KCS19_ARATH
ID KCS19_ARATH Reviewed; 464 AA.
AC Q9LZ72;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=3-ketoacyl-CoA synthase 19 {ECO:0000303|PubMed:18465198};
DE Short=KCS-19 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000305};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 19 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 19 {ECO:0000303|PubMed:18465198};
GN Name=KCS19 {ECO:0000303|PubMed:18465198};
GN Synonyms=KCS21 {ECO:0000305|PubMed:12916765};
GN OrderedLocusNames=At5g04530 {ECO:0000312|Araport:AT5G04530};
GN ORFNames=T32M21.130 {ECO:0000312|EMBL:CAB85559.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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 [6]
RP GENE FAMILY, NOMENCLATURE, 3D-STRUCTURE MODELING, TISSUE SPECIFICITY, AND
RP INDUCTION.
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 -!- TISSUE SPECIFICITY: Expressed in siliques.
CC {ECO:0000269|PubMed:18465198}.
CC -!- INDUCTION: Repressed by herbicides such as flufenacet and benfuresate
CC (PubMed:12916765). Down-regulated by low temperature, osmotic stress,
CC salt and darkness (PubMed:18465198). {ECO:0000269|PubMed:12916765,
CC ECO:0000269|PubMed:18465198}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL162875; CAB85559.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90757.1; -; Genomic_DNA.
DR EMBL; AK117173; BAC41850.1; -; mRNA.
DR EMBL; BT005386; AAO63450.1; -; mRNA.
DR PIR; T48449; T48449.
DR RefSeq; NP_196073.1; NM_120535.3.
DR AlphaFoldDB; Q9LZ72; -.
DR SMR; Q9LZ72; -.
DR STRING; 3702.AT5G04530.1; -.
DR PaxDb; Q9LZ72; -.
DR PRIDE; Q9LZ72; -.
DR ProteomicsDB; 230173; -.
DR EnsemblPlants; AT5G04530.1; AT5G04530.1; AT5G04530.
DR GeneID; 830332; -.
DR Gramene; AT5G04530.1; AT5G04530.1; AT5G04530.
DR KEGG; ath:AT5G04530; -.
DR Araport; AT5G04530; -.
DR TAIR; locus:2184387; AT5G04530.
DR eggNOG; ENOG502QVYT; Eukaryota.
DR HOGENOM; CLU_013238_3_1_1; -.
DR InParanoid; Q9LZ72; -.
DR OMA; MFETREN; -.
DR OrthoDB; 663765at2759; -.
DR PhylomeDB; Q9LZ72; -.
DR BioCyc; ARA:AT5G04530-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9LZ72; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZ72; baseline and differential.
DR Genevisible; Q9LZ72; 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 GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
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; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..464
FT /note="3-ketoacyl-CoA synthase 19"
FT /id="PRO_0000249113"
FT TRANSMEM 3..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 24..318
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 172
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 251
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 339
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 343
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 372
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 376
FT /evidence="ECO:0000250|UniProtKB:Q38860"
SQ SEQUENCE 464 AA; 52613 MW; 55837E61DF0FC90F CRC64;
MELFSLSSLL LLSTLFVFYI FKFVFKRRNQ RNCYMLHYEC YKGMEERKLD TETCAKVVQR
NKNLGLEEYR FLLRTMASSG IGEETYGPRN VLEGREDSPT LLDAHSEMDE IMFDTLDKLF
HKTKGSISPS DIDILVVNVS LFAPSPSLTS RVINRYKMRE DIKSYNLSGL GCSASVISID
IVQRMFETRE NALALVVSTE TMGPHWYCGK DRSMMLSNCL FRAGGSSVLL TNAARFKNQA
LMKLVTVVRA HVGSDDEAYS CCIQMEDRDG HPGFLLTKYL KKAAARALTK NLQVLLPRVL
PVKELIRYAI VRALKRRTSA KREPASSGIG LNLKTGLQHF CIHPGGRAII EGVGKSLGLT
EFDIEPARMA LHRFGNTSSG GLWYVLGYME AKNRLKKGEK ILMMSMGAGF ESNNCVWEVL
KDLDDKNVWE DSVDRYPELS RIPNPFVEKY DWINDDTMSF VRVD
