ID G6FSF1_9CYAN Unreviewed; 1570 AA.
AC G6FSF1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=6-deoxyerythronolide-B synthase {ECO:0000313|EMBL:EHC14787.1};
DE EC=2.3.1.94 {ECO:0000313|EMBL:EHC14787.1};
GN ORFNames=FJSC11DRAFT_1698 {ECO:0000313|EMBL:EHC14787.1};
OS Fischerella thermalis JSC-11.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Fischerella.
OX NCBI_TaxID=741277 {ECO:0000313|EMBL:EHC14787.1, ECO:0000313|Proteomes:UP000004344};
RN [1] {ECO:0000313|EMBL:EHC14787.1, ECO:0000313|Proteomes:UP000004344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-11 {ECO:0000313|EMBL:EHC14787.1,
RC ECO:0000313|Proteomes:UP000004344};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Sarkisova S., Bryant D.A., Brown I.,
RA Woyke T.J.;
RT "The draft genome of Fischerella sp. JSC-11.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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:EHC14787.1}.
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DR EMBL; AGIZ01000005; EHC14787.1; -; Genomic_DNA.
DR RefSeq; WP_009456258.1; NZ_AGIZ01000005.1.
DR GeneID; 60765848; -.
DR PATRIC; fig|741277.3.peg.1505; -.
DR Proteomes; UP000004344; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0047879; F:erythronolide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd08953; KR_2_SDR_x; 1.
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 Acyltransferase {ECO:0000313|EMBL:EHC14787.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000004344};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EHC14787.1}.
FT DOMAIN 11..437
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1459..1535
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1570 AA; 174933 MW; 305A1A82F552C28E CRC64;
MSHTVEFSRN GLEIAIIGMA GRFPGAKNIE EFWQNLRNGV ESITTFTNEE LLAGGIDPDL
LNDPNYVKAG AVLEDIELFD AEFFGFNPRE AEIIDPQHRL FLECAWEAME NAGYNSKMYS
GLIGVYAGAG SNNYVLNIYS NQNIRSSIDR NQLFFGNDKD FLATRVSYKL DLEGPAVGIQ
TACSTSLVAV HLACRGLLSG ECDIALAGGV AIDVPQKEGY LYQEGGIVSP DGRCRAFDAK
AQGTIFSNGV GIVVLKRLED AIADGDCIHA VIKGSAINND GAFKVSYTAP RIDGQAKVIR
AAQVMAEVDP ETITYIEAHG TGTSLGDPIE ISALTQVFRA STDKKGFCAV GSVKTNIGHS
DITAGVAGLI KTVLALKHKQ IPPSLHFQQP NPEIDFDNSP FYVNTTLSEW QTNGIPRRAG
VSSFGIGGTN AHVILEEAPV VETRGGASLQ SRPWHLLLLS AKTRTALETA TVNLAAYLQQ
HRDLNLADVA YTLQVGRQAF EHRFMVVCQN LEDAVQKLEF ANQEQVSTYL KELHNRPVVF
MFPGQGAQYV NMGRELYQTE PIFREEVNRC CELLKPHLGI DLRHVLYPSE EQIEAATHQL
QQTYITQPAL FVIEYALSQL WMAWGIQPEA MIGHSIGEYV AACLAGVLSL EDALILVAVR
GRLMQELPTG AMLSVHLAED DLQPWLGKEV SLAASNAPNL CVVSGSEEAI AHLQSRLNDK
GVECRRLHTS HAFHSPMIDS ILESFTNQVE KIKLNPPQIS FISNLTGTWI TAKEATDPTY
WAKHLRQTVR FAQGMAELMT QPERILLEVG PGMTLSTFAR QSRTDEPTVL ATLRHPKYQK
SDSAFLLTTV GQLWLAGVQV DWYKFHAQQS RQRIPLPTYP FERQRYWIEA QKVDNSHPQI
KLTRKPNMAD WFYVPAWKRV MLLEPWKTEG LNPHKSCWLI FVDPCGVGSQ IAKRLEQAGQ
DVIIVTIGEE FTKLSDCIYT INPQQQDDYT TLMQTLRELG KTPQNIAHFW GVTANTTSLG
KTLHPKTQLG VEDFCKSQDL VFYSLLFLAQ QLTKHHLTTP VQIIAITNNM HEVVGQEQLQ
PEKATVLGPC KAIAQEYPHM SCRSVDIVIP ESETFLEKQL IDQLMAELTQ QPSDLVVAYR
NGHRWVQTFE PIQLNEVVPE KTRLREGGIY LIVGDPVKGL GLVFAEYLAQ TVHAKLILIE
NSELPARNEW EQWLATHDQH NNISDQIRRI QALEELSGDV LIIKADVVNE EQMQQAMTIA
YERFGQIHGV FYVPEISGNE KSTLSIHEIG KTECEQEFKS KVHGIFVLEK VLQDKKLDFY
LLQSSLSSIL GGLGLVAYSA AYLFMDAFVH QKKQQNSVPW FSVNRQAFIS DLEKEKYVSL
GSTATELFMT PKEVWEAFQR ILSMGSANQI VVSTGDLQAR INQSLKLKPL ETVSNSKNSQ
QADSFSQHSR PNLQTVYVAP RNEIEQTIAN IWQEILGVSL VGVNDDFFEL GGHSLLAVQV
TSRLRETFQV DLPLNSILFE ASTVAGLAAV IAQQQPQQEE LEEMVALLQE VKSLSAEEVQ
AEMAKDFWSS
//
