ACCA_ARATH
ID ACCA_ARATH Reviewed; 769 AA.
AC Q9LD43; Q56YX0;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha, chloroplastic;
DE Short=ACCase subunit alpha;
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha;
DE EC=2.1.3.15;
DE Flags: Precursor;
GN Name=CAC3; OrderedLocusNames=At2g38040; ORFNames=T8P21.5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBUNIT, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=10759501; DOI=10.1104/pp.122.4.1057;
RA Ke J., Wen T.N., Nikolau B.J., Wurtele E.S.;
RT "Coordinate regulation of the nuclear and plastidic genes coding for the
RT subunits of the heteromeric acetyl-coenzyme A carboxylase.";
RL Plant Physiol. 122:1057-1071(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex.
CC First, biotin carboxylase catalyzes the carboxylation of biotin on its
CC carrier protein (BCCP) and then the CO(2) group is transferred by the
CC carboxyltransferase to acetyl-CoA to form malonyl-CoA (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-
CC CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728,
CC Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC carboxyl carrier protein, biotin carboxylase and two subunits each of
CC ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
CC {ECO:0000269|PubMed:10759501}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:10759501, ECO:0000269|PubMed:18431481}; Peripheral
CC membrane protein {ECO:0000269|PubMed:10759501,
CC ECO:0000269|PubMed:18431481}; Stromal side
CC {ECO:0000269|PubMed:10759501, ECO:0000269|PubMed:18431481}.
CC -!- TISSUE SPECIFICITY: Accumulates in fatty acids synthesizing tissues
CC such as embryos, expanding leaves, flower buds, flowers, and developing
CC siliques. {ECO:0000269|PubMed:10759501}.
CC -!- SIMILARITY: Belongs to the AccA family. {ECO:0000305}.
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DR EMBL; AF056969; AAF29414.1; -; mRNA.
DR EMBL; AF056970; AAF29415.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09482.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09483.1; -; Genomic_DNA.
DR EMBL; AK221200; BAD93727.1; -; mRNA.
DR RefSeq; NP_565880.1; NM_129360.4.
DR RefSeq; NP_850291.1; NM_179960.1.
DR AlphaFoldDB; Q9LD43; -.
DR SMR; Q9LD43; -.
DR BioGRID; 3726; 4.
DR STRING; 3702.AT2G38040.1; -.
DR iPTMnet; Q9LD43; -.
DR MetOSite; Q9LD43; -.
DR PaxDb; Q9LD43; -.
DR PRIDE; Q9LD43; -.
DR ProteomicsDB; 244568; -.
DR EnsemblPlants; AT2G38040.1; AT2G38040.1; AT2G38040.
DR EnsemblPlants; AT2G38040.2; AT2G38040.2; AT2G38040.
DR GeneID; 818382; -.
DR Gramene; AT2G38040.1; AT2G38040.1; AT2G38040.
DR Gramene; AT2G38040.2; AT2G38040.2; AT2G38040.
DR KEGG; ath:AT2G38040; -.
DR Araport; AT2G38040; -.
DR TAIR; locus:2065654; AT2G38040.
DR eggNOG; ENOG502QPRP; Eukaryota.
DR HOGENOM; CLU_014866_2_0_1; -.
DR InParanoid; Q9LD43; -.
DR OMA; FNNEITT; -.
DR OrthoDB; 276611at2759; -.
DR PhylomeDB; Q9LD43; -.
DR BioCyc; ARA:AT2G38040-MON; -.
DR BioCyc; MetaCyc:AT2G38040-MON; -.
DR BRENDA; 2.1.3.15; 399.
DR UniPathway; UPA00655; UER00711.
DR PRO; PR:Q9LD43; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9LD43; baseline and differential.
DR Genevisible; Q9LD43; AT.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_00823; AcetylCoA_CT_alpha; 1.
DR InterPro; IPR001095; Acetyl_CoA_COase_a_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR PANTHER; PTHR42853; PTHR42853; 1.
DR Pfam; PF03255; ACCA; 1.
DR PRINTS; PR01069; ACCCTRFRASEA.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR00513; accA; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Coiled coil; Disulfide bond;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Nucleotide-binding; Phosphoprotein; Plastid;
KW Plastid inner membrane; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 55..769
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit alpha, chloroplastic"
FT /id="PRO_0000391770"
FT DOMAIN 132..385
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 718..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 426..504
FT /evidence="ECO:0000255"
FT COILED 631..744
FT /evidence="ECO:0000255"
FT COMPBIAS 721..741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..757
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT DISULFID 322
FT /note="Interchain (with C-442 in beta subunit)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="M -> I (in Ref. 4; BAD93727)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 769 AA; 85306 MW; FDE16D95B4C774D0 CRC64;
MASISHSSLA LGGASSASAS DYLRSSSNGV NGVPLKTLGR AVFTTIRRKD LAVTSRLKKG
KKFEHPWPAN PDPNVKGGVL SYLAEFKPLG DTQKPVTLDF EKPLVELEKK IVDVRKMANE
TGLDFTEQII TLENKYRQAL KDLYTHLTPI QRVNIARHPN RPTFLDHIHN ITDKFMELHG
DRAGYDDPAI VTGIGTIDGK RYMFIGHQKG RNTKENIMRN FGMPTPHGYR KALRMMYYAD
HHGFPIVTFI DTPGAYADLK SEELGQGEAI ANNLRTMFGL KVPILSIVIG EGGSGGALAI
GCANKMLMLE NAVFYVASPE ACAAILWKTS KAAPEAAEKL RITSKELVKL NVADGIIPEP
LGGAHADPSW TSQQIKIAIN ENMNEFGKMS GEELLKHRMA KYRKIGVFIE GEPIEPSRKI
NMKKREAVFS DSRKLQGEVD KLKEQILKAK ETSTEAEPSS EVLNEMIEKL KSEIDDEYTE
AAIAVGLEER LTAMREEFSK ASSEEHLMHP VLIEKIEKLK EEFNTRLTDA PNYESLKSKL
NMLRDFSRAK AASEATSLKK EINKRFQEAV DRPEIREKVE AIKAEVASSG ASSFDELPDA
LKEKVLKTKG EVEAEMAGVL KSMGLELDAV KQNQKDTAEQ IYAANENLQE KLEKLNQEIT
SKIEEVVRTP EIKSMVELLK VETAKASKTP GVTEAYQKIE ALEQQIKQKI AEALNTSGLQ
EKQDELEKEL AAARELAAEE SDGSVKEDDD DDEDSSESGK SEMVNPSFA
