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Database: UniProt
Entry: E3FLG1_STIAD
LinkDB: E3FLG1_STIAD
Original site: E3FLG1_STIAD 
ID   E3FLG1_STIAD            Unreviewed;      2105 AA.
AC   E3FLG1;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Mycocerosic acid synthase {ECO:0000313|EMBL:ADO73053.1};
DE            EC=2.3.1.111 {ECO:0000313|EMBL:ADO73053.1};
GN   Name=mas {ECO:0000313|EMBL:ADO73053.1};
GN   OrderedLocusNames=STAUR_5282 {ECO:0000313|EMBL:ADO73053.1};
OS   Stigmatella aurantiaca (strain DW4/3-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Archangiaceae; Stigmatella.
OX   NCBI_TaxID=378806 {ECO:0000313|EMBL:ADO73053.1, ECO:0000313|Proteomes:UP000001351};
RN   [1] {ECO:0000313|EMBL:ADO73053.1, ECO:0000313|Proteomes:UP000001351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO73053.1,
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; ADO73053.1; -; Genomic_DNA.
DR   RefSeq; WP_013376713.1; NZ_AAMD01000016.1.
DR   STRING; 378806.STAUR_5282; -.
DR   KEGG; sur:STAUR_5282; -.
DR   eggNOG; COG0604; Bacteria.
DR   eggNOG; COG1028; Bacteria.
DR   eggNOG; COG3321; Bacteria.
DR   HOGENOM; CLU_000022_31_5_7; -.
DR   Proteomes; UP000001351; Chromosome.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0050111; F:mycocerosate synthase activity; IEA:UniProtKB-EC.
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; IPR013149; ADH-like_C.
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; PF00107; ADH_zinc_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; 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   Acyltransferase {ECO:0000313|EMBL:ADO73053.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADO73053.1}.
FT   DOMAIN          1..416
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2016..2094
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2105 AA;  224891 MW;  1B859144A08B1D04 CRC64;
     MVGASCRLPG GLDSSLSLWR CLLEGRDVVQ GGDPGNRWDN YFLPVPSDTE DSRLVRVGGY
     LKDIAGFDPA FFGIAPKEAA CIDPQHRLLL EVTWEALENA GIPPRRLDGS QTGVFTGLSQ
     TSYRDLIDPG ENDVYHATGI VLSGASGRIS YVLGTRGPSV TVEAACASSL VSIHLACQSL
     LTGESALALA GGVNINLDWR TTIGFTRAGM LSPQGRCHAF DSRANGFVRS EGSGMVVLKR
     LSDAERDGDR ILAIVRGSAV NHVGHSQGLM MPSVSAQKQV LGKALARAGV EPGQVGLVET
     HGTGTPVGDP IEFEAVASLY GKGPGRCALG AVKTNVGHTE SAAGVIGFIK TVMALQEGVV
     PPNLHFQSWN PQIPAQGTRL FVPTRVEPWP VRGESRFAAV SAFGVTGSNA HLVLEQAHRP
     TPSARVPAPR RRQEQERLFP LSAGSPDALR GSAARVASWL ASEGADSPLG DIAHTLAVRR
     SHALHRAAVV ASSREELAAG LRALAEGTPG KGTVTGRVEA ASQPVWVFSG YGSQWEGMGR
     GLLDQDPAFT RVINELEPIA AREAGISLRQ LITSTLPMDR MDVVQPLLYA LQVALAATWR
     SHGVHPSAVV GHSVGEVAAA AAAGMLTLEQ GMTVTCIRSR LLQRMAGGAM AVVGLCEEQV
     VEDLARQGQP GVSVAVVASP ASTVISGDVQ GVKLLMDHWS SQGHFVSPVA VQVAAHSPQV
     EPVLGELALA LAALRPSPPQ VPFYSTALDT PRAEAVCDAQ YWVTNLRSPV RFSRAIEALL
     TDGHELFVEL SPHALLTASI EETATAMGRG ARVLPTLLRE QPERTTFHTH LAALHCSGGR
     VDWSAMYPEG SLADLPATVW ERRPYWPQKP TTPMLSHSSA HPLLGIQVQV PDDTGEGVRH
     VWKGDVGTAP HPWLGDHRVR KVPVFPGAAY IEMAIAAACE VFHCAPEHVR VTNVELQQLL
     LLTEHVEVCT VASPHRGKLR FEVLTRGAAG TWVCHARAEL AHETNDVLAT RSEREDLTAV
     HDTGGHETSA LYRRLHKLGL NYGPAFSGLS RLVAGSLPSQ GRWGQVSIPE AARLRQGRVW
     LHPALLDSCL HALATLVLEE AGGENEDSPW LPTSVAQIQL SGDPSKIQWC RAWIDASKDG
     AITGRLHLLD PAGALVGVLE GIQLIRMKPQ QAVDALRDRL FQTVWEEVPL PRAEPLSPAG
     RWLILAEDGG KDFAKGLIEA LAAHGAQGEL LPETRPVQAT SVTPSVSAAG ASAPYQGLVF
     CASLPAKTDA PSQIDTLEGL KRISQVAGLV RAHAEGHTLP RLWLITHGAR PVLPEDPVRP
     DQAALQGLAR ILNYEHPELR TTHIDSDPSA GPWQIAEELL AGRNEDEVAW RGGTRRVARL
     VSSPLRPNER LRPQPVSLRY GRDGFLLEDD GSGTLEGLRF VARERRPPRK DEVEVQVRVA
     SLNFRDVMIA LGILPFEGLG RPTLGADCAG VVTAVGSGVQ HLRPGDRVMA LAGGAQGTFS
     SFCLLPAHCA AKLPDGLSLE VAATLPATYG TAWYGLHRLA RLAPGESVLI HSAAGGVGLA
     ALAIARARGA RILATAGDEN KRAHLRDMGI DHVMDSRSLN FAAEVLQLTA GRGVDVILNS
     LAGDALRAGL EVLAPNGRFI EIGKKDLYGN SKVGLRVFRH GITFSSIDMK LLDPKRIQEV
     LQEVLDEVSS GRLPPLPYRL FPFAQATEAF RIMASGKHIG RLMVTLPDSG EHLVQPTPGS
     SQAVRVGGSY VITGGLRGLG LETARWLTSH KAGRVVLNGR SAPSEETLAI VEQLRSQGTE
     IDVVLGDISL PGTAQRLVAA ANAGGRTLRG VVHAAVVLDD APVARLDPDR ISRVWQPKVA
     GAWNLHQATL GHDLDWWVAF SSQTSLVGNA GQGNYAAANS WLDAFVAWRR RQGLPALAIN
     WGAWGEIGRA QDFKARGFTT IGTREGMTAL EALLIHNRTS TGMFAFEPHM WFRSFPQAAA
     SPFFARILDT MPQQTQSQEA ADTAPLEAIR TATPGPRRQH LLQSHLVTQL GVVTGLQAAT
     ISPDTAFTLQ GLDSLMAVQL RNLVRTSLGI ELPINAVWTH PTPAKLATYL DGVLGQDIRT
     PGDRS
//
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