KCS16_ARATH
ID KCS16_ARATH Reviewed; 493 AA.
AC Q9SYZ0;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=3-ketoacyl-CoA synthase 16 {ECO:0000303|PubMed:18465198};
DE Short=KCS-16 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000305};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 16 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 16 {ECO:0000303|PubMed:18465198};
DE Flags: Precursor;
GN Name=KCS16 {ECO:0000303|PubMed:18465198}; Synonyms=EL2;
GN OrderedLocusNames=At4g34250 {ECO:0000312|Araport:AT4G34250};
GN ORFNames=F10M10.20 {ECO:0000312|EMBL:CAB36702.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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;
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 [4]
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 [5]
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). Up-regulated by osmotic stress and down-regulated by
CC low temperature, salt and darkness (PubMed:18465198).
CC {ECO:0000269|PubMed:12916765, ECO:0000269|PubMed:18465198}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; AL035521; CAB36702.1; -; Genomic_DNA.
DR EMBL; AL161585; CAB80142.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86348.1; -; Genomic_DNA.
DR EMBL; AK229262; BAF01126.1; -; mRNA.
DR PIR; T04771; T04771.
DR RefSeq; NP_195151.1; NM_119589.6.
DR AlphaFoldDB; Q9SYZ0; -.
DR SMR; Q9SYZ0; -.
DR BioGRID; 14856; 1.
DR STRING; 3702.AT4G34250.1; -.
DR PaxDb; Q9SYZ0; -.
DR PRIDE; Q9SYZ0; -.
DR ProteomicsDB; 247268; -.
DR EnsemblPlants; AT4G34250.1; AT4G34250.1; AT4G34250.
DR GeneID; 829574; -.
DR Gramene; AT4G34250.1; AT4G34250.1; AT4G34250.
DR KEGG; ath:AT4G34250; -.
DR Araport; AT4G34250; -.
DR TAIR; locus:2116144; AT4G34250.
DR eggNOG; ENOG502QPKZ; Eukaryota.
DR HOGENOM; CLU_013238_2_1_1; -.
DR InParanoid; Q9SYZ0; -.
DR OMA; YLMAHRF; -.
DR OrthoDB; 801187at2759; -.
DR PhylomeDB; Q9SYZ0; -.
DR BioCyc; ARA:AT4G34250-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9SYZ0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SYZ0; baseline and differential.
DR Genevisible; Q9SYZ0; 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: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; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..493
FT /note="3-ketoacyl-CoA synthase 16"
FT /id="PRO_0000249108"
FT TRANSMEM 52..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 71..366
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 221
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 300
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 384
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 388
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 417
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 421
FT /evidence="ECO:0000250|UniProtKB:Q38860"
SQ SEQUENCE 493 AA; 55778 MW; 3A281B4A8437E709 CRC64;
MDYPMKKVKI FFNYLMAHRF KLCFLPLMVA IAVEASRLST QDLQNFYLYL QNNHTSLTMF
FLYLALGSTL YLMTRPKPVY LVDFSCYLPP SHLKASTQRI MQHVRLVREA GAWKQESDYL
MDFCEKILER SGLGQETYVP EGLQTLPLQQ NLAVSRIETE EVIIGAVDNL FRNTGISPSD
IGILVVNSST FNPTPSLSSI LVNKFKLRDN IKSLNLGGMG CSAGVIAIDA AKSLLQVHRN
TYALVVSTEN ITQNLYMGNN KSMLVTNCLF RIGGAAILLS NRSIDRKRAK YELVHTVRVH
TGADDRSYEC ATQEEDEDGI VGVSLSKNLP MVAARTLKIN IATLGPLVLP ISEKFHFFVR
FVKKKFLNPK LKHYIPDFKL AFEHFCIHAG GRALIDEMEK NLHLTPLDVE ASRMTLHRFG
NTSSSSIWYE LAYTEAKGRM TKGDRIWQIA LGSGFKCNSS VWVALRNVKP STNNPWEQCL
HKYPVEIDID LKE
