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B9HBA8

- ACCC1_POPTR

UniProt

B9HBA8 - ACCC1_POPTR

Protein

Biotin carboxylase 1, chloroplastic

Gene

POPTRDRAFT_831870

Organism
Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (24 Mar 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.

    Cofactori

    Binds 2 magnesium or manganese ions per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei179 – 1791ATPBy similarity
    Binding sitei263 – 2631ATPBy similarity
    Binding sitei298 – 2981ATPBy similarity
    Metal bindingi338 – 3381Magnesium or manganese 1PROSITE-ProRule annotation
    Metal bindingi351 – 3511Magnesium or manganese 1PROSITE-ProRule annotation
    Metal bindingi351 – 3511Magnesium or manganese 2PROSITE-ProRule annotation
    Metal bindingi353 – 3531Magnesium or manganese 2PROSITE-ProRule annotation
    Active sitei355 – 3551By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi211 – 27262ATPPROSITE-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

    UniPathwayiUPA00655; UER00711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Biotin carboxylase 1, chloroplastic (EC:6.3.4.14)
    Alternative name(s):
    Acetyl-CoA carboxylase subunit A 1 (EC:6.4.1.2)
    Short name:
    ACC
    Gene namesi
    ORF Names:POPTRDRAFT_831870
    OrganismiPopulus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)
    Taxonomic identifieri3694 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesSalicaceaeSaliceaePopulus
    ProteomesiUP000006729: Linkage group LGVI, UP000006729: Unassembled WGS sequence

    Subcellular locationi

    Plastidchloroplast Curated

    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 – 5151ChloroplastSequence AnalysisAdd
    BLAST
    Chaini52 – 528477Biotin carboxylase 1, chloroplasticPRO_0000391773Add
    BLAST

    Proteomic databases

    PRIDEiB9HBA8.

    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

    STRINGi3694.estExt_fgenesh4_pm.C_LG_VI0248.

    Structurei

    3D structure databases

    ProteinModelPortaliB9HBA8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini183 – 380198ATP-graspPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ATP-grasp domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0439.
    HOGENOMiHOG000008988.
    KOiK01961.
    OMAiENIRHEM.

    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.

    B9HBA8-1 [UniParc]FASTAAdd to Basket

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    MEATLPVCKS VTSTPGLFMG KTSGIRSSQC SFMMGNKVNF PRQRAQTAHV    50
    HCAKNGGALG VTCRAEKILV ANRGEIAVRV IRTAHEMGIP CVAVYSTIDK 100
    DALHVKLADE SVCIGEAPSS QSYLVIPNVL SAAISRRCTM LHPGYGFLAE 150
    NAVFVEMCRE HGINFIGPNP DSIRVMGDKS TARETMKKAG VPTVPGSDGL 200
    LQSTEEGVRL ANEIGYPVMI KATAGGGGRG MRLAKEPDEF VKLLQQAKSE 250
    AAAAFGNDGV YLEKYVQNPR HIEFQVLADK FGNVVHFGER DCSIQRRNQK 300
    LLEEAPSPAL TPELRKAMGD AAVSAAASIG YIGVGTVEFL LDERGSFYFM 350
    EMNTRIQVEH PVTEMISSVD LIEEQIRVAM GEKLRYKQED IVLRGHSIEC 400
    RINAEDAFKG FRPGPGRITA YLPSGGPFVR MDSHVYPDYV VPPSYDSLLG 450
    KLIVWAPTRE KAIERMKRAL DDTIITGVPT TIDYHKLILE IEDFKNGNVD 500
    TAFIPKHEKE LAAPQQIIPA KQLTNSAA 528
    Length:528
    Mass (Da):57,707
    Last modified:March 24, 2009 - v1
    Checksum:i741BC742900ECF41
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CM000342 Genomic DNA. Translation: EEE91650.1.
    RefSeqiXP_002308127.1. XM_002308091.2.

    Genome annotation databases

    EnsemblPlantsiPOPTR_0006s07780.1; POPTR_0006s07780.1; POPTR_0006s07780.
    GeneIDi7485516.
    KEGGipop:POPTR_0006s07780g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CM000342 Genomic DNA. Translation: EEE91650.1 .
    RefSeqi XP_002308127.1. XM_002308091.2.

    3D structure databases

    ProteinModelPortali B9HBA8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3694.estExt_fgenesh4_pm.C_LG_VI0248.

    Proteomic databases

    PRIDEi B9HBA8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi POPTR_0006s07780.1 ; POPTR_0006s07780.1 ; POPTR_0006s07780 .
    GeneIDi 7485516.
    KEGGi pop:POPTR_0006s07780g.

    Phylogenomic databases

    eggNOGi COG0439.
    HOGENOMi HOG000008988.
    KOi K01961.
    OMAi ENIRHEM.

    Enzyme and pathway databases

    UniPathwayi UPA00655 ; UER00711 .

    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 genome of black cottonwood, Populus trichocarpa (Torr. & Gray)."
      Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I., Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J., Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W., Brun A.
      , Brunner A., Busov V., Campbell M., Carlson J., Chalot M., Chapman J., Chen G.-L., Cooper D., Coutinho P.M., Couturier J., Covert S., Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A., dePamphilis C.W., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J., Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J., Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F., Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., Martin F., Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O., Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J., Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J., Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A., Tsai C.-J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S., Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y., Rokhsar D.S.
      Science 313:1596-1604(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Nisqually.
    2. Cited for: GENOME REANNOTATION.
      Strain: cv. Nisqually.

    Entry informationi

    Entry nameiACCC1_POPTR
    AccessioniPrimary (citable) accession number: B9HBA8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 2, 2010
    Last sequence update: March 24, 2009
    Last modified: October 1, 2014
    This is version 42 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3