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Database: UniProt
Entry: A0A103XWW9_CYNCS
LinkDB: A0A103XWW9_CYNCS
Original site: A0A103XWW9_CYNCS 
ID   A0A103XWW9_CYNCS        Unreviewed;       526 AA.
AC   A0A103XWW9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=3-ketoacyl-CoA synthase {ECO:0000256|PIRNR:PIRNR036417};
DE            EC=2.3.1.- {ECO:0000256|PIRNR:PIRNR036417};
GN   ORFNames=Ccrd_023373 {ECO:0000313|EMBL:KVH98408.1};
OS   Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC   Carduinae; Cynara.
OX   NCBI_TaxID=59895 {ECO:0000313|EMBL:KVH98408.1, ECO:0000313|Proteomes:UP000243975};
RN   [1] {ECO:0000313|EMBL:KVH98408.1, ECO:0000313|Proteomes:UP000243975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2C {ECO:0000313|EMBL:KVH98408.1};
RX   PubMed=26786968; DOI=10.1038/srep19427;
RA   Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA   Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA   Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT   "The genome sequence of the outbreeding globe artichoke constructed de novo
RT   incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL   Sci. Rep. 6:19427-19427(2016).
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, ECO:0000256|PIRNR:PIRNR036417}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000256|ARBA:ARBA00005531,
CC       ECO:0000256|PIRNR:PIRNR036417}.
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:KVH98408.1}.
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DR   EMBL; LEKV01003799; KVH98408.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A103XWW9; -.
DR   STRING; 59895.A0A103XWW9; -.
DR   EnsemblPlants; KVH98408; KVH98408; Ccrd_023373.
DR   Gramene; KVH98408; KVH98408; Ccrd_023373.
DR   OMA; HHSKLCG; -.
DR   OrthoDB; 930987at2759; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000243975; 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:SF99; 3-KETOACYL-COA SYNTHASE 4; 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   Acyltransferase {ECO:0000256|PIRNR:PIRNR036417};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243975};
KW   Transferase {ECO:0000256|PIRNR:PIRNR036417};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        55..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          114..403
FT                   /note="FAE"
FT                   /evidence="ECO:0000259|Pfam:PF08392"
FT   DOMAIN          420..500
FT                   /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08541"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        258
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
FT   ACT_SITE        337
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
FT   ACT_SITE        421
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
FT   ACT_SITE        454
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
FT   ACT_SITE        458
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
SQ   SEQUENCE   526 AA;  58243 MW;  1028FE1F152CCCFC CRC64;
     MDGGANLNTN GGGGGGGGGG GGGPTVGVQI NQRHSHRRLP DFLQSVNLKY VKLGYHYLIS
     HLLTLCLVPV MIVILIEASQ MNPSDIRQLW VHLQYNLVSI IICSAVLVFG STVYIMTRPK
     PVYLVDYACY RPPDHLKAPY ERFMKHSRLT GDFDESSLEF QRKILERSGL GEETYVPEAM
     HFVPPRPSMA AAREEAEQVM YGALDNLFAA TGIKPKDIGI LVVNCSLFNP TPSLSSMIVN
     KYKLRGNIRS FNLGGMGCSA GVIAVDLAKD MLQVHRNTYA VVVSTENITQ NWYFGNKKSM
     LIPNCLFRVG GSAVLLSNKS VDRSRAKYKL VHVVRTHRGA DDKAFRCVYQ EQDPAGKTGV
     SLSKDLMAIA GGALKTNITT LGPLVLPISE QLLFFCTLIA KKLFNDDVKP YIPDFKLAFD
     HFCIHAGGRA VIDELEKNLQ LLPTHVEASR MTLHRFGNTS SSSIWYELAY TESKGRMRKG
     HRVWQIAFGS GFKCNSAVWK ALRNVKPPVN GPWEDCIDKY PVELVS
//
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