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O04983

- ACCC_ARATH

UniProt

O04983 - ACCC_ARATH

Protein

Biotin carboxylase, chloroplastic

Gene

CAC2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      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.1 Publication

    Catalytic activityi

    ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].
    ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.

    Cofactori

    Binds 2 magnesium or manganese ions per subunit.By similarity

    Kineticsi

    1. KM=2.3 mM for biotin1 Publication
    2. KM=88 mM for bicarbonate1 Publication

    Vmax=16 nmol/min/mg enzyme1 Publication

    pH dependencei

    Optimum pH is 8.3-8.9.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei188 – 1881ATPBy similarity
    Binding sitei272 – 2721ATPBy similarity
    Binding sitei307 – 3071ATPBy similarity
    Metal bindingi347 – 3471Magnesium or manganese 1PROSITE-ProRule annotation
    Metal bindingi360 – 3601Magnesium or manganese 1PROSITE-ProRule annotation
    Metal bindingi360 – 3601Magnesium or manganese 2PROSITE-ProRule annotation
    Metal bindingi362 – 3621Magnesium or manganese 2PROSITE-ProRule annotation
    Active sitei364 – 3641By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi220 – 28162ATPPROSITE-ProRule annotationAdd
    BLAST

    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: UniProtKB-KW

    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, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciARA:AT5G35360-MONOMER.
    ARA:GQT-2157-MONOMER.
    ARA:GQT-2739-MONOMER.
    ReactomeiREACT_185257. Defective HLCS causes multiple carboxylase deficiency.
    REACT_187915. Biotin transport and metabolism.
    UniPathwayiUPA00655; UER00711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Biotin carboxylase, chloroplastic (EC:6.3.4.14)
    Alternative name(s):
    Acetyl-CoA carboxylase subunit A (EC:6.4.1.2)
    Short name:
    ACC
    Gene namesi
    Name:CAC2
    Ordered Locus Names:At5g35360
    ORF Names:T26D22.8
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G35360.

    Subcellular locationi

    Plastidchloroplast 3 Publications

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 7070ChloroplastSequence AnalysisAdd
    BLAST
    Chaini71 – 537467Biotin carboxylase, chloroplasticPRO_0000391772Add
    BLAST

    Proteomic databases

    PaxDbiO04983.
    PRIDEiO04983.

    Expressioni

    Tissue specificityi

    Accumulates in fatty acids synthesizing tissues. Mostly expressed in siliques, developing leaves, and flowers, present in roots and embryos (especially at torpedo stage), and, to a lower extent, in mature leaves.3 Publications

    Gene expression databases

    GenevestigatoriO04983.

    Interactioni

    Subunit structurei

    Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein, biotin carboxylase and two subunits each of ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).Curated

    Protein-protein interaction databases

    BioGridi18751. 5 interactions.
    IntActiO04983. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliO04983.
    SMRiO04983. Positions 75-513.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini192 – 389198ATP-graspPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ATP-grasp domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0439.
    HOGENOMiHOG000008988.
    InParanoidiO04983.
    KOiK01961.
    PhylomeDBiO04983.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 1 isoform i produced by alternative splicing. Align

    Note: A number of isoforms are produced. According to EST sequences.

    Isoform 1 (identifier: O04983-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDASMITNSK SITSPPSLAL GKSGGGGVIR SSLCNLMMPS KVNFPRQRTQ    50
    TLKVSQKKLK RATSGGLGVT CSGGDKILVA NRGEIAVRVI RTAHEMGIPC 100
    VAVYSTIDKD ALHVKLADEA VCIGEAPSNQ SYLVIPNVLS AAISRGCTML 150
    HPGYGFLSEN ALFVEMCRDH GINFIGPNPD SIRVMGDKAT ARETMKNAGV 200
    PTVPGSDGLL QSTEEAVRVA NEIGFPVMIK ATAGGGGRGM RLAKEPGEFV 250
    KLLQQAKSEA AAAFGNDGCY LEKFVQNPRH IEFQVLADKF GNVVHFGERD 300
    CSIQRRNQKL LEEAPSPALT AELRKAMGDA AVAAAASIGY IGVGTVEFLL 350
    DERGSFYFME MNTRIQVEHP VTEMIYSVDL IEEQIRVAMG EKLRYKQEDI 400
    VLRGHSIECR INAEDPFKGF RPGPGRITSY LPSGGPFVRM DSHVYSDYVV 450
    PPSYDSLLGK LIVWAPTREK AIERMKRALN DTIITGVPTT INYHKLILDV 500
    EDFKNGKVDT AFIVKHEEEL AEPQEIVAVK DLTNATV 537
    Length:537
    Mass (Da):58,387
    Last modified:July 1, 1997 - v1
    Checksum:iCB57C973A2A735C8
    GO

    Sequence cautioni

    The sequence CAA70282.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti181 – 1811S → T in CAA70282. (PubMed:9349276)Curated
    Sequence conflicti230 – 2301K → T in CAA70282. (PubMed:9349276)Curated
    Sequence conflicti314 – 3141Missing in CAA70282. (PubMed:9349276)Curated
    Sequence conflicti447 – 4471D → N in AAK25989. (PubMed:14593172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09061 Genomic DNA. Translation: CAA70282.1. Sequence problems.
    U90879 mRNA. Translation: AAC09008.1.
    U91414 Genomic DNA. Translation: AAC09009.1.
    AB025636 Genomic DNA. Translation: BAB11486.1.
    AF058826 Genomic DNA. Translation: AAC13611.1.
    CP002688 Genomic DNA. Translation: AED93956.1.
    AF360279 mRNA. Translation: AAK25989.1.
    AY142630 mRNA. Translation: AAN13088.1.
    AY085968 mRNA. Translation: AAM63178.1.
    PIRiT01180.
    RefSeqiNP_198386.1. NM_122927.3. [O04983-1]
    UniGeneiAt.22848.
    At.70066.

    Genome annotation databases

    EnsemblPlantsiAT5G35360.1; AT5G35360.1; AT5G35360. [O04983-1]
    GeneIDi833497.
    KEGGiath:AT5G35360.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09061 Genomic DNA. Translation: CAA70282.1 . Sequence problems.
    U90879 mRNA. Translation: AAC09008.1 .
    U91414 Genomic DNA. Translation: AAC09009.1 .
    AB025636 Genomic DNA. Translation: BAB11486.1 .
    AF058826 Genomic DNA. Translation: AAC13611.1 .
    CP002688 Genomic DNA. Translation: AED93956.1 .
    AF360279 mRNA. Translation: AAK25989.1 .
    AY142630 mRNA. Translation: AAN13088.1 .
    AY085968 mRNA. Translation: AAM63178.1 .
    PIRi T01180.
    RefSeqi NP_198386.1. NM_122927.3. [O04983-1 ]
    UniGenei At.22848.
    At.70066.

    3D structure databases

    ProteinModelPortali O04983.
    SMRi O04983. Positions 75-513.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 18751. 5 interactions.
    IntActi O04983. 1 interaction.

    Proteomic databases

    PaxDbi O04983.
    PRIDEi O04983.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G35360.1 ; AT5G35360.1 ; AT5G35360 . [O04983-1 ]
    GeneIDi 833497.
    KEGGi ath:AT5G35360.

    Organism-specific databases

    TAIRi AT5G35360.

    Phylogenomic databases

    eggNOGi COG0439.
    HOGENOMi HOG000008988.
    InParanoidi O04983.
    KOi K01961.
    PhylomeDBi O04983.

    Enzyme and pathway databases

    UniPathwayi UPA00655 ; UER00711 .
    BioCyci ARA:AT5G35360-MONOMER.
    ARA:GQT-2157-MONOMER.
    ARA:GQT-2739-MONOMER.
    Reactomei REACT_185257. Defective HLCS causes multiple carboxylase deficiency.
    REACT_187915. Biotin transport and metabolism.

    Miscellaneous databases

    PROi O04983.

    Gene expression databases

    Genevestigatori O04983.

    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. "Isolation and characterization of an Arabidopsis biotin carboxylase gene and its promoter."
      Bao X., Shorrosh B.S., Ohlrogge J.B.
      Plant Mol. Biol. 35:539-550(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
      Strain: cv. Columbia.
    2. "Biochemical and molecular biological characterization of CAC2, the Arabidopsis thaliana gene coding for the biotin carboxylase subunit of the plastidic acetyl-coenzyme A carboxylase."
      Sun J., Ke J., Johnson J.L., Nikolau B.J., Wurtele E.S.
      Plant Physiol. 115:1371-1383(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, TISSUE SPECIFICITY.
      Strain: cv. Columbia and cv. Landsberg erecta.
    3. "Structural analysis of Arabidopsis thaliana chromosome 5. XI."
      Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
      Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
      , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
      Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    5. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    6. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    7. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    8. "Coordinate regulation of the nuclear and plastidic genes coding for the subunits of the heteromeric acetyl-coenzyme A carboxylase."
      Ke J., Wen T.N., Nikolau B.J., Wurtele E.S.
      Plant Physiol. 122:1057-1071(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
      Strain: cv. Columbia.
    9. "Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis."
      Froehlich J.E., Wilkerson C.G., Ray W.K., McAndrew R.S., Osteryoung K.W., Gage D.A., Phinney B.S.
      J. Proteome Res. 2:413-425(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. Cited for: SUBCELLULAR LOCATION.
    11. "Sorting signals, N-terminal modifications and abundance of the chloroplast proteome."
      Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J.
      PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiACCC_ARATH
    AccessioniPrimary (citable) accession number: O04983
    Secondary accession number(s): P93650, Q9C5F8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 2, 2010
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3