ID   E0I7G9_9BACL            Unreviewed;      1225 AA.
AC   E0I7G9;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:EFM11985.1};
GN   ORFNames=PaecuDRAFT_1593 {ECO:0000313|EMBL:EFM11985.1};
OS   Paenibacillus curdlanolyticus YK9.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM11985.1, ECO:0000313|Proteomes:UP000005387};
RN   [1] {ECO:0000313|EMBL:EFM11985.1, ECO:0000313|Proteomes:UP000005387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YK9 {ECO:0000313|EMBL:EFM11985.1,
RC   ECO:0000313|Proteomes:UP000005387};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA   Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT   "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004789}.
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DR   EMBL; AEDD01000003; EFM11985.1; -; Genomic_DNA.
DR   RefSeq; WP_006037604.1; NZ_AEDD01000003.1.
DR   AlphaFoldDB; E0I7G9; -.
DR   STRING; 717606.PaecuDRAFT_1593; -.
DR   eggNOG; COG3321; Bacteria.
DR   OrthoDB; 9765680at2; -.
DR   Proteomes; UP000005387; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   CDD; cd08953; KR_2_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 1.10.1240.100; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR049490; C883_1060-like_KR_N.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF21394; Beta-ketacyl_N; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005387};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..433
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1143..1217
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1118..1141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1225 AA;  133635 MW;  67B340BCC2C780D9 CRC64;
     MKETNQGDIA IIGMASRFPN ASGNRQFWDI IRDGLDCVGD CPEMRKQDIE QYLNAIGYDA
     DGRLYRQAAY LEEIDKFDYE FFKIPPREAA LMDPHQRIFL ETAYQAIEDA GYCGRMGGTK
     TGIYVGFPTE FSAKVYQNII FETTPHLAGD SFTGNLPAVL PARLAYLLNL RGPSMLIDTS
     CSSSLVAIHL ACQSLRQGEC EYALAGGINI FVVPVINPAV EGIGIVASDG KTKSFDDQCD
     GVGQGEGVGV LLLKPLEKAL NDRDLIYAVI KGSAVNQDGK SIGITAPNAA AQEDAIVEAW
     HNAAVPPETI TYVEAHGTAT KLGDPTELKG IRKAFQRYTG KRQFCAIGSV KSNIGHTIGA
     AGVAGVIKSA LAMQARKLPP NVHFQMPNRK ISFEDSPVYV SNQLKDWKQE GPLRSGVSSF
     GISGTNCHVV MEEAPCYSER QPSNYASHLF TLSAPTKERL GIMISSYADF LKEYPELELR
     DICFTANTGR TRYRHRLAIV ASSVLDLAAK LARIARSWDE CEGRGAEWRL GEAIEKLEAT
     AVMASLSEPA CIEAACSAFM AGEPLDWTEA YPDARKISLP GYPFKRSRCW IEVPLRASAI
     CMPASRTPVS ATGESFYAAE WEERPLAFRA AAGAALSLAI FTDGAMTGSS IVEALRSEGQ
     TVYEIMPGQA YERNGEYEYT VGSDAASMLE LMKELQHKEI TDVVVLSTLP GMKRPGTLHE
     VRGELQEGVY GLFHIVQALD HYFANRRVRL LIAVSGASEV VAGDEVRPTS NATIGFAKAV
     HWEYPNIRCR TVDIGRRTSL NALLEEIRGG HGADFGCAYR DGKRYVELIR PLRVQPRSDR
     TAGIKEGGTY IITGGTGRLG LRLAAHIAKD FPVRAVLLSR SGLPDRAEWG RLLQESADES
     LKNKIRAVVQ IEENGSTVRV IPCDVSDETI ARAMLDSLYA EYGRVDGIVH CAVSDENIRI
     AEMTDEHLSA SFASKIEAAW IVADSSRQWE MDFFVLFSSV MTLVSGQANA IYTAGNSYLD
     ALPYAVRRAG MVTINWPEWK NIGLDESKTV EEERSIFLKL DASEGLRLFD AAIASGQPRL
     IAGSMNYASE AFELIDYLPF QVSEDILAQL PKRAVRSKSA PDTADAPAHS APPKVRLTGR
     SSGQYSVTEQ LLAEAWSTVL GYEEVNIGDN FFEIGGSSIS AVRIAIELMA HDIVLEAPEI
     LRYQTVEKIA GFIGGAVHAA VAGRA
//