ID C2NS69_BACCE Unreviewed; 2114 AA.
AC C2NS69;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:EEK53066.1};
GN ORFNames=bcere0004_55960 {ECO:0000313|EMBL:EEK53066.1};
OS Bacillus cereus BGSC 6E1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=526970 {ECO:0000313|EMBL:EEK53066.1};
RN [1] {ECO:0000313|EMBL:EEK53066.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 6E1 {ECO:0000313|EMBL:EEK53066.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004789}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEK53066.1}.
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DR EMBL; ACLU01000171; EEK53066.1; -; Genomic_DNA.
DR RefSeq; WP_002004136.1; NZ_CM000716.1.
DR HOGENOM; CLU_001495_0_0_9; -.
DR Proteomes; UP000000284; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 1.10.1240.100; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 3.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 3.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 3.
DR SMART; SM01294; PKS_PP_betabranch; 3.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 3.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 970..1044
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1102..1176
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1218..1643
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 2114 AA; 241009 MW; 51D85C365BD786D0 CRC64;
MNKFESFDSL KIHFCKVNNF FESVVSSNKG YQDKNEFDLY LHENYDFLND IINQSSFCNK
QIYHTSVIQQ DSKNKEFDII EYKNLIAENI PLILSNSNCS NDDFLHFQKE LYYLSVISEK
QYSMLKEHCN KYMYKIKSTL ITSLISVFSH YTDKVKVGIC ISSEEKGNVT WFNNFSSNNE
SFEQQVRKID KHIENEYGEH LGQSLSYQIL IKFDSFNYEK MGNEIVPHLS IDIKEEENLI
GIMRYFPLVC SSLGVETVWG HFETFLYNAI HSPDKNIMTI SILDEKEETF IQNCIGYREK
FVLNESLYKL FEKQVKEKPS VLAVVHERGE DNDNYLTYKQ LYMAIDILAD KINEIVGDTG
NPPISIGVYG ERSVHTLISI LAILKSGNTY VPLDTTYPKS HLEYIVEDAS LAVILTTNKY
VNSLPKNKVK IQTLDFINFE VNNNEEYKEK ASDKSDINNT SLIMYTSGST GKPKGVKHKQ
HQLINYFNYM WGKYPFNADD RMCQRTSMNF MPSMWEFMGG LLGGIPTVII SDSIVKDPAR
FAAALKKNKI SYLVIIPSML QRMFEASFDM SELVNIRLCL TVGEPITLEL VQLFYKLLPN
AKLIADYGST EVNGVLQINT GMYREDIECL PGLKPIANVK AYILDENMNL SPVGVTGELY
ISGACLAEEY VNLDMLTKEK FIDNPFELEG KLYNMGDLAS YLPDGTIKVL GRKDSQVKIR
GIRIELPSIE KVLLENESIK ESVVIVKEIR TGTKRLIAFI IPHDNHVVNS QEIRDFLMEK
LPEYMVPSTF IQLNEFPRIP NGKIDHKKLA NLEKSYDLEG EKAAINTIKE KSFNVNEEFV
KNQLRDTAAA VLKTHKNNVL TSKKYYEIGF DSVTIVDFVN KLNTLCNTKL EVVDLYDYSC
IDDLTNYLMD KETFRNYINS NWDGVSSIQN NPIQDNNSVS KKQSLEKEPL KELKGNLIKD
SSLNVKEMKP YLKEYLKENA AHVLGTDKNN ILTDKKYYEI GFDSVTIVDF VNKLNALYST
GLEVADLYDY SCIDDLTNYL MDKETFRNYI NSNWDEVSLI QNNLIQDNNS ISKKQSLEKE
PLKELKGNLI KDSSLNVKEM KPYLKEYLKE NAAHVLGTDK NNILTDKKYY EIGFDSVTIV
DFVNKLNALY STKLEVADLY DYSCIDDLAD FLITKDVFKQ YFKKNNHIDE KEKEEKNISN
AYGTTNAEEH IENEDSAEMK IAIIGISGRF PGADNVEVFW RNLSCGIDSI VQIPKHRWDK
DEIYDSDAKK PFKSVSKWGG FVEGVDLFDS DFFNISPRES EAMDPQQRLC LEESWKALED
AGYSEKELNG NSVGVFIGAK PGDYINLIKE RNIAPNPYTT MGCNQAILAA RISYHLNLKG
PSMTVDTACS SSLVAVHLAY NSILQGECDM AIAGGVSVMS SPELYLESSK MGMFSVDGRC
KAFDNAANGI VPGEAVGVVI LKRLDKALKD RNQIYGVIAG SGINQDGKTN GITAPSSSSQ
YELIKSVYEK HKINSEDITY VETHGTGTKL GDPIEIKALS RAFADFTQKK NFCAVGSVKT
NIGHTIASSG IVGLIKVLLS MKYKKIPASL HFKKKNEHIN FSDSPFFVNT TLKNWEVAPN
SPRMAAVSSF GISGTNSHMV IEELLHPLKE SSGPKSYYLI PISAKNKNSL RQRAKDLLNW
LQHEGSNQSL DDISYTLQQG RSHFKYKLAF VVESQKDLIR KLESILSKKS HFNIVSNENK
AVYESPSSIS AKDINKTQEK SLDYLIQLAE LYINNYEIDW NLFNEEGKSY LISMPTYPFN
RERYWITNEN ERNEYISPTD FDISSEEKSP TIEEEEFSIL FSKDDISIED HIINNKVILP
GAALLEKVLT SVENVYKQTV SSIQSVVWKN TVVFDVERKK INTKLTLGTE QVKFVCELEE
GIPVCEGILV FQNSRKTDRY HIIDQIKTRC NQYKDGRRFY SSCFNNGLHY GENYQVVKEL
FYNETELISH MEIPKDIGKN IDNLRMLPQM LDGALHSIAG FDIICDSGDT YLPFSVESIE
IVKPLESCCW AYIKLKDKNY TGIVIAEINI FNEKNELLIS IKDFAIKPLN KIQSSELKEE
RVEPKFFINK WIRG
//
