ID F4XWJ8_9CYAN Unreviewed; 1754 AA.
AC F4XWJ8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Polyketide synthase module {ECO:0000313|EMBL:EGJ31034.1};
DE Flags: Fragment;
GN ORFNames=LYNGBM3L_44030 {ECO:0000313|EMBL:EGJ31034.1};
OS Moorena producens 3L.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Moorena.
OX NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ31034.1, ECO:0000313|Proteomes:UP000003959};
RN [1] {ECO:0000313|Proteomes:UP000003959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3L {ECO:0000313|Proteomes:UP000003959};
RX PubMed=21555588; DOI=10.1073/pnas.1101137108;
RA Jones A.C., Monroe E.A., Podell S., Hess W.R., Klages S., Esquenazi E.,
RA Niessen S., Hoover H., Rothmann M., Lasken R.S., Yates J.R.III.,
RA Reinhardt R., Kube M., Burkart M.D., Allen E.E., Dorrestein P.C.,
RA Gerwick W.H., Gerwick L.;
RT "Genomic insights into the physiology and ecology of the marine filamentous
RT cyanobacterium Lyngbya majuscula.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:8815-8820(2011).
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DR EMBL; GL890943; EGJ31034.1; -; Genomic_DNA.
DR eggNOG; COG2518; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_0_3; -.
DR OrthoDB; 499075at2; -.
DR Proteomes; UP000003959; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
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; IPR013217; Methyltransf_12.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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; PF18558; HTH_51; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}.
FT DOMAIN 36..462
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT COILED 6..40
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1754
FT /evidence="ECO:0000313|EMBL:EGJ31034.1"
SQ SEQUENCE 1754 AA; 193518 MW; 53F217B73B3723D1 CRC64;
MISNQEQEYA QLMQMALDKI SNLEAEVDRL KNQKQSEAIA IIGMGCRVPG GASIPEAFWD
ILQNGVDAIT EVPPDRWPIN KYYDSDPTTP GKISTRYGGF VEQLQEFDAN FFGISPKETI
HLDPQQRLLL EVSWEALERS GINPQQLTGT STGVFVGICG SDYTQKILTQ GLEQIDAYLG
TGNSHSTASG RISYLLGLKG PSLAVDTACS SSLVSIHLAT TSLRNRECDL ALAGGVNALI
SPEFSINFSK AGMLSPDGRC KTFDATADGF VRSEGCGMVV LKRLSDAVAH GDNILAVIRG
TAINQDGDTS GLTVPNGPSQ QAVIRQALEN GGVDPASISY IEAHGTGTSL GDPIEVGAIG
TVFGKTHSQE QPVIIGSAKT NIGHLEGAAG IAGLMKVVLQ LQNHKIAPSL HFNQPNPYID
WDQLPVQVAI KLTSWPTNGK SRIAGVSSFG FSGTNAHIVL EEAPSHQVKS QKFKVESQNV
VERPVHIFTM SAKTEKALAD LVNSYQSYLE AERNHKDLGD ICYTANIGRA EFNHRLALIT
SEHEQQELIE KLKQYKQGEN VPGICSGQIT SQTKTKIAFL FTGQGSQYLQ MGRQLYQTQP
TFQKIIDQCS EILGKYLEFS LLDVLYPAQV KDETSTLIDQ TAYTQPAIFS LGYALAKLWE
SWGIKANVVM GHSVGEYVAA CVAGVFSLED GLKLIAMRGQ LMQQLPSGGQ MVSVMASESQ
VIEAIEEYSS QVTIAGINGP ESIVISGNSG AITTICDILK NMGIKTKQLQ VSHAFHSPLM
EPMLTEFEAV AKQVTYNQPK IPLISNVTGE EVGAEITTAE YWVGHVRKPV RFAQSMKTLE
EQGYETFLEI GPKPILLGMG RQCVTEDVGE WLPSLRPGIE EWQQMLSSLG QLYVKGAKID
WSGFEKDYNR QKVALPTYPF QRERYWIETK NKFWSKQQLS TDQNLHPLLG QKLNCAGEQQ
IFASQIGEKS PNYLSNHRVF NQALFPTTGY LEIAIAAGNH QLKTPQIVIE DLTISRGWIL
PAGELTNAQT ILTPTDSQSY KFQIFSQLEE EEWKLHTTGK IRKESTPPPQ TKIDLEKYKS
ECNQAIEVKQ HYQKCQQVGI DYGNSFQGIQ QLWSGSNQAL AYIKLPEELI TQTRDYNFHP
ALLDAALQVI FQALPATDSD QTYLPVGIEE FKLYKNPGLS LWAYASVTSP EVKTPESLTT
LVTIVTPSGE IIANLKGLQL KLATKQTLLG TETESIENWL YEVEWRSQGI LGKLLPPDFL
RPPVEIAQKL APTLTELVTQ VDQKRTGSIE TSLEELTVDY IVQALHEMGW SYKPTESFEF
DAAVKKLGIV PSQRQLFKRL LQILTEVGIL NYNQQQWQVE QTLAQVKPTE KSQSLQNQYP
EEAATLTLLE RCASQLSGVL RGAIDPVQLV FPQGDLTTAT QLYEESTVAK VMNTIVEKSI
TKAIEKLPKS RGIRLLEIGA GTGGTTSYIL PHLNPQQTEY IFTDIGALFT AKAQDKFQDY
QFISYQTLDI EVDPKSQGFE ANQYDIIIAA NVLHATTIMK QTLSHVRELL ADGGMLVLLE
VTTAQRWLDL VFGLLEGWWK FNDYELRPDY PLLSRDQWQK VLRETDFTEV VTMPEVEGMA
ETLSGQTVIV AQSSQTKLEQ TNDGSKSWLI LADKEGIGKQ LARQLNSVGE VCTLVFAGEK
YQQIAPAEFT INPNNLEDFE EVIETVAGKS PSLYGVVQCW TTEAGVGQTV NSEELGSLSK
LGCGTTLSLV QALV
//
