ACC1_ARATH
ID ACC1_ARATH Reviewed; 2254 AA.
AC Q38970; Q0WNF3; Q38971; Q9C8G1; Q9SKV1;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Acetyl-CoA carboxylase 1;
DE Short=AtACC1;
DE EC=6.4.1.2 {ECO:0000269|PubMed:9008389};
DE AltName: Full=Protein EMBRYO DEFECTIVE 22;
DE AltName: Full=Protein GURKE;
DE AltName: Full=Protein PASTICCINO 3;
DE Includes:
DE RecName: Full=Biotin carboxylase;
DE EC=6.3.4.14;
GN Name=ACC1; Synonyms=EMB22, GK, PAS3; OrderedLocusNames=At1g36160;
GN ORFNames=F15C21.1;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=7915036; DOI=10.1104/pp.105.2.611;
RA Roesler K.R., Shorrosh B.S., Ohlrogge J.B.;
RT "Structure and expression of an Arabidopsis acetyl-coenzyme A carboxylase
RT gene.";
RL Plant Physiol. 105:611-617(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=7551584; DOI=10.1093/oxfordjournals.pcp.a078822;
RA Yanai Y., Kawasaki T., Shimada H., Wurtele E.S., Nikolau B.J., Ichikawa N.;
RT "Genomic organization of 251 kDa acetyl-CoA carboxylase genes in
RT Arabidopsis: tandem gene duplication has made two differentially expressed
RT isozymes.";
RL Plant Cell Physiol. 36:779-787(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1246-2254.
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=9011083; DOI=10.1046/j.1365-313x.1996.10061005.x;
RA Torres-Ruiz R.A., Lohner A., Juergens G.;
RT "The GURKE gene is required for normal organization of the apical region in
RT the Arabidopsis embryo.";
RL Plant J. 10:1005-1016(1996).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY AS ACETYL-COA CARBOXYLASE.
RX PubMed=9008389; DOI=10.1104/pp.113.1.75;
RA Roesler K., Shintani D., Savage L., Boddupalli S., Ohlrogge J.;
RT "Targeting of the Arabidopsis homomeric acetyl-coenzyme A carboxylase to
RT plastids of rapeseeds.";
RL Plant Physiol. 113:75-81(1997).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9449673; DOI=10.1242/dev.125.5.909;
RA Faure J.-D., Vittorioso P., Santoni V., Fraisier V., Prinsen E.,
RA Barlier I., Van Onckelen H., Caboche M., Bellini C.;
RT "The PASTICCINO genes of Arabidopsis thaliana are involved in the control
RT of cell division and differentiation.";
RL Development 125:909-918(1998).
RN [9]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12376641; DOI=10.1104/pp.008110;
RA Fatland B.L., Ke J., Anderson M.D., Mentzen W.I., Cui L.W., Allred C.C.,
RA Johnston J.L., Nikolau B.J., Wurtele E.S.;
RT "Molecular characterization of a heteromeric ATP-citrate lyase that
RT generates cytosolic acetyl-coenzyme A in Arabidopsis.";
RL Plant Physiol. 130:740-756(2002).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=12943542; DOI=10.1046/j.1365-313x.2003.016010.x;
RA Baud S., Guyon V., Kronenberger J., Wuilleme S., Miquel M., Caboche M.,
RA Lepiniec L., Rochat C.;
RT "Multifunctional acetyl-CoA carboxylase 1 is essential for very long chain
RT fatty acid elongation and embryo development in Arabidopsis.";
RL Plant J. 33:75-86(2003).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-1588 AND GLY-1787.
RC STRAIN=cv. Wassilewskija;
RX PubMed=15088065; DOI=10.1038/sj.embor.7400124;
RA Baud S., Bellec Y., Miquel M., Bellini C., Caboche M., Lepiniec L.,
RA Faure J.D., Rochat C.;
RT "gurke and pasticcino3 mutants affected in embryo development are impaired
RT in acetyl-CoA carboxylase.";
RL EMBO Rep. 5:515-520(2004).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15509834; DOI=10.1093/pcp/pch148;
RA Kajiwara T., Furutani M., Hibara K., Tasaka M.;
RT "The GURKE gene encoding an acetyl-CoA carboxylase is required for
RT partitioning the embryo apex into three subregions in Arabidopsis.";
RL Plant Cell Physiol. 45:1122-1128(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1031 AND SER-1192, AND
RP IDENTIFICATION BY 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).
RN [14]
RP FUNCTION.
RX PubMed=20145257; DOI=10.1105/tpc.109.071209;
RA Roudier F., Gissot L., Beaudoin F., Haslam R., Michaelson L., Marion J.,
RA Molino D., Lima A., Bach L., Morin H., Tellier F., Palauqui J.C.,
RA Bellec Y., Renne C., Miquel M., Dacosta M., Vignard J., Rochat C.,
RA Markham J.E., Moreau P., Napier J., Faure J.D.;
RT "Very-long-chain fatty acids are involved in polar auxin transport and
RT developmental patterning in Arabidopsis.";
RL Plant Cell 22:364-375(2010).
RN [15]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
CC -!- FUNCTION: Multifunctional enzyme that catalyzes the carboxylation of
CC acetyl-CoA, forming malonyl-CoA, which is used in the plastid for fatty
CC acid synthesis and in the cytosol in various biosynthetic pathways
CC including fatty acid elongation. Required for very long chain fatty
CC acids elongation. Necessary for embryo and plant development. Plays a
CC central function in embryo morphogenesis, especially in apical meristem
CC development. Involved in cell proliferation and tissue patterning. May
CC act as a repressor of cytokinin response. {ECO:0000269|PubMed:12943542,
CC ECO:0000269|PubMed:15088065, ECO:0000269|PubMed:15509834,
CC ECO:0000269|PubMed:20145257, ECO:0000269|PubMed:9008389,
CC ECO:0000269|PubMed:9449673}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-
CC CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;
CC Evidence={ECO:0000269|PubMed:9008389};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000250|UniProtKB:O04983};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01066};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC ECO:0000255|PROSITE-ProRule:PRU00969};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC ECO:0000255|PROSITE-ProRule:PRU00969};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-
CC ProRule:PRU00969};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, trichomes, epidermal leaf
CC cells, siliques, petals, anthers, and seeds.
CC {ECO:0000269|PubMed:12376641, ECO:0000269|PubMed:12943542,
CC ECO:0000269|PubMed:7551584, ECO:0000269|PubMed:7915036}.
CC -!- DEVELOPMENTAL STAGE: Expressed in flower buds at stage 6 of development
CC in tapetal cells and at stage 10 in the epidermal cells of growing
CC petals and ovaries. In young siliques, expressed transiently in the
CC inner integument of the ovules just prior to testal deposition.
CC {ECO:0000269|PubMed:12376641}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethal with an arrest in development at
CC the late globular stage in acc1-1 and acc1-2 null allele mutants. In
CC the leaky pas3 and gk alleles, defect in embryo development, very short
CC and thick hypocotyl and misshaped cotyledons that do not expand.
CC Abnormal root development, abnormal fused leaves and compact rosettes
CC with multiple shoots. Uncoordinated cell divisions in the apical
CC region. Reduced levels of very long chain fatty acids in seeds.
CC {ECO:0000269|PubMed:12943542, ECO:0000269|PubMed:15088065,
CC ECO:0000269|PubMed:15509834, ECO:0000269|PubMed:9011083,
CC ECO:0000269|PubMed:9449673}.
CC -!- MISCELLANEOUS: The acc1-1 and pas3-1 mutants can be partially
CC complemented by exogenous supply of malonate.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF18638.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG51250.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; L27074; AAC41645.1; -; Genomic_DNA.
DR EMBL; D34630; BAA07012.1; -; mRNA.
DR EMBL; AF062308; AAG40563.1; -; Genomic_DNA.
DR EMBL; AC006228; AAF18638.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AC025781; AAG51250.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31849.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31850.1; -; Genomic_DNA.
DR EMBL; AK229488; BAF01346.1; -; mRNA.
DR PIR; D86483; D86483.
DR RefSeq; NP_001185143.1; NM_001198214.2.
DR RefSeq; NP_174849.2; NM_103313.4.
DR AlphaFoldDB; Q38970; -.
DR SMR; Q38970; -.
DR BioGRID; 25753; 4.
DR IntAct; Q38970; 1.
DR STRING; 3702.AT1G36160.2; -.
DR iPTMnet; Q38970; -.
DR PaxDb; Q38970; -.
DR PRIDE; Q38970; -.
DR ProteomicsDB; 244566; -.
DR EnsemblPlants; AT1G36160.1; AT1G36160.1; AT1G36160.
DR EnsemblPlants; AT1G36160.2; AT1G36160.2; AT1G36160.
DR GeneID; 840521; -.
DR Gramene; AT1G36160.1; AT1G36160.1; AT1G36160.
DR Gramene; AT1G36160.2; AT1G36160.2; AT1G36160.
DR KEGG; ath:AT1G36160; -.
DR Araport; AT1G36160; -.
DR TAIR; locus:2034310; AT1G36160.
DR eggNOG; KOG0368; Eukaryota.
DR HOGENOM; CLU_000395_5_2_1; -.
DR InParanoid; Q38970; -.
DR OMA; CGRDSTL; -.
DR OrthoDB; 156081at2759; -.
DR PhylomeDB; Q38970; -.
DR BioCyc; ARA:AT1G36160-MON; -.
DR BioCyc; MetaCyc:AT1G36160-MON; -.
DR BRENDA; 6.4.1.2; 399.
DR UniPathway; UPA00655; UER00711.
DR PRO; PR:Q38970; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q38970; baseline and differential.
DR Genevisible; Q38970; AT.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; ISS:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0030497; P:fatty acid elongation; IMP:TAIR.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009933; P:meristem structural organization; IMP:TAIR.
DR GO; GO:0010072; P:primary shoot apical meristem specification; IMP:TAIR.
DR GO; GO:0009735; P:response to cytokinin; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0048367; P:shoot system development; IMP:TAIR.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR013537; AcCoA_COase_cen.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF08326; ACC_central; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52096; SSF52096; 2.
DR SUPFAM; SSF52440; SSF52440; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; ATP-binding; Biotin; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..2254
FT /note="Acetyl-CoA carboxylase 1"
FT /id="PRO_0000412211"
FT DOMAIN 36..543
FT /note="Biotin carboxylation"
FT DOMAIN 189..381
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 670..744
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 1492..1831
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 1835..2150
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 1492..2150
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT ACT_SITE 356
FT /evidence="ECO:0000250"
FT BINDING 215..272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 338
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 352
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 352
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 354
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 354
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 1740
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 2041
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 2043
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT MOD_RES 711
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 1031
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 1192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MUTAGEN 1588
FT /note="E->K: In pas3-1; developmental phenotype and reduced
FT levels of very long chain fatty acids in seeds."
FT /evidence="ECO:0000269|PubMed:15088065"
FT MUTAGEN 1787
FT /note="G->S: In pas3-2; developmental phenotype and reduced
FT levels of very long chain fatty acids in seeds."
FT /evidence="ECO:0000269|PubMed:15088065"
FT CONFLICT 337
FT /note="V -> I (in Ref. 1; AAC41645 and 2; AAG40563)"
FT /evidence="ECO:0000305"
FT CONFLICT 1378..1379
FT /note="EQ -> DE (in Ref. 1; AAC41645 and 2; AAG40563)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2254 AA; 251382 MW; F00A5AE316CC5E87 CRC64;
MAGSVNGNHS AVGPGINYET VSQVDEFCKA LRGKRPIHSI LIANNGMAAV KFIRSVRTWA
YETFGTEKAI LLVGMATPED MRINAEHIRI ADQFVEVPGG TNNNNYANVQ LIVEMAEVTR
VDAVWPGWGH ASENPELPDA LDAKGIIFLG PPASSMAALG DKIGSSLIAQ AADVPTLPWS
GSHVKIPPNS NLVTIPEEIY RQACVYTTEE AIASCQVVGY PAMIKASWGG GGKGIRKVHN
DDEVRALFKQ VQGEVPGSPI FIMKVASQSR HLEVQLLCDK HGNVSALHSR DCSVQRRHQK
IIEEGPITVA PPETVKKLEQ AARRLAKSVN YVGAATVEYL YSMDTGEYYF LELNPRLQVE
HPVTEWIAEI NLPAAQVAVG MGIPLWQIPE IRRFYGIEHG GGYDSWRKTS VVAFPFDFDK
AQSIRPKGHC VAVRVTSEDP DDGFKPTSGR VQELSFKSKP NVWAYFSVKS GGGIHEFSDS
QFGHVFAFGE SRALAIANMV LGLKEIQIRG EIRTNVDYTI DLLHASDYRD NKIHTGWLDS
RIAMRVRAER PPWYLSVVGG ALYKASATSA AVVSDYVGYL EKGQIPPKHI SLVHSQVSLN
IEGSKYTIDV VRGGSGTYRL RMNKSEVVAE IHTLRDGGLL MQLDGKSHVI YAEEEAAGTR
LLIDGRTCLL QNDHDPSKLM AETPCKLMRY LISDNSNIDA DTPYAEVEVM KMCMPLLSPA
SGVIHFKMSE GQAMQAGELI ANLDLDDPSA VRKAEPFHGS FPRLGLPTAI SGRVHQRCAA
TLNAARMILA GYEHKVDEVV QDLLNCLDSP ELPFLQWQEC FAVLATRLPK NLRNMLESKY
REFESISRNS LTTDFPAKLL KGILEAHLSS CDEKERGALE RLIEPLMSLA KSYEGGRESH
ARVIVHSLFE EYLSVEELFN DNMLADVIER MRQLYKKDLL KIVDIVLSHQ GIKNKNKLVL
RLMEQLVYPN PAAYRDKLIR FSTLNHTNYS ELALKASQLL EQTKLSELRS NIARSLSELE
MFTEDGENMD TPKRKSAINE RIEDLVSASL AVEDALVGLF DHSDHTLQRR VVETYIRRLY
QPYVVKDSVR MQWHRSGLLA SWEFLEEHME RKNIGLDDPD TSEKGLVEKR SKRKWGAMVI
IKSLQFLPSI ISAALRETKH NDYETAGAPL SGNMMHIAIV GINNQMSLLQ DSGDEDQAQE
RVNKLAKILK EEEVSSSLCS AGVGVISCII QRDEGRTPMR HSFHWSLEKQ YYVEEPLLRH
LEPPLSIYLE LDKLKGYSNI QYTPSRDRQW HLYTVTDKPV PIKRMFLRSL VRQATMNDGF
ILQQGQDKQL SQTLISMAFT SKCVLRSLMD AMEELELNAH NAAMKPDHAH MFLCILREQQ
IDDLVPFPRR VEVNAEDEET TVEMILEEAA REIHRSVGVR MHRLGVCEWE VRLWLVSSGL
ACGAWRVVVA NVTGRTCTVH IYREVETPGR NSLIYHSITK KGPLHETPIS DQYKPLGYLD
RQRLAARRSN TTYCYDFPLA FGTALELLWA SQHPGVKKPY KDTLINVKEL VFSKPEGSSG
TSLDLVERPP GLNDFGMVAW CLDMSTPEFP MGRKLLVIAN DVTFKAGSFG PREDAFFLAV
TELACAKKLP LIYLAANSGA RLGVAEEVKA CFKVGWSDEI SPENGFQYIY LSPEDHERIG
SSVIAHEVKL SSGETRWVID TIVGKEDGIG VENLTGSGAI AGAYSKAYNE TFTLTFVSGR
TVGIGAYLAR LGMRCIQRLD QPIILTGFST LNKLLGREVY SSHMQLGGPK IMGTNGVVHL
TVSDDLEGVS AILNWLSYIP AYVGGPLPVL APLDPPERIV EYVPENSCDP RAAIAGVKDN
TGKWLGGIFD KNSFIETLEG WARTVVTGRA KLGGIPVGVV AVETQTVMQI IPADPGQLDS
HERVVPQAGQ VWFPDSAAKT AQALMDFNRE ELPLFILANW RGFSGGQRDL FEGILQAGST
IVENLRTYRQ PVFVYIPMMG ELRGGAWVVV DSQINSDYVE MYADETARGN VLEPEGTIEI
KFRTKELLEC MGRLDQKLIS LKAKLQDAKQ SEAYANIELL QQQIKAREKQ LLPVYIQIAT
KFAELHDTSM RMAAKGVIKS VVEWSGSRSF FYKKLNRRIA ESSLVKNVRE ASGDNLAYKS
SMRLIQDWFC NSDIAKGKEE AWTDDQVFFT WKDNVSNYEL KLSELRAQKL LNQLAEIGNS
SDLQALPQGL ANLLNKVEPS KREELVAAIR KVLG
