ID S8C1X0_9LAMI Unreviewed; 503 AA.
AC S8C1X0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=very-long-chain 3-oxoacyl-CoA synthase {ECO:0000256|ARBA:ARBA00012307};
DE EC=2.3.1.199 {ECO:0000256|ARBA:ARBA00012307};
DE Flags: Fragment;
GN ORFNames=M569_14036 {ECO:0000313|EMBL:EPS60765.1};
OS Genlisea aurea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS60765.1, ECO:0000313|Proteomes:UP000015453};
RN [1] {ECO:0000313|EMBL:EPS60765.1, ECO:0000313|Proteomes:UP000015453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23855885;
RA Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA Logacheva M.D.;
RT "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT number of genes and short non-coding sequences.";
RL BMC Genomics 14:476-476(2013).
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:0000256|ARBA:ARBA00001906};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000256|ARBA:ARBA00005531}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPS60765.1}.
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DR EMBL; AUSU01007312; EPS60765.1; -; Genomic_DNA.
DR AlphaFoldDB; S8C1X0; -.
DR OrthoDB; 930987at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000015453; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009922; F:fatty acid elongase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00831; CHS_like; 1.
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; 3-KETOACYL-COA SYNTHASE; 1.
DR PANTHER; PTHR31561:SF23; 3-KETOACYL-COA SYNTHASE; 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; Thiolase-like; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000015453};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 93..381
FT /note="FAE"
FT /evidence="ECO:0000259|Pfam:PF08392"
FT DOMAIN 398..477
FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08541"
FT ACT_SITE 236
FT /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
FT ACT_SITE 315
FT /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
FT ACT_SITE 399
FT /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
FT ACT_SITE 403
FT /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
FT ACT_SITE 432
FT /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
FT ACT_SITE 436
FT /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EPS60765.1"
FT NON_TER 503
FT /evidence="ECO:0000313|EMBL:EPS60765.1"
SQ SEQUENCE 503 AA; 56312 MW; 597F478F673C98AB CRC64;
GAGGDTVGVR IHQSRRLPDF LQSVNLKYVK LGYHYLISNL LALCLVPLIG AIFIHASEMN
PDDVLQLWLH LKYNLVSVVI CSAFLVFGST VYIMTLPRAV YLVDYSCYRA PESLKASYRQ
FMEHSRLTGD FDDSSLEFQR KILERSGLGD ETYVPEAMHF VPPRPSMQAA REEAEQVMFG
ALDNLFANTN LRPKEIGILI VNCSLFNPTP SLSAMIVNKY KLRGNIKSFN LGGMGCSAGV
IAVDLAKDLL QIHRNTYAVV VSTENITQNW YFGNKKSMLI PNCLFRVGGA ALLLSNKAAD
RRRSKYKLVH VVRTHKGADD KAFHCVYQEQ DENGKTGVSL SKDLMAIAGG ALKTNITTLG
PVVLPISEQL IFFMTLVIKK VFKYNLRPYI PDFKLAFDHF CIHAGGRAVI DEVEKNLQLL
PVHVEASRMT LHRFGNTSSS SIWYELAYIE AKGRMRRGNK VWQIAFGSGF KCNSAVWVAL
RSVAPSKNGP WDDCIDRYPV KVI
//
