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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha, chloroplastic

Gene

ACCA

Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA (By similarity).By similarity

Catalytic activityi

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

Enzyme regulationi

Activated by reductants such as dithiothreitol (DTT), and by thioredoxin in vivo, following exposure to light.2 Publications

Kineticsi

    1. Vmax=151 nmol/min/mg enzyme1 Publication

    Pathwayi: malonyl-CoA biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.
    Proteins known to be involved in this subpathway in this organism are:
    1. Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic (accD), Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha, chloroplastic (ACCA), Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic (accD)
    This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00655; UER00711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha, chloroplastic (EC:6.4.1.2)
    Short name:
    ACCase subunit alpha
    Short name:
    Acetyl-CoA carboxylase carboxyltransferase subunit alpha
    Alternative name(s):
    pIEP96
    Gene namesi
    Name:ACCA
    OrganismiPisum sativum (Garden pea)
    Taxonomic identifieri3888 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Membrane, Plastid, Plastid inner membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi297 – 2971C → A: Loss of 30% of carboxyltransferase activity in E.coli. 1 Publication
    Mutagenesisi317 – 3171C → A: Loss of redox control, also 20% loss of carboxyltransferase activity in E.coli. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5050Chloroplast1 PublicationAdd
    BLAST
    Chaini51 – 875825Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha, chloroplasticPRO_0000389652Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi317 – 317Interchain (with C-442 in beta subunit)1 Publication

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Developmental stagei

    Activity is highest in chloroplasts isolated from young, actively dividing leaves (at protein level).1 Publication

    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).1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ41008.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili664 – 70542Sequence analysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the AccA family.Curated

    Keywords - Domaini

    Coiled coil, Transit peptide

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    HAMAPiMF_00823. AcetylCoA_CT_alpha. 1 hit.
    InterProiIPR001095. Acetyl_CoA_COase_a_su.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    [Graphical view]
    PfamiPF03255. ACCA. 1 hit.
    [Graphical view]
    PRINTSiPR01069. ACCCTRFRASEA.
    SUPFAMiSSF52096. SSF52096. 1 hit.
    TIGRFAMsiTIGR00513. accA. 1 hit.
    PROSITEiPS50989. COA_CT_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q41008-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MASSSATLVG STASDLLRSS TTGFTGVPLR TLGRAGLVLK RRDLTVSVTA
    60 70 80 90 100
    KLRKVKRREY PWSSNPDPNM KGGRLRHLST FQPLKQPPKP VILEFEKPLI
    110 120 130 140 150
    NMEKKINDFR KVAEKTGVDL SDQILALEAK YQKALVELYT NLTPIQRVTV
    160 170 180 190 200
    ARHPNRPTFL DHMYNMTEKF VELHGDREGY DDPAIAAGLG SIDGKTYMFI
    210 220 230 240 250
    GHQKGRDTKE NIKRNFAMPT PHGYRKALRL MEYADHHGFP IVTFIDTPGA
    260 270 280 290 300
    FADLKSEQLG QGEAIAHNLR SMFALKVPVI SIVIGEGGSG GALAIGCANK
    310 320 330 340 350
    LLMLENSVFF VAMPEACGAI LWKSNKAAPK AAERLKITAS ALLDLEIADG
    360 370 380 390 400
    IIPEPLAGAH TDPSWMSQQI KIAINEAMDE LTKLSTEDLI KDRMHKFRKL
    410 420 430 440 450
    GVDGIQEGIP LVPSKKVNTK KREIGVPPKR QEVPIPDSQI EAEIEKLKKA
    460 470 480 490 500
    IFEGEDSSAA KKNPGSQIGS AIDKLKGLFL EGKDSSAAKK TPGSQIVAEL
    510 520 530 540 550
    DKLKGLYLEA KDSSAAKVPG SQIVAEIEKL KNSIFEDEDS SSAVLPEKIP
    560 570 580 590 600
    GSEIAVEIAK LKKNILEGKD SSSEPSKLDL DKTIETLKRE VNREFSEAVK
    610 620 630 640 650
    AAGLTKTLTK LRGEISKAKA GNQPLTPLLK VEIKSFNQRL SAAPNSRKLL
    660 670 680 690 700
    KKRGLLREVT KVKLLLDKNK AATRKQELKK KSDEHKEAAR LEQELKKKFD
    710 720 730 740 750
    EVMDTPRIKE KYEALRSEVR RVDASSGSGL DDELKKKIIE FNKEVDLELA
    760 770 780 790 800
    TAVKSVGLEV ESVKPGHGWN KSSVPEIEEL NKDVQKEIEI VANSSPNVKR
    810 820 830 840 850
    LIEQLKLEVA KSGGKPDSES KSRIDALTQQ IKKSLAEAVD SPSLKEKYEN
    860 870
    LTRPAGDTLT DDKLREKVGV NRNFS
    Length:875
    Mass (Da):96,421
    Last modified:November 1, 1996 - v1
    Checksum:i61CE277A9FC3E7C9
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti313 – 3131M → S in strain: cv. Miranda. 1 Publication
    Natural varianti452 – 4521F → L in strain: cv. Miranda. 1 Publication
    Natural varianti631 – 6311V → E in strain: cv. Miranda. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z31559 mRNA. Translation: CAA83434.1.
    AB029556 mRNA. Translation: BAA94752.1.
    PIRiS56667.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z31559 mRNA. Translation: CAA83434.1.
    AB029556 mRNA. Translation: BAA94752.1.
    PIRiS56667.

    3D structure databases

    ProteinModelPortaliQ41008.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00655; UER00711.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    HAMAPiMF_00823. AcetylCoA_CT_alpha. 1 hit.
    InterProiIPR001095. Acetyl_CoA_COase_a_su.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    [Graphical view]
    PfamiPF03255. ACCA. 1 hit.
    [Graphical view]
    PRINTSiPR01069. ACCCTRFRASEA.
    SUPFAMiSSF52096. SSF52096. 1 hit.
    TIGRFAMsiTIGR00513. accA. 1 hit.
    PROSITEiPS50989. COA_CT_CTER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiACCA_PEA
    AccessioniPrimary (citable) accession number: Q41008
    Secondary accession number(s): Q9MBB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2009
    Last sequence update: November 1, 1996
    Last modified: January 7, 2015
    This is version 65 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

    Direct protein sequencing

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.