ID A7EA79_SCLS1 Unreviewed; 2148 AA.
AC A7EA79;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Ketosynthase family 3 (KS3) domain-containing protein {ECO:0000259|PROSITE:PS52004};
GN ORFNames=SS1G_02211 {ECO:0000313|EMBL:EDN99357.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN99357.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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DR EMBL; CH476623; EDN99357.1; -; Genomic_DNA.
DR RefSeq; XP_001595995.1; XM_001595945.1.
DR EnsemblFungi; EDN99357; EDN99357; SS1G_02211.
DR GeneID; 5492442; -.
DR KEGG; ssl:SS1G_02211; -.
DR eggNOG; KOG1198; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; A7EA79; -.
DR OMA; KDVQHYT; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion 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; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 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; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR001227; Ac_transferase_dom_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; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF18; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43775; 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; 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 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; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312}.
FT DOMAIN 6..433
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1397..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2148 AA; 235530 MW; 06B07302E57385EB CRC64;
MVQNSQEPIA IIGFACRLPG GNTTPKKLWE FLRRGDVASN KVPKSRFNVE GHWDGSQKPH
TMRTCGGMFL EDIDLADFDA SFFEISRIDA ISMDPNQRQM LEVVFEGLEN SGIPLESLDG
APVGCFIGSY ASDYSDMQNR DPEDKPANFK IGVGRVTMAN RLSHFLNIKG PSMTIDTACS
SSLGSLDVAC RYLQSREINA AIIAASNLYL NPEHVMNLGE VSNAYSPTGL CHTFDLDADG
YVKAEAVSSI IVKRLSDALR DSDPIRAVIR GSATNSSGRT SGIATPSAEA QYAVIRAAYA
NAGITDLDET AYLECHGTGT QTSDTIEAEV AALAFSGTRS RDRPLIIGSI KSNLGHAGPA
AGISGIIKAV MAIENGIIPG NPTFINPNPK IDFARLKVKA TRTAIPWPAS SIRRASVNSF
GHGGSNAHVI FEQPEFSDGP KHATSYLSDS DDFDLDEDDS EHPYTLVLSA NDKASLKANI
MALCNHLINP SVKVDLKDLA YTLSERRTRF WHRAYITTQN TDIDENDFII GQKNPEALRI
GFVFTGQGAQ WPQMGKKLLQ FFPWTREILE HLDDALQSLS EPPNWLLIHE LTEVRSTEHF
RRPEFSQTLV TALQLCVIEV LRKWGVKPQS VVGHSSGEIA AAYAAGFLDQ ATAIKVAYYI
GRAALNRKNE VESGAGMLAV GLGAEGILPY LEKYAGQVWI ACYNSPSSLT VSGKRGAFES
LAEELKAGNH FCRLLEVDLA YHSELIGVIA EEYEKILKSD FTCLRGSSDV SMFSSVTGSK
KNTTTDALYW KTNLVSPVCF DKALIELLSQ EKGPNFLIEI GPSGALARPI SQILKSLPNG
DSISYNPSWA RGQHAGKAIF DLAGFLFVTG HDINLGNVNQ YTEAKTLIDL PNYNWNHSIK
YWHENESSKD WRFKKFVNHD LLGSKVLGTT WQSPTWRKLL NLSDVPWLKD HKIGSDVLMP
AAGYITMAVE ALYQKTRVLA TDDKTINSPN ELCYRFRNIR FAKPLVLEDD KVSTVLLSLT
QKHGVTDWQE FRISSTTGDL MVEHCSGLIR LQDPVDESLA ESDDKPLQYP TVGKAWYKSQ
AEAGYGFGPS FQKLLNVESK SGQRQCRVKV SLEEPSSKWS PQFCYPIHPA SLDGCFQTVT
PALWAGEHSS VNAVLVPAII DDLIINSVPS GVKEGLSLAT SEYSGHGRLE EAKSYFANCS
VYQPENGVLL MQMTGLRFAK LDMGIKTDPH VFHCISWKPD VTFLSHEKLV GLNQENFEPQ
LDTVIDLIAH KKPGLIILEV KLNSTEIRST WFEPGHLSSR SAYLQYDFAS DNARDLASLG
IKYKTKSNTS FFLLNTTKEA LGFSSDAMYD LVILKISKTS VVDQIVNDIL RYIKAHLFHK
GYVLVVDEED RLQSRISSVH TPSLDESVKS PSPSSAGSTK PLEIATKPFE SIAENSEISG
TIEKVVSEEV HKSKRKSLES DAAVAGLTQG FSNHETMREA MKVHKFTSIL QVPSDEDSLA
WSLYTNEAQV GVNSHLRKLI IVQLSENTPS LDPSLKAALE LSGWKIKNVT YPPKILTETG
AVILVLDELY GPVLTNIDAT QWGGLKMLIS SGNHLLWVTK GAQYKVTHPN NALVQGLFRV
ARRENPSAKL NILDVESSTG PATEYAIDAV LKSLESSPPN SGFDVDTEFV ERNGILYVQR
VVPDFPVNEF KRAEVEGAEP ILRNLHEVEA AVQLRAESLG TFQGLTWCET AVGEVPVDPE
KIEIDVMAVG VNFKDVAVTM DIVPGNEYSI GYEGAGIVKR LGPGVTKFKV GDRVCFLNNG
SYANRLQVAI GRAHAIPDSM SFEDAATIPM MYLCSFYSLC DIANLREGQS VLIHSASGGV
GIACLQLARH MKAEIYVTVG TEEKGKFLTD SYGIPPSRDP FIARLLGQIF ELINGGHIKP
INPVTVFGFN DIPAALTLMH SGRHIGKVVV SDKGKSLQVP IRPATQKLKL RPDASYLIVG
GLKGMCGSLA IHMARHGAMN IIACSRSGIN DAASQKIVMN CLAYGCKVVD AQGDAANVNF
MRKVFRQASP RITGVIHGAM ILRDRPLETM TLDDYHTALH AKINGTWNLH YICQEQKEPL
DFFTLLSSIS GVVGNKGQAN YAAGNTFLDA FAEYRESLGL RANSVDLA
//
