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PKS1_METGA
ID   PKS1_METGA              Reviewed;        2148 AA.
AC   A0A0B4G9F9;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   04-MAR-2015, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Polyketide synthase 1 {ECO:0000303|PubMed:29958281};
DE            EC=2.3.1.- {ECO:0000269|PubMed:29958281};
DE   AltName: Full=Conidial pigment biosynthesis polyketide synthase {ECO:0000303|PubMed:29958281};
GN   Name=Pks1 {ECO:0000303|PubMed:29958281}; ORFNames=MGU_09383;
OS   Metarhizium guizhouense (strain ARSEF 977).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=1276136;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 977;
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
RN   [2]
RP   IDENTIFICATION, DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY,
RP   INDUCTION, AND DOMAIN.
RX   PubMed=29958281; DOI=10.1371/journal.pgen.1007472;
RA   Zeng G., Zhang P., Zhang Q., Zhao H., Li Z., Zhang X., Wang C., Yin W.B.,
RA   Fang W.;
RT   "Duplication of a Pks gene cluster and subsequent functional
RT   diversification facilitate environmental adaptation in Metarhizium
RT   species.";
RL   PLoS Genet. 14:E1007472-E1007472(2018).
CC   -!- FUNCTION: Polyketide synthase; part of the Pks1 gene cluster that
CC       mediates the biosynthesis of an anthraquinone derivative pigment that
CC       contributes to conidial pigmentation that provides protection from UV
CC       radiation, heat and cold stress (PubMed:29958281). The polyketide
CC       synthase Pks1 produces 1-acetyl-2,4,6,8-tetrahydroxy-9,10-anthraquinone
CC       though condensation of acetyl-CoA with malonyl-CoA (By similarity). The
CC       dehydratase EthD and the laccase Mlac1 further convert the
CC       anthraquinone derivative into the final conidial pigment (By
CC       similarity). {ECO:0000250|UniProtKB:E9F646,
CC       ECO:0000269|PubMed:29958281}.
CC   -!- INDUCTION: Highly expressed during conidiation (PubMed:29958281). A
CC       conserved conidiation regulatory pathway containing BrlA, AbaA and WetA
CC       regulates expression. During conidiation BlrA up-regulates AbaA, which
CC       in turn controls WetA. Moreover, the Hog1 MAPK regulates fungal
CC       conidiation by controlling the conidiation regulatory pathway, and that
CC       all three pigmentation genes Pks1, EthD and Mlac1 exercise feedback
CC       regulation of conidiation (By similarity).
CC       {ECO:0000250|UniProtKB:E9F646, ECO:0000269|PubMed:29958281}.
CC   -!- DOMAIN: Multidomain protein; including a starter unit:ACP transacylase
CC       (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes
CC       repeated decarboxylative condensation to elongate the polyketide
CC       backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and
CC       transfers the extender unit malonyl-CoA; a product template (PT) domain
CC       that controls the immediate cyclization regioselectivity of the
CC       reactive polyketide backbone; and an acyl-carrier protein (ACP) that
CC       serves as the tether of the growing and completed polyketide via its
CC       phosphopantetheinyl arm. {ECO:0000305|PubMed:29958281}.
CC   -!- DOMAIN: The release of the polyketide chain from the non-reducing
CC       polyketide synthase is mediated by the thioesterase (TE) domain
CC       localized at the C-ter of the protein. {ECO:0000305|PubMed:29958281}.
CC   -!- DISRUPTION PHENOTYPE: Results in red conidia.
CC       {ECO:0000269|PubMed:29958281}.
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DR   EMBL; AZNH01000061; KID83385.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B4G9F9; -.
DR   SMR; A0A0B4G9F9; -.
DR   EnsemblFungi; KID83385; KID83385; MGU_09383.
DR   HOGENOM; CLU_000022_6_0_1; -.
DR   Proteomes; UP000031192; Unassembled WGS sequence.
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   Gene3D; 1.10.1200.10; -; 2.
DR   Gene3D; 3.10.129.110; -; 1.
DR   Gene3D; 3.40.366.10; -; 2.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
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; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020807; PKS_dehydratase.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR030918; PT_fungal_PKS.
DR   InterPro; IPR032088; SAT.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF14765; PS-DH; 1.
DR   Pfam; PF16073; SAT; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF47336; SSF47336; 2.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Repeat;
KW   Transferase.
FT   CHAIN           1..2148
FT                   /note="Polyketide synthase 1"
FT                   /id="PRO_0000445744"
FT   DOMAIN          1678..1752
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:29958281"
FT   DOMAIN          1793..1870
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:29958281"
FT   REGION          19..261
FT                   /note="N-terminal acylcarrier protein transacylase domain
FT                   (SAT)"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT   REGION          397..832
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT   REGION          929..1233
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT   REGION          1310..1624
FT                   /note="Product template (PT) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT   REGION          1619..1657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1755..1796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1882..2146
FT                   /note="Thioesterase (TE) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:29958281"
FT   ACT_SITE        566
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        1018
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        1973
FT                   /note="For thioesterase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q03149"
FT   MOD_RES         1712
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1830
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2148 AA;  234867 MW;  4AC0D8BDA6206623 CRC64;
     MNHVTIKQSD TRADPFRVFI FGDQSSCNLS NLQLLLFKKS NVYLASFIDQ VNLTLRHEIA
     RLTAAERQSF PAFSSIQNLV ARALKKDTSV ALESTLATIY HLCCFLNYFG DGQEAYPTGP
     TTHVSGLCIG ALAAAAVSSS KSLAELVQAG IDAVRVSLKV GLLVARTAAL FSHQESNGAS
     SSPWSYAVPD SQLPLALAEE AIESYQAKTN IPPLSLPYIS AKGQNSWTVS GPPAIVQHFL
     QTSQFEKTLR LTPLAVHAPY HAPHIFSAVD VQHIMHAVGT VSNFSSKLSF ISSSSSRNLP
     TGLKFQDLLY RAVEDILILP LDLREAAENI RLVLEATDNV QQCALFPIST GVCPSLKQSF
     SPAMASRVSI VDCIMERATA DAGPKSTSGP KPSESKIAII GMSGRFPESA DVEAFWDLLH
     QGLDVHRPVP PDRYNGELYY DVTGKRKNTC KVMHGCWIND PGLFDAKFFN ISPKEAEQSD
     PGQRLALATA YEALEAAGVV ADRTPSTQRD RVGVFYGMTS DDYREVSCGQ NVDTYFIPGG
     NRAFTPGKIN YFFKYCGPSV SVDTACSSSL AAIHLACNSI WRNECDTAIA GGTNVMSNPD
     SFVGLDRGYF LSRTGNCHTF DDEADGYCRA DAVGTVILKR LEDAIADHDP ILGVISGALT
     NHSADAVSIT RPHSGAQEEI FSKLLTESGV HPHQVSYIEM HGTGTQAGDA TEMTSVLNCF
     APSTSPRRLP HESLHLGSTK ANVGHSESAS GVSALIKVLL MMEKNIIPPH CGIKGKINHK
     FPTDLDQRNV HIAKTATQWN RRNEFNNIRR AFVNNFSAAG GNTALLVEDY PLLIADSSQQ
     DARTAHVVTV SAKCIKSLKG NLENLKKFVQ KQASTDGFLP KLSYTTTARR MHHPFRVAIP
     AANSEQLLSA LDEELKHDSY TCSSESPVAF VFSGQGSQYS AMGQHLLHFT IFRDEVHAYD
     ILAQRHGFPS IMPLIDGSVD IEDLEPLVVQ LGTVCVQMAL ASLWMALGMR PAYVVGHSLG
     HYAALKVAGV LTASDTIYLV AMRARLLQNK CSRGSHAMLA IRSSAAAIQA HLDEGIHDIA
     CINGPQDTVV SGCIDDIDRL SQKLMDKGIK ATRVNVPFAF HSAQVDPILD ELEAIASQVE
     FHTPRVAIGC PLLGRTFKAG ETPSIEANHI RRHCRETVNF FDVLRSAKDE GFVSEKTAWI
     EIGPHTVCSN LVKANINQDI VAVPSLMRNK DGWQVLASSV ATLYRHGSSV AWDEYHHDFE
     ACKEVLRLPA YSWDNKLYWI DYVHDWLLTR GDPPVQAAAS LPAPPSSFST ASVHRIVHES
     VDKGKLTLTA ECEFTNEQLR EVVYGHVVNG NRVCSSSLYT DFGVTLGSYI LEKYRPDLQD
     HAVDVQDMVV NKALVHKEGP TMLLRIDVVL DMTDSKAASM SIYSVNSKGN KTADHAQSSL
     HFEQPKVWLK SWDSTQYYVE RSIEWLKEKA DQGLNSRMSS GVIYKLFSSL VDYSTAYKGM
     QEAIVNTEDF EATALVRFQV DEGNFRCNPM WVDSCGQLAG FLMNGHAKTP KDQVFINHGW
     QSFRTVRKFS KDKTYRTYVR MRCIEGTTYA GDVYIFDDEG IVGVCGSITF QGIPRKVLNT
     AMPPPKSQNE APVRSAPAKP AAKPPKSASS EHSGHFARHS NIEPLKLDAA LKSATTARNP
     MLAVFKIVSE EIGIPSASVD NGLVFADYGV DSLLSLSISG RLREELDLDV ESSAFETCAT
     LADLATHLGL DTFSSDQSSG QSSSSGGLSP RSDSIGEITS SATTPPSLSP RGSVSGSQCK
     DVCAILAEEI GVSMSEITND TDLGALGMDS LMSLAVLSRL REELELDLEG DFFVSHPNFS
     SFKHMFQQGH GDEVEPEPSA ELKQYRATST LLQGNPKSAL YTLFLLPDGS GSSFSYAPIN
     AVRKDVCVFG LNCPWLKSAE KLVQFGLKGL ATLYVEEIRR RAPHGPYNLG GWSAGGICAY
     EAAIQFTREG ETVERLILLD SPNPIGLEKL PARLFDFVNG LGLFGDGKAP DWLLAHFLAF
     IDALDEWKPV PWDKALGGNS PPPRTYILWA EDGICKGTDA RPEYRDDDPR EMKWLLENRT
     NFGGNNWDVL LGQQSLSIER IQDANHFTML RKGKNSERVA AFIRSTFG
 
 
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