ID L8LJB0_9CHRO Unreviewed; 1451 AA.
AC L8LJB0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Polyketide synthase family protein {ECO:0000313|EMBL:ELR97623.1};
GN ORFNames=GLO73106DRAFT_00014350 {ECO:0000313|EMBL:ELR97623.1};
OS Gloeocapsa sp. PCC 73106.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Chroococcaceae; Gloeocapsa.
OX NCBI_TaxID=102232 {ECO:0000313|EMBL:ELR97623.1, ECO:0000313|Proteomes:UP000011180};
RN [1] {ECO:0000313|EMBL:ELR97623.1, ECO:0000313|Proteomes:UP000011180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 73106 {ECO:0000313|EMBL:ELR97623.1,
RC ECO:0000313|Proteomes:UP000011180};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:ELR97623.1}.
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DR EMBL; ALVY01000207; ELR97623.1; -; Genomic_DNA.
DR RefSeq; WP_006529540.1; NZ_ALVY01000207.1.
DR STRING; 102232.GLO73106DRAFT_00014350; -.
DR PATRIC; fig|102232.3.peg.2558; -.
DR eggNOG; COG3321; Bacteria.
DR OrthoDB; 499075at2; -.
DR Proteomes; UP000011180; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR049490; C883_1060-like_KR_N.
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; 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; 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; 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; SM00827; PKS_AT; 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; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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; PS00606; KS3_1; 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:UP000011180};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..428
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1347..1423
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1328..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1451 AA; 160552 MW; 5FAFBD190B179795 CRC64;
MKTNGLEIAI IGMAGRFPGS RNIDEFWDNL RLGVESIQIL SDEELLQSGV DKALINHPQY
IKACGKLAGL ELFDAAFFGL VPREAEILDP QHRLFLECAW SALEQAGYDS EKTSGTVGVY
AGAGMNGYLF NVYTNNTIRN SVNPYEIFLS TDKDFLTTRV SYKLNLEGPS VDVQTACSTS
LVAVHIACQS LLSGECKMAL AGGVAISRND GYMYQEGGIY APDGHCRAFD AKAQGTVAGN
GVGIVVLKRL EDAIAENDTI HAVIKGSAIN NDGSLKVSYT APRIDSQATA IRTAQMMAEV
EPETITYIEA HGTGTPLGDP IEIAALSQVF RHSTQKTGFC AIGSVKTNIG HLDAAAGIAS
LIKTVLALKH RQIPPSLHFE EANPQIDFAN SPFYVNKALK DWDEPALRKA GVSSFGIGGT
NAHVILEEYQ NTEISAQAKS DYLLILSAKT PTAIETATTN LIEHLRKHPH LNLADVAYTL
AVGRRAFAYR RMVVGENLTE ITHALTSSQA EQSGTPSVVF MFSGQGSQYP NMGRSLWESE
PVFKEYIDCS CELLKPHLGV DLREILYSDH HQANEINATV YAQPALFVVE YALAQLWMSW
GIYPEAMIGH SIGEYVAACI AGVFSLEEAL ELVAFRGKLM QQQPSGSMLS VSLSEAEVQS
WLNEEICLAA INSPSLCVVS GTEQAIATLS DSLTTQGISC RLLHTSHGFH SSLMDSAVNP
FAEKVKQMNL AQPKIPMISN VTGTWLTASA ATNPYYWAKH LRQPVKFASG ITELTQHQER
LFLEVGPGNT LSTFTQQPHF LSLPHPKQKQ SDINCLLNTL GKLWLKGVSV NWENFYEAEK
RYRIPLPTYP FEGQRYWIEP ETVTNLSLIE RDTDWFYTPS WERDLLPESK KGQKLSQACW
LIFIDSEGIG ANLAQQLILA GQDVITVAKG ESFTELDYRA FTIHPNHKED YYNLLEDLSW
RELKPDYIVH CWGITEDSLS FHSFQQQGFY SLIFLMQALE KYKIATDLQI TLITNNLHEV
IGGETLQPVK ATLLGLCKVI PQEYPSITCR NLDIVLSDKD KLGDYLFNEL LTPTNDLVSA
YRSPYRWRQI FKPIHLNKAG ATIKPEGVYL ILGDLNEGLG RVWAQSLPKS VKLILIDSSP
FVHDLKTEHI FIQVDIKDEE QVRKGIEQGE KHFGLIQGVF YSTPFSNPQG TAPIQLLELS
QCEYNFQKKN EGLYVLAAIL KERKIDFCLL QSSLASIIGG LGLAAYGAAN AFIDAFAIEQ
GWLSTNWDAC KFAENETIDK GFGASLAQFT LTPSEVWEVT QRVLAMGSLP QVIVSKGNLQ
SRFLSTKPKE KNEVQHSRPN LANDFIPPRD ETESQIAKIW QDILGIEKVG IYDSFFDLGG
HSLLAIQVLS RLRETFQVEL SMGDLLFETP TVAGLAAAIA SKQPLTEIAE VLAEIQDLSL
EEIQQQLEDS F
//
