVHLFERDCS VQRRHQKVIE EAPSPFVDDE 250
    LRMKIGQTAV KAAKAIGYTN AGTIEFIVDQ KQNFYFLEMN TRLQVEHPVT 300
    EEITGLDLVE QQLRIAAGHT LTFSQKDIQR NGHAIEVRIY AEDPKTFFPS 350
    PGTITAFSLP DQKGVRHECA VAKDSTVTPF YDPMIAKMIV KGQTRTEAIE 400
    KLETALRDYR VEGIKTNLPL LIQAAATKAF KEGDVTTDFL KQHL 444
    Length:444
    Mass (Da):49,087
    Last modified:January 1, 1998 - v1
    Checksum:iC866DEB8B4177E3B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13917 Genomic DNA. Translation: CAA74216.1.
    AL009126 Genomic DNA. Translation: CAB13707.1.
    PIRiE69893.
    RefSeqiNP_389706.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13707; CAB13707; BSU18240.
    GeneIDi939474.
    KEGGibsu:BSU18240.
    PATRICi18975485. VBIBacSub10457_1934.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13917 Genomic DNA. Translation: CAA74216.1 .
    AL009126 Genomic DNA. Translation: CAB13707.1 .
    PIRi E69893.
    RefSeqi NP_389706.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali O34544.
    SMRi O34544. Positions 1-443.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU18240.

    Proteomic databases

    PaxDbi O34544.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13707 ; CAB13707 ; BSU18240 .
    GeneIDi 939474.
    KEGGi bsu:BSU18240.
    PATRICi 18975485. VBIBacSub10457_1934.

    Organism-specific databases

    GenoListi BSU18240. [Micado ]

    Phylogenomic databases

    eggNOGi COG0439.
    HOGENOMi HOG000008988.
    KOi K01961.
    OMAi AVILEFA.
    OrthoDBi EOG6CVV6Z.
    PhylomeDBi O34544.

    Enzyme and pathway databases

    UniPathwayi UPA00655 ; UER00711 .
    BioCyci BSUB:BSU18240-MONOMER.

    Family and domain databases

    Gene3Di 3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    InterProi 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.
    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. "Sequence completion, identification and definition of the fengycin operon in Bacillus subtilis 168."
      Tosato V., Albertini A.M., Zotti M., Sonda S., Bruschi C.V.
      Microbiology 143:3443-3450(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.

    Entry informationi

    Entry nameiACCC2_BACSU
    AccessioniPrimary (citable) accession number: O34544
    Secondary accession number(s): Q799L8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 20, 2009
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3