KCS21_ARATH
ID KCS21_ARATH Reviewed; 464 AA.
AC Q9FH27;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable 3-ketoacyl-CoA synthase 21 {ECO:0000303|PubMed:18465198};
DE Short=KCS-21 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000305};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 21 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 21 {ECO:0000303|PubMed:18465198};
GN Name=KCS21 {ECO:0000303|PubMed:18465198};
GN Synonyms=KCS20 {ECO:0000305|PubMed:12916765};
GN OrderedLocusNames=At5g49070 {ECO:0000312|Araport:AT5G49070};
GN ORFNames=K20J1.4 {ECO:0000312|EMBL:BAB10089.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
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 [3]
RP INDUCTION, AND GENE FAMILY.
RX PubMed=12916765; DOI=10.1002/ps.714;
RA Lechelt-Kunze C., Meissner R.C., Drewes M., Tietjen K.;
RT "Flufenacet herbicide treatment phenocopies the fiddlehead mutant in
RT Arabidopsis thaliana.";
RL Pest Manag. Sci. 59:847-856(2003).
RN [4]
RP GENE FAMILY, NOMENCLATURE, 3D-STRUCTURE MODELING, AND TISSUE SPECIFICITY.
RX PubMed=18465198; DOI=10.1007/s11103-008-9339-z;
RA Joubes J., Raffaele S., Bourdenx B., Garcia C., Laroche-Traineau J.,
RA Moreau P., Domergue F., Lessire R.;
RT "The VLCFA elongase gene family in Arabidopsis thaliana: phylogenetic
RT analysis, 3D modelling and expression profiling.";
RL Plant Mol. Biol. 67:547-566(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-
CC chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736;
CC EC=2.3.1.199; Evidence={ECO:0000305};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FH27-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in flowers.
CC {ECO:0000269|PubMed:18465198}.
CC -!- INDUCTION: Repressed by herbicides such as flufenacet and benfuresate.
CC {ECO:0000269|PubMed:12916765}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; AB023028; BAB10089.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95768.1; -; Genomic_DNA.
DR RefSeq; NP_199718.1; NM_124284.1. [Q9FH27-1]
DR AlphaFoldDB; Q9FH27; -.
DR SMR; Q9FH27; -.
DR STRING; 3702.AT5G49070.1; -.
DR iPTMnet; Q9FH27; -.
DR PaxDb; Q9FH27; -.
DR PRIDE; Q9FH27; -.
DR EnsemblPlants; AT5G49070.1; AT5G49070.1; AT5G49070. [Q9FH27-1]
DR GeneID; 834966; -.
DR Gramene; AT5G49070.1; AT5G49070.1; AT5G49070. [Q9FH27-1]
DR KEGG; ath:AT5G49070; -.
DR Araport; AT5G49070; -.
DR TAIR; locus:2155194; AT5G49070.
DR eggNOG; ENOG502RGTN; Eukaryota.
DR HOGENOM; CLU_013238_2_1_1; -.
DR InParanoid; Q9FH27; -.
DR OMA; CIRPANN; -.
DR PhylomeDB; Q9FH27; -.
DR BioCyc; ARA:AT5G49070-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9FH27; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FH27; baseline and differential.
DR Genevisible; Q9FH27; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR012392; 3-ktacl-CoA_syn.
DR InterPro; IPR013747; ACP_syn_III_C.
DR InterPro; IPR013601; FAE1_typ3_polyketide_synth.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR31561; PTHR31561; 1.
DR Pfam; PF08541; ACP_syn_III_C; 1.
DR Pfam; PF08392; FAE1_CUT1_RppA; 1.
DR PIRSF; PIRSF036417; 3-ktacl-CoA_syn; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
PE 2: Evidence at transcript level;
KW Acyltransferase; Alternative splicing; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..464
FT /note="Probable 3-ketoacyl-CoA synthase 21"
FT /id="PRO_0000249112"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 42..333
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 187
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 352
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 356
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 385
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 389
FT /evidence="ECO:0000250|UniProtKB:Q38860"
SQ SEQUENCE 464 AA; 52558 MW; A0BFDBC7605EA421 CRC64;
MNQTIHRVSP ISMSISELTT LLSSGVSVFE IFAGLLVVHL IYQRIRTRVK VYLLDFTCYR
APDSNRVPMS TLIETIYLDD KLDQESIDFQ ARILERSWLS NQTSIPRSLM EIPLKKSLSS
VKIETMTTIF TSVEDLLRKN KLSPRSIDIL ITNCSLHSPS PSLSAMVINK FHMRSNIKSF
NLSGMGCAAG ILSVNLANDL LQAHRGSLAL IVSTEALNTH WYIGKDRSML LTNCLFRMGA
AAVLMSSNDH DRDNAKYELL HVVRKNKAKD DRAYRCIYQD IDSDEKQGVS ITKDVISVAG
DMLKMNLTSL GPLVLPYLEQ FQYVIQHILC KKLKIYESNS SYTPNFKTAF EHFCIHTGGR
AVIQAMEMNL KLTKVDIEPS KMTLHRFGNT SSSSIWYALS YLEAKRRMKK GDRVLQIAFG
SGFKCNSAVW RCIRKVEPNT ENKWLDFIDS YPVDVPDSTN IRPG
