ID   A7TAS5_NEMVE            Unreviewed;       338 AA.
AC   A7TAS5;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   02-SEP-2026, entry version 90.
DE   RecName: Full=Beta-ketoacyl-acyl-carrier-protein synthase I {ECO:0000256|PROSITE-ProRule:PRU10022};
DE            EC=2.3.1.41 {ECO:0000256|PROSITE-ProRule:PRU10022};
GN   ORFNames=NEMVEDRAFT_v1g224623 {ECO:0000313|EMBL:EDO26892.1};
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO26892.1, ECO:0000313|Proteomes:UP000001593};
RN   [1] {ECO:0000313|EMBL:EDO26892.1, ECO:0000313|Proteomes:UP000001593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3Z)-decenoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxo-(5Z)-
CC         dodecenoyl-[ACP] + holo-[ACP] + CO2; Xref=Rhea:RHEA:54940, Rhea:RHEA-
CC         COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9927, Rhea:RHEA-
CC         COMP:14042, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78798, ChEBI:CHEBI:138410;
CC         Evidence={ECO:0000256|ARBA:ARBA00048121};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54941;
CC         Evidence={ECO:0000256|ARBA:ARBA00048121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + malonyl-[ACP] + H(+) = a 3-oxoacyl-[ACP]
CC         + holo-[ACP] + CO2; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC         EC=2.3.1.41; Evidence={ECO:0000256|ARBA:ARBA00048506};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837;
CC         Evidence={ECO:0000256|ARBA:ARBA00048506};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000256|ARBA:ARBA00008467,
CC       ECO:0000256|RuleBase:RU003694}.
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DR   EMBL; DS474396; EDO26892.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7TAS5; -.
DR   STRING; 45351.A7TAS5; -.
DR   KEGG; nve:5497117; -.
DR   eggNOG; KOG1394; Eukaryota.
DR   HOGENOM; CLU_000022_69_2_1; -.
DR   InParanoid; A7TAS5; -.
DR   OMA; WMAGASE; -.
DR   PhylomeDB; A7TAS5; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd00834; KAS_I_II; 1.
DR   FunFam; 3.40.47.10:FF:000005; 3-oxoacyl-[acyl-carrier-protein] synthase I; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR000794; Beta-ketoacyl_synthase.
DR   InterPro; IPR014031; KAS_C.
DR   InterPro; IPR014030; KAS_N.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; NF005935; PRK07967.1; 1.
DR   PANTHER; PTHR11712:SF306; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 1; 1.
DR   PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001593};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003694}.
FT   DOMAIN          1..335
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10022"
SQ   SEQUENCE   338 AA;  35712 MW;  F793837B863C3CF9 CRC64;
     MGNAAAYSYL AMDQAIKDAG LSEDQVSNVR TGLIAGSGGA SSADIVESAD ILRDKGVRRV
     GPYRVTRTMG STVSACLATP FKIKGINYSI TSACATSAHC IGNAMEQIQM GKQDVVFAGG
     GEELHWSLTV MFDAMGALSS KYNETPEKAS RAYDANRDGF VIAGGAGMLV LEDLEHAKAR
     GAKIYAEVVG YGATSDGYDM VAPSGEGAMR CMQQAMSTVD GKIDYINSHG TSTPAGDIQE
     LKAMKQTFGT EMPPVSSTKS LTGHSLGATG VQEAIYSLLM MENDFICASA NIEELDPEAD
     GMPVVTERRD NVKLDRVMSN SFGFGGTNST LVFQRYEG
//