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P49787

- ACCC1_BACSU

UniProt

P49787 - ACCC1_BACSU

Protein

Biotin carboxylase 1

Gene

accC1

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 3 (07 Jul 2009)
      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
    Active sitei293 – 2931By 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:BSU24340-MONOMER.
    UniPathwayiUPA00655; UER00711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Biotin carboxylase 1 (EC:6.3.4.14)
    Alternative name(s):
    Acetyl-CoA carboxylase subunit A 1 (EC:6.4.1.2)
    Short name:
    ACC 1
    Gene namesi
    Name:accC1
    Synonyms:accC, yqhX
    Ordered Locus Names:BSU24340
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU24340. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 450450Biotin carboxylase 1PRO_0000146789Add
    BLAST

    Proteomic databases

    PaxDbiP49787.

    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

    IntActiP49787. 1 interaction.
    MINTiMINT-8365265.
    STRINGi224308.BSU24340.

    Structurei

    3D structure databases

    ProteinModelPortaliP49787.
    SMRiP49787. Positions 3-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 447447Biotin carboxylationAdd
    BLAST
    Domaini120 – 318199ATP-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.
    OrthoDBiEOG6CVV6Z.
    PhylomeDBiP49787.

    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.

    P49787-1 [UniParc]FASTAAdd to Basket

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    MIKKLLIANR GEIAVRIIRA CRELGIETVA VYSEADKDAL HVQMADEAFC    50
    IGPKASKDSY LNVTNIVSVA KLTGTDAIHP GYGFLAENAD FAELCEEVNV 100
    TFVGPSADAI SKMGTKDVAR ETMKQAGVPI VPGSQGIIEN VEEAVSLANE 150
    IGYPVIIKAT AGGGGKGIRV ARTEEELING IKITQQEAAT AFGNPGVYIE 200
    KYIEDFRHVE IQVLADNYGN TIHLGERDCS IQRRLQKLLE ESPSPALDSE 250
    IREQMGDAAV KAAKAVGYTG AGTVEFIYDY NEQRYYFMEM NTRIQVEHPV 300
    TEMVTGTDLI KEQIKVASGM ELSLKQEDVE FEGWAIECRI NAENPSKNFM 350
    PSPGEIKMYL PPGGLGVRVD SAAYPGYSIP PYYDSMIAKV ITYGKTRDEA 400
    IARMKRALSE FVIEGIETTI PFHLKLLEHE TFVSGEFNTK FLETYDVMGS 450
    Length:450
    Mass (Da):49,452
    Last modified:July 7, 2009 - v3
    Checksum:i2F93B3E793478334
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti107 – 1071A → P in BAA12569. (PubMed:8969508)Curated
    Sequence conflicti193 – 1931G → R in BAA12569. (PubMed:8969508)Curated
    Sequence conflicti240 – 2401E → G in AAB00183. (PubMed:7592499)Curated
    Sequence conflicti248 – 2481D → G in AAB00183. (PubMed:7592499)Curated
    Sequence conflicti344 – 3485NPSKN → TQVK in AAB00183. (PubMed:7592499)Curated
    Sequence conflicti357 – 3626KMYLPP → NVPAS in AAB00183. (PubMed:7592499)Curated
    Sequence conflicti409 – 4102SE → QQ in AAB00183. (PubMed:7592499)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U36245 Genomic DNA. Translation: AAB00183.1.
    D84432 Genomic DNA. Translation: BAA12569.1.
    AL009126 Genomic DNA. Translation: CAB14365.2.
    PIRiA69581.
    RefSeqiNP_390314.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB14365; CAB14365; BSU24340.
    GeneIDi938588.
    KEGGibsu:BSU24340.
    PATRICi18976702. VBIBacSub10457_2541.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U36245 Genomic DNA. Translation: AAB00183.1 .
    D84432 Genomic DNA. Translation: BAA12569.1 .
    AL009126 Genomic DNA. Translation: CAB14365.2 .
    PIRi A69581.
    RefSeqi NP_390314.2. NC_000964.3.

    3D structure databases

    ProteinModelPortali P49787.
    SMRi P49787. Positions 3-448.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P49787. 1 interaction.
    MINTi MINT-8365265.
    STRINGi 224308.BSU24340.

    Proteomic databases

    PaxDbi P49787.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14365 ; CAB14365 ; BSU24340 .
    GeneIDi 938588.
    KEGGi bsu:BSU24340.
    PATRICi 18976702. VBIBacSub10457_2541.

    Organism-specific databases

    GenoListi BSU24340. [Micado ]

    Phylogenomic databases

    eggNOGi COG0439.
    HOGENOMi HOG000008988.
    KOi K01961.
    OrthoDBi EOG6CVV6Z.
    PhylomeDBi P49787.

    Enzyme and pathway databases

    UniPathwayi UPA00655 ; UER00711 .
    BioCyci BSUB:BSU24340-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 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. "The genes encoding the biotin carboxyl carrier protein and biotin carboxylase subunits of Bacillus subtilis acetyl coenzyme A carboxylase, the first enzyme of fatty acid synthesis."
      Marini P.E., Li S.J., Gardiol D., Cronan J.E. Jr., de Mendoza D.
      J. Bacteriol. 177:7003-7006(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
      Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
      Microbiology 142:3103-3111(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / JH642.
    3. "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.
    4. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 107 AND 193.

    Entry informationi

    Entry nameiACCC1_BACSU
    AccessioniPrimary (citable) accession number: P49787
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 121 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Leu-235 is present instead of the conserved His which is expected to bind ATP.Curated

    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