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
//