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Q31796

- ACCD_ANTFO

UniProt

Q31796 - ACCD_ANTFO

Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic

Gene

accD

Organism
Anthoceros formosae (Hornwort)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 2 (28 Feb 2003)
      Previous versions | rss
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    Functioni

    Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.UniRule annotation

    Catalytic activityi

    ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.UniRule annotation

    Cofactori

    Binds 1 zinc ion per subunit.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi51 – 511ZincUniRule annotation
    Metal bindingi54 – 541ZincUniRule annotation
    Metal bindingi70 – 701ZincUniRule annotation
    Metal bindingi73 – 731ZincUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri51 – 7323C4-typeUniRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. acetyl-CoA carboxylase activity Source: UniProtKB-HAMAP
    2. ATP binding Source: UniProtKB-KW
    3. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-HAMAP
    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, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00655; UER00711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticUniRule annotation (EC:6.4.1.2UniRule annotation)
    Short name:
    ACCase subunit betaUniRule annotation
    Short name:
    Acetyl-CoA carboxylase carboxyltransferase subunit betaUniRule annotation
    Gene namesi
    Name:accDUniRule annotation
    Encoded oniPlastid; Chloroplast
    OrganismiAnthoceros formosae (Hornwort)
    Taxonomic identifieri48387 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaAnthocerotophytaAnthocerotopsidaAnthocerotidaeAnthocerotalesAnthocerotaceaeAnthoceros

    Subcellular locationi

    Plastidchloroplast stroma UniRule annotation

    GO - Cellular componenti

    1. acetyl-CoA carboxylase complex Source: InterPro
    2. chloroplast stroma Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 313313Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticPRO_0000199779Add
    BLAST

    Interactioni

    Subunit structurei

    Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein, biotin carboxylase and 2 subunits each of ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ31796.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AccD/PCCB family.UniRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri51 – 7323C4-typeUniRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    HAMAPiMF_01395. AcetylCoA_CT_beta.
    InterProiIPR000438. Acetyl_CoA_COase_Trfase_b_su.
    IPR000022. Carboxyl_trans.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011762. COA_CT_N.
    [Graphical view]
    PfamiPF01039. Carboxyl_trans. 1 hit.
    [Graphical view]
    PRINTSiPR01070. ACCCTRFRASEB.
    SUPFAMiSSF52096. SSF52096. 1 hit.
    TIGRFAMsiTIGR00515. accD. 1 hit.
    PROSITEiPS50980. COA_CT_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q31796-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLMNWFEDR RKFSGLIGAF IEKATKGYIL SERRKDRHIK IDTTKGLWTR    50
    CDNCENMLYI RFLRQNKRIC EECGYHLQMS STERIESLID RGTWHPMDED 100
    MVARDALKFS DEDSYKNRVL FYQKRTGLTD AIQTGIGKLN GIPIALGVMD 150
    FQFMGGSMGS VVGEKITRLI EYGTRESMPV IIVCSSGGAR MQEGTLSLMQ 200
    MAKISAVLQI HQAQKKLLYI AILTYPTTGG VTASFGMLGD VIIAEPKAYI 250
    AFAGKRVIEQ TLRQKIPDGS QVAESLFDHG LLDLIVPRNL LRGVLSEIFE 300
    LYSSAPCRRS NNS 313
    Length:313
    Mass (Da):35,272
    Last modified:February 28, 2003 - v2
    Checksum:i6881B7B5FF780126
    GO

    RNA editingi

    The nonsense codons at positions 50, 78, 104, 260 and 264 are modified to sense codons.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB086179 Genomic DNA. Translation: BAC55358.1.
    AB087450 mRNA. Translation: BAC55454.1.
    D43695 Genomic DNA. Translation: BAA07797.1. Sequence problems.
    PIRiS71147.
    RefSeqiNP_777422.1. NC_004543.1.

    Genome annotation databases

    GeneIDi2553479.

    Keywords - Coding sequence diversityi

    RNA editing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB086179 Genomic DNA. Translation: BAC55358.1 .
    AB087450 mRNA. Translation: BAC55454.1 .
    D43695 Genomic DNA. Translation: BAA07797.1 . Sequence problems.
    PIRi S71147.
    RefSeqi NP_777422.1. NC_004543.1.

    3D structure databases

    ProteinModelPortali Q31796.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2553479.

    Enzyme and pathway databases

    UniPathwayi UPA00655 ; UER00711 .

    Family and domain databases

    Gene3Di 3.90.226.10. 1 hit.
    HAMAPi MF_01395. AcetylCoA_CT_beta.
    InterProi IPR000438. Acetyl_CoA_COase_Trfase_b_su.
    IPR000022. Carboxyl_trans.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011762. COA_CT_N.
    [Graphical view ]
    Pfami PF01039. Carboxyl_trans. 1 hit.
    [Graphical view ]
    PRINTSi PR01070. ACCCTRFRASEB.
    SUPFAMi SSF52096. SSF52096. 1 hit.
    TIGRFAMsi TIGR00515. accD. 1 hit.
    PROSITEi PS50980. COA_CT_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete nucleotide sequence of the hornwort (Anthoceros formosae) chloroplast genome: insight into the earliest land plants."
      Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.
      Nucleic Acids Res. 31:716-721(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], RNA EDITING.
    2. "RNA editing in hornwort chloroplasts makes more than half the genes functional."
      Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.
      Nucleic Acids Res. 31:2417-2423(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], RNA EDITING.
      Tissue: Thallus.
    3. "Extensive RNA editing of U to C in addition to C to U substitution in the rbcL transcripts of hornwort chloroplasts and the origin of RNA editing in green plants."
      Yoshinaga K., Iinuma H., Masuzawa T., Ueda K.
      Nucleic Acids Res. 24:1008-1014(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-91.
      Tissue: Thallus.

    Entry informationi

    Entry nameiACCD_ANTFO
    AccessioniPrimary (citable) accession number: Q31796
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 28, 2003
    Last modified: October 1, 2014
    This is version 78 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3