KCS7_ARATH
ID KCS7_ARATH Reviewed; 460 AA.
AC Q9C992;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=3-ketoacyl-CoA synthase 7 {ECO:0000303|PubMed:18465198};
DE Short=KCS-7 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000305};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 7 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 7 {ECO:0000303|PubMed:18465198};
GN Name=KCS7 {ECO:0000303|PubMed:18465198};
GN OrderedLocusNames=At1g71160 {ECO:0000312|Araport:AT1G71160};
GN ORFNames=F23N20.15 {ECO:0000312|EMBL:AAG51695.1};
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=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 [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 Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2004) 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, 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 -!- 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; AC016972; AAG51695.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35167.1; -; Genomic_DNA.
DR EMBL; BT015084; AAT71956.1; -; mRNA.
DR PIR; C96736; C96736.
DR RefSeq; NP_177272.1; NM_105785.2.
DR AlphaFoldDB; Q9C992; -.
DR SMR; Q9C992; -.
DR STRING; 3702.AT1G71160.1; -.
DR iPTMnet; Q9C992; -.
DR PaxDb; Q9C992; -.
DR PRIDE; Q9C992; -.
DR ProteomicsDB; 247319; -.
DR EnsemblPlants; AT1G71160.1; AT1G71160.1; AT1G71160.
DR GeneID; 843456; -.
DR Gramene; AT1G71160.1; AT1G71160.1; AT1G71160.
DR KEGG; ath:AT1G71160; -.
DR Araport; AT1G71160; -.
DR TAIR; locus:2026331; AT1G71160.
DR eggNOG; ENOG502QQXN; Eukaryota.
DR HOGENOM; CLU_013238_2_1_1; -.
DR InParanoid; Q9C992; -.
DR OMA; FFKPRCI; -.
DR OrthoDB; 801187at2759; -.
DR PhylomeDB; Q9C992; -.
DR BioCyc; ARA:AT1G71160-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9C992; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C992; baseline and differential.
DR Genevisible; Q9C992; 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; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..460
FT /note="3-ketoacyl-CoA synthase 7"
FT /id="PRO_0000249099"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 38..328
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 183
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 262
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 345
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 349
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 382
FT /evidence="ECO:0000250|UniProtKB:Q38860"
SQ SEQUENCE 460 AA; 51496 MW; C2020FB71C02F2F6 CRC64;
MESSFHFINE ALLITQTFIT FHQFLVASAC VLIAVFGYYF FKPRCIIYLI DFSCYQPPDF
LRAPVSNFIE HLTISGVFDQ ESLDLQQKIL ERSGISDDAS VPATVHEIPP NASISAAREE
THEILFAIVQ DLFSKHEIDP KSIDILVSNC SLFCPSPSIT SMIINKFGMR SDIKSFSLSG
MGCSAGILSV NLVKDLMKIH GDSLALVLSM EAVSPNGYRG KCKSMLIANT IFRMGGAAIL
LSNRKQDSHK AKYKLQHIIR THVGSDTESY ESVMQQVDEE GKVGVALSKQ LVRVASKALK
INVVQLGPRV LPYSEQLKYI ISFIQRKWGM HKEIYTPNFK KAFEHFCIHA GGRAIIEGVE
KHLKLDKEDV EASRSTLYRY GNTSSSSLWY ELQYLEAKGR MKMGDKVWQI GFGSGFKANS
AVWKCISEID SRGRNAWSDR IHLYPVCGDT SSALKTELLS
