ID Q1D4E8_MYXXD Unreviewed; 1422 AA.
AC Q1D4E8;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE SubName: Full=Polyketide synthase type I {ECO:0000313|EMBL:ABF87608.1};
GN OrderedLocusNames=MXAN_4300 {ECO:0000313|EMBL:ABF87608.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF87608.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF87608.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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DR EMBL; CP000113; ABF87608.1; -; Genomic_DNA.
DR STRING; 246197.MXAN_4300; -.
DR EnsemblBacteria; ABF87608; ABF87608; MXAN_4300.
DR KEGG; mxa:MXAN_4300; -.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_2_7; -.
DR OrthoDB; 5476655at2; -.
DR Proteomes; UP000002402; Chromosome.
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; cd08955; KR_2_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 2.
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; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
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; 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; 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:UP000002402};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 37..462
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1324..1401
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1422 AA; 150166 MW; 6DC757EE0B6C9E3E CRC64;
MMNRKDGFMA ELSPLQQALL TIEKLQKKLA TASNGEREPI AIIGMACRFP GGATSPAKFR
DLLWGAREAL TEIPSDRQAL QGLYDPDPSR PGKLAMRRAG FVDEVDRFDA EFFHISRREA
EGMDPQQRFF LEVSWEALED AGIPPHQLQG TRTGVFAGVH AKDYAFVTGG GLEKVSAHYS
TGVDASYVAG RLSYLLGLEG PSMAVDTACS SSLSAVHLAC QSLRTEESTL AIAGGVKLIL
APQLSVFLSK AGALSPSGHC RTFDRDADGM VQGEGCGVVV LKRLRDAVRD GDRILATLRG
TGMNHDGASG GLTVPNVGAQ EALYRRVLQR AGIEPGQVDY LEAHGTGTRL GDPIELDGVS
RVYGAARTSE RPLWIGSVKP NIGHTEAAAG IAGLIKAVLV LQAGEVPPSI NFEHPTPEFA
WEGSGLAVPR ARTALAEKDG PHRVAVSSFG MSGVNAHALV EAYAEAAHAA VDAGPYVLPL
SARSEPALRT LAASWLQYVS EAGPGARLQD ACFMAGAGRS HHAHRAVLVA RTPEALRAAL
HAVTEGRDAP GVNRGSGEGE PVFLFGGTEP EASRLMRELL GRDVFRAHAE KVDAVFRQVA
GGSVIEQVAG AQAGEGHPVG TLLVLQLALA ELWRACGLTP AAVSGFGVGA LSAGVVAGAL
SVEDAVRLAL QLTPAQPVRP QPVKYPFFST VDGAWVEAGA TVPGAYWERQ RAAVIDPASS
VANLCARNAS AFIQVSCEAS VGAALEATAR SRGSKAVILR ASRPGDDAWT GVLGVIAGGY
SSGGSIRFEG LFTGARKTVV PTYPWQRERY WWDGAVAPAP SSVQPVRDAS PRDLFCELTW
HARTVGQGPV DAEGRWLIVS TQPAASESLR QSLSTAGGTV RVAIVGSEQA SVLREWLSES
PAPRGVIYLS GSEHPESLEG LHTSVQREVH AAASLVQTLA RHSAPTLPRL FLVTQGSQAA
DGAAGPTAIA GAPLWGLGRV VAYEHPELAC KRIDIEPAAF GALVTELARK VSASADDDEV
VLRGEQRLVP SLTQTQTIPE GTGAFRPRQD RTYLITGGLG GIGLRLASWL VERGARHLAL
CGRKGETDEA RQALAPLRAA GARVETFRVD VSRPESVAEM LAAVRRGGAP LGGIFHSAGV
LADSSLLQWE PQGFETVMGP KVDGAWNLHA LATDTTLEHF VLFSSTASLI GSPGQASYAA
ANAFLDALAH FRRARGLPAI SLNWGSWGEV GMAVADARRG DRLAERGMSP MSVDEALAAM
ALVLAENRVT RGIARFDVTR WTASHPSIVA SSLFRTESVT DAVPDVMEAP RKLREVLLAL
EGSARRGVLE ARLKEMISEV GKIPTTKLSS TDSFDALGFD SIMALELRDM VLGELDVSMP
LKSFVDESSI EQVTAELLGK LAVASVLGAA SSERDDSKRV LL
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