GenomeNet

Database: UniProt
Entry: Q38970
LinkDB: Q38970
Original site: Q38970 
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   13-FEB-2019, entry version 148.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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
RT   carboxylase 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.,
RA   Ichikawa N.;
RT   "Genomic organization of 251 kDa acetyl-CoA carboxylase genes in
RT   Arabidopsis: tandem gene duplication has made two differentially
RT   expressed 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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Hayashizaki Y., 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
RT   region in 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
RT   to plastids of rapeseeds.";
RL   Plant Physiol. 113:75-81(1997).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9449673;
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
RT   control 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.,
RA   Allred C.C., 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.,
RA   Caboche M., Lepiniec L., Rochat C.;
RT   "Multifunctional acetyl-CoA carboxylase 1 is essential for very long
RT   chain 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
RP   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
RT   impaired 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.,
RA   Marion J., Molino D., Lima A., Bach L., Morin H., Tellier F.,
RA   Palauqui J.C., Bellec Y., Renne C., Miquel M., Dacosta M., Vignard J.,
RA   Rochat C., 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.,
RA   Yamazaki M., Tohge T., Fernie A.R.;
RT   "The flavonoid biosynthetic pathway in Arabidopsis: Structural and
RT   genetic diversity.";
RL   Plant Physiol. Biochem. 72:21-34(2013).
CC   -!- FUNCTION: Multifunctional enzyme that catalyzes the carboxylation
CC       of acetyl-CoA, forming malonyl-CoA, which is used in the plastid
CC       for fatty acid synthesis and in the cytosol in various
CC       biosynthetic pathways including fatty acid elongation. Required
CC       for very long chain fatty acids elongation. Necessary for embryo
CC       and plant development. Plays a central function in embryo
CC       morphogenesis, especially in apical meristem development. Involved
CC       in cell proliferation and tissue patterning. May act as a
CC       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(+) +
CC         malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         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] +
CC         phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
CC         Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
CC         ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000250|UniProtKB:O04983};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from 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
CC       development in tapetal cells and at stage 10 in the epidermal
CC       cells of growing petals and ovaries. In young siliques, expressed
CC       transiently in the inner integument of the ovules just prior to
CC       testal deposition. {ECO:0000269|PubMed:12376641}.
CC   -!- DISRUPTION PHENOTYPE: Embryo lethal with an arrest in development
CC       at the late globular stage in acc1-1 and acc1-2 null allele
CC       mutants. In the leaky pas3 and gk alleles, defect in embryo
CC       development, very short and thick hypocotyl and misshaped
CC       cotyledons that do not expand. Abnormal root development, abnormal
CC       fused leaves and compact rosettes with multiple shoots.
CC       Uncoordinated cell divisions in the apical region. Reduced levels
CC       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};
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   UniGene; At.39402; -.
DR   ProteinModelPortal; Q38970; -.
DR   SMR; Q38970; -.
DR   BioGrid; 25753; 4.
DR   IntAct; Q38970; 1.
DR   STRING; 3702.AT1G36160.1; -.
DR   iPTMnet; Q38970; -.
DR   PaxDb; Q38970; -.
DR   PRIDE; Q38970; -.
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   eggNOG; COG0439; LUCA.
DR   eggNOG; COG0511; LUCA.
DR   eggNOG; COG4799; LUCA.
DR   HOGENOM; HOG000214115; -.
DR   InParanoid; Q38970; -.
DR   KO; K11262; -.
DR   OMA; YLQVEHH; -.
DR   OrthoDB; 156081at2759; -.
DR   PhylomeDB; Q38970; -.
DR   BioCyc; ARA:AT1G36160-MONOMER; -.
DR   BioCyc; MetaCyc:AT1G36160-MONOMER; -.
DR   BRENDA; 6.4.1.2; 399.
DR   Reactome; R-ATH-163765; ChREBP activates metabolic gene expression.
DR   Reactome; R-ATH-196780; Biotin transport and metabolism.
DR   Reactome; R-ATH-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
DR   Reactome; R-ATH-75105; Fatty acyl-CoA biosynthesis.
DR   UniPathway; UPA00655; UER00711.
DR   PRO; PR:Q38970; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   Genevisible; Q38970; AT.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA: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: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; Complete proteome; Cytoplasm;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Ligase;
KW   Lipid biosynthesis; Lipid metabolism; Magnesium; Manganese;
KW   Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN         1   2254       Acetyl-CoA carboxylase 1.
FT                                /FTId=PRO_0000412211.
FT   DOMAIN       36    543       Biotin carboxylation.
FT   DOMAIN      189    381       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      670    744       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   DOMAIN     1492   1831       CoA carboxyltransferase N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01136}.
FT   DOMAIN     1835   2150       CoA carboxyltransferase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01137}.
FT   NP_BIND     215    272       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   REGION     1492   2150       Carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01138}.
FT   ACT_SITE    356    356       {ECO:0000250}.
FT   METAL       338    338       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       352    352       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       352    352       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       354    354       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   BINDING    1740   1740       Coenzyme A. {ECO:0000250}.
FT   BINDING    2041   2041       Coenzyme A. {ECO:0000250}.
FT   BINDING    2043   2043       Coenzyme A. {ECO:0000250}.
FT   MOD_RES     711    711       N6-biotinyllysine. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   MOD_RES    1031   1031       Phosphothreonine.
FT                                {ECO:0000244|PubMed:19376835}.
FT   MOD_RES    1192   1192       Phosphoserine.
FT                                {ECO:0000244|PubMed:19376835}.
FT   MUTAGEN    1588   1588       E->K: In pas3-1; developmental phenotype
FT                                and reduced levels of very long chain
FT                                fatty acids in seeds.
FT                                {ECO:0000269|PubMed:15088065}.
FT   MUTAGEN    1787   1787       G->S: In pas3-2; developmental phenotype
FT                                and reduced levels of very long chain
FT                                fatty acids in seeds.
FT                                {ECO:0000269|PubMed:15088065}.
FT   CONFLICT    337    337       V -> I (in Ref. 1; AAC41645 and 2;
FT                                AAG40563). {ECO:0000305}.
FT   CONFLICT   1378   1379       EQ -> DE (in Ref. 1; AAC41645 and 2;
FT                                AAG40563). {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
//
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