ID D8FTZ4_9CYAN Unreviewed; 1680 AA.
AC D8FTZ4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:CBN53834.1};
DE EC=2.3.1.94 {ECO:0000313|EMBL:CBN53834.1};
DE EC=5.4.3.8 {ECO:0000313|EMBL:CBN53834.1};
GN ORFNames=OSCI_270025 {ECO:0000313|EMBL:CBN53834.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN53834.1, ECO:0000313|Proteomes:UP000004532};
RN [1] {ECO:0000313|Proteomes:UP000004532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6506 {ECO:0000313|Proteomes:UP000004532};
RX PubMed=20675499; DOI=10.1128/JB.00704-10;
RA Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT reveals several gene clusters responsible for the biosynthesis of toxins
RT and secondary metabolites.";
RL J. Bacteriol. 192:5264-5265(2010).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CACA01000024; CBN53834.1; -; Genomic_DNA.
DR RefSeq; WP_007353061.1; NZ_CACA01000024.1.
DR OrthoDB; 499075at2; -.
DR Proteomes; UP000004532; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0047879; F:erythronolide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 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; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:CBN53834.1};
KW Isomerase {ECO:0000313|EMBL:CBN53834.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000004532};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBN53834.1}.
FT DOMAIN 7..433
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 934..1009
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1097..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1611..1660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1680 AA; 182072 MW; 8EF5DB055EF8A14C CRC64;
MTNSQEYEGV AIVGMVGRFP GATNLDELWS NLCNGVESTT FLTDAELDPS IDSQLKSDPN
YIKAKGIIKD ADKFDADFFG INPREAEIID PQQRIFLEMA WEALEKAGCN PDTYKGLIGV
FAGTGNNTYF ANNVSKRPDL IEAIGAFQAM VANEKDFLTT RTSYKLNLKG PSLNIYTACS
TSLVTVSNAF YSLLSYQCDM AIAGGISVTV PQNSGYLYQD GGMFSNDGYT RSFEANAQGT
VFGNGAGVVV LKRLEDAIAD RNYIYAVIKG AATNNDGAGK VSFAAPSVDG QAGAIAMAQS
FAGIEPETIS YIEAHGTATP LGDPIEIEAL TQVFRAQTQK KQFCAIGTIK SNFGHIIAGA
GVAGLIKTAL SLHHKLIPPT LHFDKPNPKI DFANSPFYVN ATLSEWKAGP TPRRAGVSSF
GVGGTNAHAV LEEAPPVTPS GPSRPRQLLL LSAKTPSALD AATANLREYL QQDPALNLAD
VAYTLKVGRK PFNHRRFAVC SSREDALQVL DSLPPQQSAT RQTDGKQRPI AFMFPGQGSQ
YINMGLNLYE TEAVFRDTVD ECAELLKPHL DLDLRDILYP DGGDAEAATT QLRQTCFTQP
ALFVVEYALA QLWMSWGIQP QATIGHSIGE FVSACLAGVF SLQDALMLVA TRGRLIQSLP
TGSMLSVALP AATLEQRLSA EVAIAAINGP SLCVASGATD AIAALESQLA SEGITCKHLH
TSHAFHSPMM EPIIDTFANY VRQVELKPPQ IPFVSTVTAS WITAEQATDC LYWAKHLRQT
VRFAEGVQEL WQNDSTLILL EVGPRTTAAT LARKQAKDLK KQVVISSLSD TAVNNSEWSA
LLTAVGQLWL AGRAIDWESF YAEETRSLIP LPTYPFERKR YWVEPIASIP SAAEVAVTSA
QKAIDSQPPL PLPITHSSST MQTSLANQTK SRKERIFPLL QEVIEETSGL EIDIADAATL
FVELGIDSLA LTQVGTALQK KFNIKITFRQ LLEDFPTLDS LAEFLDGNLP PEVLPAPQET
APILSQTVSE SAPPPHQITR QENQNQLPVT NYQLPITNYQ VPIANTQPGS LESVVAQQLQ
LMSKQLDLLG NNHSSSLPSA LPVSTPQTIQ QSPPILSPAP IGNGSSNGTS SAPTSQNSPP
PTEEKKPFGA AARINTQGRE LNSQQQAKFE AFVKRYTAKT PSSKKYAQSH RHHLADPRTV
SGFNPTYKEI VYPIVVNRSL GSKLWDLDGN EYLDLTNGFG SNFFGYSAPF IVQAIEEQLK
QGYEIGPQTP LAGEVAELIC ELTKLERVAF CNTGSEAVLG AMRLARTVTG RNKIAIFSGA
YHGIFDEVIV RGTKKLRSIP ASPGIMPEAV ENVLIVDYGE PESLEILRNH ADELAAIMVE
PVQSRRPDLQ PKEFLHELRR ITEKSGSAFI MDEVITGFRI HPGGSQAYFG VEADIATYGK
VVGAGLPIGV IAGNRKFMDA LDGGFWQYGD SSFPEVGVTY FAGTFVRHPL VLAAAKAALE
YLKQCGPQLQ QSLNQKTNKL AADLNGLFEQ LQVPFQAKNF GSLFKVIYPP EFVEGELLFY
WLREKGIHIW DHRPCFLTIA HSDAELEFVV ATFKQSIVEM QAEGFLPSPG NGSKALELAG
NGQKQGSGAN GSASPQPPVP GAKLGRDPKG NPAWYIPDPE RPGKYLQVGE SLLQSKAISL
//
