ID   A0A091SZE1_NESNO        Unreviewed;      1337 AA.
AC   A0A091SZE1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Phthioceranic/hydroxyphthioceranic acid synthase {ECO:0000313|EMBL:KFQ48881.1};
DE   Flags: Fragment;
GN   ORFNames=N333_01714 {ECO:0000313|EMBL:KFQ48881.1};
OS   Nestor notabilis (Kea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Nestor.
OX   NCBI_TaxID=176057 {ECO:0000313|EMBL:KFQ48881.1, ECO:0000313|Proteomes:UP000053840};
RN   [1] {ECO:0000313|EMBL:KFQ48881.1, ECO:0000313|Proteomes:UP000053840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N333 {ECO:0000313|EMBL:KFQ48881.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC         Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449; EC=2.3.1.39;
CC         Evidence={ECO:0000256|ARBA:ARBA00023404};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41793;
CC         Evidence={ECO:0000256|ARBA:ARBA00023404};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194}.
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DR   EMBL; KK938507; KFQ48881.1; -; Genomic_DNA.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000053840; Unassembled WGS sequence.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05274; KR_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR45681:SF6; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053840};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..193
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ48881.1"
FT   NON_TER         1337
FT                   /evidence="ECO:0000313|EMBL:KFQ48881.1"
SQ   SEQUENCE   1337 AA;  149334 MW;  C9474AD69DE19ED6 CRC64;
     RGEGCGVLFL KPLKKAKEDY SKIWGVINIS AINQNGRFMT PITRPSQIQQ ENLLRSIYET
     HVDPSVVQYV EAHGTGTAAG DPTEAESLGN VIAKKRSSQV SILKIGSVKG NIGHTESAAG
     AAALIKVLLM MHHGKIVPSL HYSKDMSSID TEKLNIAIPT AVEPWEESSE YGRVAAINCF
     GFGGTNAHVV VRQAKQLEPL PAFKRPLELV LLSAASSKSL QMTMADTADQ LSTRNSITLP
     GLAYTSACRR SHANYRYRKA FVTNSLQHLQ QEVMLAASTE VATPKVEPQL IFVFCGNGVT
     LKEFSEVLLS SEPVFRDKCK ETEALFQKYA PFSFLPAKSD SPKDLLNPEL SQVMLFTLQV
     ALGALLKYWG IKPVAVVGHS VGEVAAVHFA GYLSLADAVK VIYHRSRLQA KTDSGRMLVV
     GNIPVEEIAE YLHRYSGKVC IAAFNSPISC TLSGSSDFIG TVQRDLAQAF SQRNIFLHVL
     SVSAAYHSPS MDMILGELEE NIQPLEKQKG ETEVISTLTG VAASENDFAQ GKFWARHIRE
     PVAFAQAIKT AARDRENVVF VEISPHRALQ RNIKEVLGKS TKVFSSLQTD VEYQTLFTLV
     GNLFELGYNP NWQHFYNGYQ SAPVDIPRYQ FDRKKLIRYL KLHQEAGRDI SVGHPLIHGI
     NSDKMEFSCL LSQDTTSYIY EHKNNGVALV PGAFYVELGL ASVMSSSRPK VPLSSCQMSI
     NFSTPCVLTQ SSQVLSIKLS PQKAVTAFEI LSSSNVIYAA GQVTKEPEAV VEESTISFRD
     IYQRCRSVIS REEIYETLSQ TGFQYGSIFK QLSDVHYCQE LKEAITSIKV DKETAIEMYS
     YCIHPVLLDC FLQMTTVMTS RTFSSRPGFP SEIGSLVVLR PLEEEMMIYM RTSKSTENCL
     EVCGCFMDKH GSILSELKRV TITFMKQTSS RENEFMFENK WKETSLSQMV GNLGAMPRVL
     VFADRFGIAE KLKKYLHPDS RYIMYEDWEA LLEGHMQNKM RAEVENYDEI LFLWGIQKLN
     EGFPSKVVDQ LAKCCEAYRQ VIVALREKMS RCLIRVITYR TTERYVDHVN CGFALYGMTR
     TCIVEVPEII FQMIDLSSAS SLDISVLADV LVKHKTTEYP ELCISQGRTY VSEIRRTPFV
     DAYYYIPLYE SQKLFKQNAV YVVVGGLTGL GFETVKFIAE NGGGNIAIFS RKMPSNEKQE
     EMKALQEQYK RSKVLFVQCD VTSTNDVEKA FQSIANIFAG SPVKGVFQSA VVLHDGRLEV
     LKLADFQKVL SPKVAGTLNL HWATRGHELD YFVCYSSVTS FLGNSTQANY AAANSFLDIF
     CLYRRNCGLS GQSINWG
//