ID A0A365NCF9_GIBIN Unreviewed; 2591 AA.
AC A0A365NCF9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Beta-ketoacyl synthase domain-containing protein {ECO:0000313|EMBL:RBA18238.1};
GN ORFNames=FPRO05_10533 {ECO:0000313|EMBL:RBA18238.1};
OS Gibberella intermedia (Bulb rot disease fungus) (Fusarium proliferatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=948311 {ECO:0000313|EMBL:RBA18238.1, ECO:0000313|Proteomes:UP000251714};
RN [1] {ECO:0000313|EMBL:RBA18238.1, ECO:0000313|Proteomes:UP000251714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ITEM 2341 {ECO:0000313|EMBL:RBA18238.1,
RC ECO:0000313|Proteomes:UP000251714};
RA Almiman B.F., Shittu T.A., Muthumeenakshi S., Baroncelli R.,
RA Sreenivasaprasada S.;
RT "Genome sequence of the mycotoxigenic crop pathogen Fusarium proliferatum,
RT strain ITEM 2341 from Date Palm.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RBA18238.1}.
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DR EMBL; PKMI01000014; RBA18238.1; -; Genomic_DNA.
DR Proteomes; UP000251714; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
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; 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; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR011032; GroES-like_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
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; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 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; PF08242; Methyltransf_12; 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 SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..433
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2508..2585
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 445..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2591 AA; 284522 MW; 5E90AD9278C156B6 CRC64;
MEENRAPEPI AVIGLSCKFA GEATNADNLW QMIANGRDAW SQIPLSRFNW AGSFHPDHEK
SSTMHVRAGY FINDDLGNFD AAFFNLSAET AASMDPQFRL QLESVYEALE NAGQPIETIA
GSDTSVYMGT FNHDYREGMI RDEDDLPRFM ITGTGAAMAS NRVSHFFDLR GASMTLDTGC
STSLVALHQA VSDLRSGNST MAIVGSSNLM LNPDMFKALG SIGVLSPDGK SFSFDSRANG
YGRGEGVATV IIKRWRDAVA AGDPIRAVIR ETCLNQDGKT ETITSPSSNA QEQLIRKCYK
NALLDPLETQ YFEAHGTGTP TGDPIELQAV AAVFQSRQST EPLQIGSIKA NIGHTEPVSG
LASLIKVVMA LEHGALPPSI NFEKPNTKLN LKEWNFEVPQ RLEPWIPNSN GIRRASINNF
GYGGTNAHVI VEMGPQWRTD SGIHATNGNS HINGHTNGTE STLGSDQKPT SEGNNTNFSR
NKTKVLVLSA RDEQTCQHMI SNLKDHLRRL KDHGKPDQLL QSIIYTLGHR RSMMPWVAAC
PISYTRGIST VVESLESSQF KPKRIVRTPR IGMVFTGQGA QWYAMGRELI IAYPVFKASL
ELGDAYLREL GADWSLMEEL MRDATDTKVY DTAVSIPICA ALQISLVNLL QSWGIKPAAV
TSHSSGEIAA AYAAGVIDYR ASMAIAHYRS VLSADKALRG SVKGGMVAVG VGPDHAATYL
EELQSDGKAS IACINSPKSV TVAGDLSAIL EVETRAKDDG VLASRLNVDI GYHSHQMEPI
SHRYRDALRR VKLFNSANNL ESIIYASPVT GGRMTEAEEI ASAEHWVASL VQPVQFLDAF
TDMVLGGFDP SGTSVDVVVE VGPHSALRGP IKQILELPEF GGLQIPYYPC LIRKNDARDT
MQALAANLIG EGLGLQLDCL NFPYGRESFV NVLTDLPSYP WNHQTRHWVE PRFNRALRER
DQEPHSLIGS LVLGTERDSP SWRHVLRVSE SPWLRDHVVQ SNVLYPGAGF ICLAVAGVAQ
MVSMQVIKSV DKLGKDRQIS GYRLRDVEIL RALLVPDIQP LELQTKLCPA SDREIGLRGW
YHFEILSVTG ENRWNLHAKG SIKVEFADES TPGVGGLEAI SPLIPSTARR IAPDDVFATF
RSVGIEHGPA FQNFKTILQR QTEPRSKATI IVADTSANNT IIHPTTFDSV VQAAYTALPK
AGYFQESPRV PRRFRHIWIS SNIGHEAGHE FEACSRVNDA SAQSFEADVR LFDAQKDSHG
SQTPVLEIQG LFLQSLGHAV GTGNKRPWEN EVCNRVEWDI DMTVADPRTF ERIKKDLTLS
DPGESFTKEL RPICLYYIHE ALAELSDPDV SSLSGHLAKF YGWMQDQVKL ALPETKSDNI
DETLDLRSLN PGLRLFLISQ AITKSVAGEM ICRLGPHLAD ILRGKTTPLE VMAHNNLLSR
YYEESPGLKR CFRQLSQLLR KIVHKNPRAR ILEIGAGTGS VTRHALEVLG TRDSGGPLAE
LYHYTDISMG FFEAAREEFS GWSDVLAFDK LDIEQDPAEQ GFKLGSYDIV IACQVLHATK
SISHTMANVR SLMKPSSSLL LIETTQDQID IQFIFGLLPG WWLSQEPTRQ NSPSLSIPSW
DSALRTTGFT GVDMVVNESE DASEYAFSTI MSHAKAEVDS SVGIRSEDIV LVTTSKSVPP
RDWIVSLARS IGGKDDSFAV QLLDAPDATD STYRGKICVF LAEVEDNVLF ELNLTLLEGL
KLVVANCRGL LWVTIGGAIK CEIPCSALAT GFVRSLRNEY VGRRIMTLDL DPSPTTWSSA
ASDAISRILK HSFRDTDDSD MFDGSAMDFE FAERGEAIMV PRYYKDTIRN ELVMPQKNQQ
SPDNAVTELF HQEHPVRLHV GTRGLLDTLT FVHDELVMTA DDSQMLESFV EIEVRAYGLN
FRDVMVAMGQ LEDKIMGIEC AGIITKVGAV AALHGHFVGE KVFALLRGPF ASRVRTEHWN
AVSIPEATTF EEAASMPMVF TTAYVALFDV AHIQRGQSVL IHAAAGGVGQ AAIQLAQHLG
AEIYVTVGSP KKKKLIQQRY GIPDHHIFNS RDASFASGVR DITEGRGVDL VLNSLAGPLL
QESFDLVAPF GHFVEIGRRD LEQNSFLEMR PFIRHISFSS LDVLHMTRGK GPDVRRILTE
IARLKQRNVI APVDPLTSYP ISDLTKAFRL MQTGQHTGKI VVSTGPLQKV AVQPYPKDIK
LSPDASYLLV GGLGGIGQCL ASWLVNLGAR QIILMSRSAG TKDEDAVFIR DLAETGCRIE
CISCDVSKSH DLERALQLCT AKGLPPIRGV IHAAMVLQDS ILEQMTIENF RAAVVPKVHG
SWNLHTKFQK VDFFIMLSSI NGIVGYASQS NYSAGGSYQD ALAHWRVTIG LPAVSLDLCA
VKTVGYVAET AGVAVRMQRA GHMLLREDQL LGLLESAILH PFTPQIVAGL NTGPGSHWNR
DGESQLGRDA RFSALQYRQP REQRARDADM AHKNSLAASL AEATSRTDAE AIVFEAIAQK
LSSIFVIVVG EIEPSKHPSY YGVDSLVAVE LRNMISLQAA ADVSIFSILQ SQSLGALASE
IVDKSRYTEV I
//