ID   A0A0N9HZ68_9PSEU        Unreviewed;      1309 AA.
AC   A0A0N9HZ68;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Ketosynthase family 3 (KS3) domain-containing protein {ECO:0000259|PROSITE:PS52004};
GN   ORFNames=AOZ06_20965 {ECO:0000313|EMBL:ALG09058.1};
OS   Kibdelosporangium phytohabitans.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Kibdelosporangium.
OX   NCBI_TaxID=860235 {ECO:0000313|EMBL:ALG09058.1, ECO:0000313|Proteomes:UP000063699};
RN   [1] {ECO:0000313|EMBL:ALG09058.1, ECO:0000313|Proteomes:UP000063699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLBMP1111 {ECO:0000313|EMBL:ALG09058.1,
RC   ECO:0000313|Proteomes:UP000063699};
RA   Qin S., Xing K.;
RT   "Genome sequencing of Kibdelosporangium phytohabitans.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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DR   EMBL; CP012752; ALG09058.1; -; Genomic_DNA.
DR   RefSeq; WP_054290962.1; NZ_JADBEI010000002.1.
DR   STRING; 860235.AOZ06_20965; -.
DR   KEGG; kphy:AOZ06_20965; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000063699; Chromosome.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
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; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43074; OMEGA-3 POLYUNSATURATED FATTY ACID SYNTHASE PFAB-RELATED; 1.
DR   PANTHER; PTHR43074:SF1; PKS_AT DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063699}.
FT   DOMAIN          3..452
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   1309 AA;  139379 MW;  C5FE20070ACB3010 CRC64;
     MRPLDVAIVG MGALFPGAGD TPAFWHNIVG SVDAIGTIPA HRWDPAIHYH PAASPASDRF
     YCRRGGFLDD EATFDPTRFG IMPSTVVDAE PDQLLALAVA AEAIADAGGE QSLPDRARIG
     VVVGRGGYLT PGCARLDQRV QIGQLLSVVK DLVPGVDTAA LREAVRERLG PEQPEASIGL
     VPNLAASRIA NRFDLRGPAY TVDAACASGL VAVEHAVREL ASGRCDAMIA GAVHVSHHPT
     LWSVFTQLRA LSQKERIRPF DRAADGTLLS EGVGMVLLRR LRDAEASGDR IYAVIRGVGT
     ASDGRATSMM TPNPEGQLLA VRRAWQEAGL EPGEGLGLIE AHGTATPAGD AAELATMVTA
     FGGSGGTVGI GTVKSMIGHA MPAAGMAGLI KAALAVHHAT LPPTLHIDDP HPALHGTRFA
     PVLEPREWQG PRRAGVNAFG FGGINAHVVL DQAGDSRAAD VNPLAPVLLL SANSPAELER
     DLLADDGDLL SRAARRTRAE DLPCRLAIWQ PDARRLKIAR QVVARGKTWT GRHDIWFSPE
     PLLTRDDQIA FLFPGFEQRG TTELAGEQSV VEHALALLRA GRGQAHKLRE AGIVPTAMAG
     HSMGEWTAMI VAGIYPTIDS FVDSLRPGMV AVADVVYAAL GCSAEKAQAV LDELAVDVVI
     SHDNCPHQSV ICGPADHLAA AVRSLQDHGV MAQIMPFRTG FHTPALAPHL AAARSTVEAL
     AVNPPSIPVW SATSLAPMPG DPAGIRELVL RHLVEPVRFR PLLHRLHTSG IRAFVQVGAG
     SLPGFVEDTL SGEQILTVAG DNEHRAVAAL WAFGLKRPTA GKKLSLGLTP LRLGPITVDQ
     PVAVDVGTPV GAALNAVLAQ TTAVAREVAQ ALAEPIPAEL ERTEVFSLRT MPHLVDHSVF
     PQADGWPDPS DGFPIVPITG LVDVIKDAAR ALVPGGVVTA VESVKAMRWL EVEPAQEVRI
     TAKREGGLVR VRVGGYAEGL VRIESAYPVP DERVYPRLRA PRPAPVSAAG LYDEGWMFHG
     PRFAGVSEIT TLADNGITGA LTVLPSPGAL LDCAGQLIGH WMQVSKSVDQ TVLPTGIDRV
     RYYGPDPEPG TRIDCDARIV DVTGELMRAD ARLLTDDGRL WCRIDGWTTR RFTTDDRIWQ
     VKLRAEHNTL AEPRDGGWVL VTEKWADDSA TRELMARRYL TAAERAGYAT LDLRTRRQWL
     LRRIAAKDAV RRWLWNRGAG AIFPAELTVT DDGIEVEVRG AFATPKVSVA HCADPGKPSA
     AGCAVAIAGD DDVVIDIRPG AAATPGSAVV TDQGTSYVVA WRQTGERRA
//