ID D8G9C1_9CYAN Unreviewed; 1093 AA.
AC D8G9C1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:CBN59211.1};
GN ORFNames=OSCI_4080007 {ECO:0000313|EMBL:CBN59211.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN59211.1, 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).
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DR EMBL; CACA01000370; CBN59211.1; -; Genomic_DNA.
DR AlphaFoldDB; D8G9C1; -.
DR Proteomes; UP000004532; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
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; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR 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; 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; 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; 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; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000004532};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 15..442
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 998..1074
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1093 AA; 120472 MW; C1A85A80F5CD756F CRC64;
MPMNSSNQFN RFDGKDEIAI VGMAGRFPGA KNVDDFWQNL RDGVESISFF TDEELISTGT
DSALLNDSKY VKAGTILEDI ELFDAAFFGF TPREAEIADP QQRLFLECAW EALENAGYDS
ESYPGQIGLF AGVTLSSYLF YNLYSNRNLI ESLDPFQVLI GNDKDHLCTQ TSYKLNLKGP
SINVQTTCST SLVAVHLACQ SLLNGESDIV LAGGVSIQVP QKTGYRYQEG GINSPDGHCR
AFDANAQGTI FGSGLGIVVL KRLEDAVADG DCIHAVIKGS AINNDGSLKV GYTAPSVEGQ
REVILEALAL AGVEAETISY IEAHGTGTSL GDPIEIEALN QAFRTNTDRN NFCAIGSVKT
NVGHLNTAAG ITGLIKTIQA LKHKQIPPSL HFQQPNPQID FANSPFYVNT KLSAWKTNGN
PRRAGVSSFG IGGTNAHVIL EETPAVEASS SSRPWQLLLL SAKTNTALET ATANLATYLQ
LHPHSNIADV AYTLQVGRRA FEHRRMVVFQ DIEDAINTLT NLDPQRVFTH YQKPSHRPIV
FMFSGQGAQY VNMGRELYEV EPTFREQIDI CSDILKPHLG IDLRSILYPS EAQTAAASQQ
LEQTAITQPA IFVVEYAIAK LWIEWGVNPV ALIGHSIGEY VAATLAGVFS LEYALFLVAI
RGQLMQELPS GSMLAVPLPE QEVQPFLGKE LSLAAVNAPS SCVVSGSTEA IETLQNKLNS
QAIDCRRLHT SHAFHSEMMQ PILEQFTLAI KKVKLNPHQI PFISNVTGTW ITENEATNPS
YWSKHLRQTV RFSAGISELL KQPEAIFLEV GPGRTLSSLT KRHLEPDTKH LVLNSLHHPQ
EKQSDVALLL NALGRLWMAG IKIDWSGFYT HESRHRLPLP TYPFERQRYW IDAKSPSLSA
SNNSITSDKK DRWLVFVDES GAGSQLLNKL EEKCQNVITL KLGEQFAKVS EGIYTLNPQN
QDDIDALLAE LIPETKSSQQ TDSSPRYLRP ILSNSYIPPT NELEQQIAEM WQEVIGIKQV
GIHDNFFELG GDSLIATQLV SRLRSHFPVE LPLRDLLLQA STVAKQAEML DQLLLEKISD
LSDEEVEAFL ANP
//
