ID E3FQI4_STIAD Unreviewed; 2191 AA.
AC E3FQI4;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Tylactone synthase modules 4 & 5 {ECO:0000313|EMBL:ADO69489.1};
GN OrderedLocusNames=STAUR_1685 {ECO:0000313|EMBL:ADO69489.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:ADO69489.1, ECO:0000313|Proteomes:UP000001351};
RN [1] {ECO:0000313|EMBL:ADO69489.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO69489.1,
RC ECO:0000313|Proteomes:UP000001351};
RX PubMed=21037205; DOI=10.1093/molbev/msq292;
RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA Sogaard-Andersen L.;
RT "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL Mol. Biol. Evol. 28:1083-1097(2011).
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DR EMBL; CP002271; ADO69489.1; -; Genomic_DNA.
DR RefSeq; WP_013374824.1; NC_014623.1.
DR STRING; 378806.STAUR_1685; -.
DR KEGG; sur:STAUR_1685; -.
DR eggNOG; COG0604; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_31_0_7; -.
DR OrthoDB; 5349841at2; -.
DR Proteomes; UP000001351; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase 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; cd05195; enoyl_red; 1.
DR CDD; cd08955; KR_2_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
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; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
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.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 38..465
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2100..2175
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2191 AA; 236302 MW; DE877C383CA72E8D CRC64;
MSPSSPPNYP KLLNEALQAL KAMRHKLETA EATSAANQEP IAVVGMACRL PGGVRSPEDF
WALLESGRDA IGPIPAERWD SEKYYDPDPD APGKICTREG GFLNAHKAFD AQFFRISPRE
AMYMDPQQRM VLEVAWEALE RACIPPDSLY GSDTGVYVGL TCTDYAALMA QYVPEEEADP
TASTGSAHSP AAGRLSYVLG LHGPSMALDT ACSSALVAVH LACESLRRRE SHAALAGGVN
LMFAPLGHVL LSRAHMLSPE GRCKTFDEAA NGYVRSEGVG MAVLKRLSDA RRDKDPILAL
IRGSAVNQDG PSGGLTAPSG PAQRQVIRKA LENAGLEPSA VDYIEAHGTG TALGDPIEMN
ALGEVFASNH DAARPLWVGS AKTSIGHMES AAGIGGLIKV ILQLSHGAIP PHLHLKQPSS
RIPWSKLPFQ VPTALTPWPA GARKRVAGVS SFGFSGTNAH LVVEEPPRPE PAPQAVDRTR
HLLALSAKTE DALEALVAKY VSLLEKQPAW ALADVCHSAN AGRSHFPHRL ALQADSSLEL
LARLKASQQG KTPPGTSRGM VRNRPPSVGF LFTGQGSQFL GMGRELYETQ PTFRKVLEQC
DAVLATEAGW SLREVLYAPE AEAARVHQTA YAQPLLFALE YALAMLWQSW GVQPSAVMGH
SLGEYVAACV AGVFSLEDGL KLVVARGRLM GALPEGGAMM AFASDEETVR QLIAPFPDEV
SLAAINGPKQ LVVSGSRQRL QALAEAFRQQ GPAPKALEVS HAFHSPLMRP MREAFAQVAE
QVRYSPPKVE FVSNLTGTSL SNEVAQASYW VRHVSEPVRF HEGIETLHRL GCRLFLEIGP
RPTLSPLGRH CLPDPELKWL PSLTAEKRDW EQVLASLGEL YTLGVPVDWA GVDRAYARRK
LDGLPTYPFQ QEEHWFPTYA LPEGGAQRQP APVHPLLGRR VAARSSRDEA YVFEAELKEG
HPAYLTDHRV FGRALVPAAG FLEVALAAGR VALPDTRPTV KNVAIRAALA LSPDTSTRLR
TTLKPHPSGG FAFQITSQVD AGGGESAPWK LHVQGLLCAE SPDAPEPLRA DAVLRSLPES
TAPQAFYEGM RQRGLAYGPA FQALKHLRAH DGQVLGHVEL PAGLREESAL YGLHPALLDS
AFQAMALAVQ RADTTSTYLP TGIEALHWWK KPEGQCEAYV VQRPSEGEDA RIARVDVHLT
DEAGHRVALV LGLQVLQTQE AALRRILEGD PAEFLYSFLW SQKALGAGGQ AAPGAGSSPG
RWLVFADHGG VGLAVARALK EAQAVCTLVH PSPGIATLRH EDGQYHLDPS RPEHFTALME
AVCPQVPGGD KHLPPGILYF WGLDLLGTAA EPSQAWEQTQ ALGCGPLLRL LQALGPFREM
AVQLVTRGVF VPGERPAPVH IEQSALLGLF NTFRIERPAF RCLHMDLEPG PRRGPPELEV
RQLLQEVLAH EGEEQVAFRK GLRFVSRWER MKDLPASSDP AQARPFQLTF DASGALERLS
QTPVERRPPG PGEAEVEIRA SALNFKDVLH ALAMLKKPDA TKTLGLECAG TITRVGPGVP
ESRIGERVVA IGNECLASHI TLPIQDVIPL PRGLSFLDAA AAPSVFMTTW HSLLSLARIR
PGERVLIHAA AGGVGQAAIR LCQRLGAEVL ATASPPKWPF LQAQGVRHIM NSRTLHFQEQ
VLEATGGRGV DVVLNSLNGD FIPTNLKVLA PGGRFIEIGK LGIWTPEQVA AVRPDITYHA
FDLSEASAEV RDGLRQSLAE VLGWMASGSV EPLPIERYPL SSVETAFRHL SQAKNIGKVV
IEMPRREAVD EPPIIRAQGT YLLTGGLGAL GLEVAQWLVN QGARSLVLLG RRGPSAEALP
LLERLRAAGA SVEVLQADVT ELGSLTQVMA HLRTPGRPPL VGVLHAAGLL DDGTLQELTE
ERFLKVMEPK VKGTWNLHLL TKDLPLDFFV CFSSMASALG SLGQGNYAAA NAFMDALMHQ
RRALGQPGLS INWGSWASVG MAATLDPQHR KQAAARGIHT LPTPLALAAL GVLLRGGPPQ
AGVAAIDWER FIRQVRLGIP LKLIEVLVAS ASRGKSSAPA ESPELFRARL REAPPLQRRE
LLLSFMRSLL ARMLGFASPE KIDPHHRLVE LGLDSLSSVE LKNHLEITLG CSLPAALLFD
FPTLDALAVH LHDEVLGYGQ AADEGPTKAT G
//
