ID A0A0D1DMG7_USTMA Unreviewed; 2121 AA.
AC A0A0D1DMG7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Polyketide synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=UMAG_06414 {ECO:0000313|EMBL:KIS65714.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS65714.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS65714.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CM003162; KIS65714.1; -; Genomic_DNA.
DR RefSeq; XP_011392698.1; XM_011394396.1.
DR STRING; 237631.A0A0D1DMG7; -.
DR ESTHER; ustma-q4p0e9; Thioesterase.
DR EnsemblFungi; KIS65714; KIS65714; UMAG_06414.
DR GeneID; 23566013; -.
DR KEGG; uma:UMAG_06414; -.
DR VEuPathDB; FungiDB:UMAG_06414; -.
DR eggNOG; KOG1202; Eukaryota.
DR InParanoid; A0A0D1DMG7; -.
DR OMA; WKDSIWA; -.
DR OrthoDB; 3378513at2759; -.
DR Proteomes; UP000000561; Chromosome 23.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
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; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF16073; SAT; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 2.
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:UP000000561};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 500..938
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1625..1700
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1750..1827
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1599..1619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2121 AA; 231501 MW; 2B6A38F812FA08D6 CRC64;
MSAAILPSSA ISFDSTFSSF DNAVPSDDSQ KFDPPSPPPL PRASVIVFGS QGSDFLNAFD
AIIGLSHYHA ELAAFLSLAL TAVRAELQSV ASRYHHVPES DEFTTTGQRK AEVELLASLP
PFEPFAGLRT LVDFHRRSQQ KDPTINGVLL CLLQTASVVA VCCVAHHDQD DPHAPSTASG
LKRAWKALTQ PCSHLLGYCT GALSAFSLRE MVEHEATASS VDIWAYAKDA IRAIRICFWI
SLRSAHARLR LISADDSATA SDPWSFLVSV KDPDLIQNVY LYLARFNDLE QQRPLDKPIP
LVVSARALNQ ISIAGLPRQL QRFKAYLLEH LGSKCKMFSL KLFSPYHMSD LAPEADLVMR
DLEHRKLVDP SNLSPSLKSL WETKNANILS EANLQEALRV LVATNLCATA DWNAMVDQLV
SLEGELPRSM HPEDRVVVSF CPGASLGADI AMRLSSLHDS CDSNGSVVHI DVSAALSEHL
MHPYYSGLDV PFVSQSDVNG EEVVIVSMAC RFPGEVCNPD QFWTCLETGR STVTEIPKHL
FDIDAYYGDG VNQTMARHMH ALPENVVKSM DARLFSMSPK EIEQLDPQHR LVMLCSYEAL
ERAGYSAEAN SPSSFDGKRI AVCMAASWDD YRENASWNIG SYFITGNIRA FIPGHVSFSL
NWEGPSVSVD SLECSAVSAL QWSRRALLSG QCDVALAGAV NVLTQPQMFI AMDKEGILSR
TGTNATFSSK LDGKTRGDGC GVLLLKRRST ALRDGDKILA TLPAARTTYH GSAHESEEAS
TNQSRFLARV MSEASVRASD LIHIEASGFH TQQAEAAEFE SFSRLLPQSQ GDRSSQVRDR
ISVASSRPNI GAGEAVSAMA SVIKAVLMFQ QGSVPRQISI SDPSELQPSI TAICAGSSLF
VPTQARRLPS DRDHEGRHVI LVNSLASTNC HGVVLVGAPT TDDVAPLQIR SKALDATFTR
TEGTWVFLLS AKTRESAEML RKALIDYLRR DVNLADLSYT LTCRRTHHPF RLSVVASDKD
ELVRSLRTAE FIEAKALADL PAFGLVLRHP ERSACQNMEG SLDLIVGLRD RFEELTSVMG
YSEIPADTER KLNLKQVCLA LLLDDCGVHP LSFHGSYDLM QLLQRSFPAA KESDLSKRFT
WIHIGSLISI STTEAAEQAK PAGSVADGQN QQRSLLSTLG SLHQKGHCIR WIEYFRPLLA
KLNFIETLPT YLFNLQQHWM EYHDRDLLPR SASKEGQGGQ RIRHISDGVL YSPSSQVEAW
VSPSQPLLSE QTAADDRLRT YSSSLFDEAA AALLSEASPG ALIAELVVEA IKEACESIEG
TVEAYEHRPV RLYELFLAEV VKQWPATGKV KLSVKSVQQT GNRSEGTVQI SFDATTSPVG
ECRYEWITQT NMHQRWWKLQ KLLAEKISTI KDKGELFSPK LIYKTLGVDP TTTTMSIHSA
YLDCQSSEAV VCNTIRTHTS AVGQIALPQL LSSLEEIARW FVGDKPSSAD GKLTFIGVDE
LLICADWLDS LTRPAGASVS YTAYISQSHT DGSLRASTDG LELDILILDG MHKVVGELSR
LRLAKCNSTA KKTTSKCASE STLALSSGVK TVSGSFPVQE PVEQHKEPRS TSAKPVAGRQ
SSRAMGLHAK VLDVLASELG VAVEEMKPTV KFADLGLDSL MSLVCISTLE TMNLGLDIPQ
SLFMECDSPA ELLQFIREQV SDGTDVGQLG PDESTNATEQ VQGSDAVVQL SPSANAAETQ
LTATTGQGSS AVEEAMKAIR CTVETELGVD LGSIDEDANL ADLGMDSLMS LLVLGNLSGT
LPIELPSSLF MDCSSLGEIR SFMTSQLGAA RDCARSDTVD QRDSNSQIAF FLPPVKKPIL
IREGSSSGMD PPLFLLPEGA GMATVYQQFP GIDRAIYSIN SPFLADTSAW TGGIAQIARY
YLESIKLIQP VGPWLVGGWS FGGMAAFEIA RLLADCGGDK DRVAGLFILD SPSPEYPPLP
MSILDWINSA PEVRDMAPPT MSAKLIAHFR ATVDSLVGWE PTTMRAADEA SKPLPKTWYI
VAEQALPGKM EDVKELNETV RWLFRSKRAE KSGADGWQHL IPHHLTVIGV AEANHFTMVR
RPNVGQVAHI LQNACRNALL N
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