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BA17A_METAN
ID   BA17A_METAN             Reviewed;        3068 AA.
AC   P0DUT7;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 1.
DT   03-AUG-2022, entry version 4.
DE   RecName: Full=Highly reducing polyketide synthase 17 {ECO:0000303|PubMed:33991663};
DE            Short=HR-PKS 17 {ECO:0000303|PubMed:33991663};
DE            EC=2.3.1.- {ECO:0000269|PubMed:33991663};
DE   AltName: Full=PKS17 biosynthesis gene cluster protein Ba17a {ECO:0000303|PubMed:27801295};
DE   AltName: Full=Polyenoic acids biosynthesis gene cluster protein Ba17a {ECO:0000303|PubMed:33991663};
GN   Name=Ba17a {ECO:0000303|PubMed:33991663};
GN   Synonyms=PKS17 {ECO:0000303|PubMed:27801295}; ORFNames=MANI_025650;
OS   Metarhizium anisopliae (Entomophthora anisopliae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=5530;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=25263348; DOI=10.1186/1471-2164-15-822;
RA   Staats C.C., Junges A., Guedes R.L., Thompson C.E., de Morais G.L.,
RA   Boldo J.T., de Almeida L.G., Andreis F.C., Gerber A.L., Sbaraini N.,
RA   da Paixao R.L., Broetto L., Landell M., Santi L., Beys-da-Silva W.O.,
RA   Silveira C.P., Serrano T.R., de Oliveira E.S., Kmetzsch L., Vainstein M.H.,
RA   de Vasconcelos A.T., Schrank A.;
RT   "Comparative genome analysis of entomopathogenic fungi reveals a complex
RT   set of secreted proteins.";
RL   BMC Genomics 15:822-822(2014).
RN   [2]
RP   IDENTIFICATION, AND INDUCTION.
RX   PubMed=27801295; DOI=10.1186/s12864-016-3067-6;
RA   Sbaraini N., Guedes R.L., Andreis F.C., Junges A., de Morais G.L.,
RA   Vainstein M.H., de Vasconcelos A.T., Schrank A.;
RT   "Secondary metabolite gene clusters in the entomopathogen fungus
RT   Metarhizium anisopliae: genome identification and patterns of expression in
RT   a cuticle infection model.";
RL   BMC Genomics 17:736-736(2016).
RN   [3]
RP   FUNCTION, DOMAIN, AND CATALYTIC ACTIVITY.
RX   PubMed=33991663; DOI=10.1016/j.fgb.2021.103568;
RA   Sbaraini N., Hu J., Roux I., Phan C.S., Motta H., Rezaee H., Schrank A.,
RA   Chooi Y.H., Christian Staats C.;
RT   "Polyketides produced by the entomopathogenic fungus Metarhizium anisopliae
RT   induce Candida albicans growth.";
RL   Fungal Genet. Biol. 152:103568-103568(2021).
CC   -!- FUNCTION: Highly reducing polyketide synthase; part of the gene cluster
CC       that mediates the biosynthesis of (2Z,4E,6E,10E)-9-hydroxydodeca-
CC       2,4,6,10-tetraenoic acid (BAA), (2E,4E,6E,10E)-9-hydroxydodeca-
CC       2,4,6,10-tetraenoic acid (BAB), and (2Z,4E,6E)-octa-2,4,6-trienedioic
CC       acid (PBA) (PubMed:33991663). The highly reducing polyketide synthase
CC       Ba17a is sufficent to produce PBA and BAA (PubMed:33991663). The still
CC       to be characterized protein Ba17b leads to an increased production of
CC       BAA as well as to the production of the new compound BAB
CC       (PubMed:33991663). BAA does not possess insecticidal activity against
CC       G.mellonella larvae, however, both BAA and BAB increase the growth of
CC       Candida albicans and BAA can mitigate the fungicidal effects of
CC       fluconazole over C.albicans, suggesting that generalist pathogens such
CC       as M.anisopliae, can potentially manipulate the yeast microbiota found
CC       in arthropods (and anywhere else) by the activity of compounds as BAA
CC       and BAB (PubMed:33991663). {ECO:0000269|PubMed:33991663}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:33991663}.
CC   -!- INDUCTION: Expression is induced under mimicked-infection conditions.
CC       {ECO:0000269|PubMed:27801295}.
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 dehydratase (DH) domain that
CC       reduces hydroxyl groups to enoyl groups; an enoylreductase (ER) domain
CC       that reduces enoyl groups to alkyl groups; a ketoreductase (KR) domain
CC       that catalyzes beta-ketoreduction steps; an acyl-carrier protein (ACP)
CC       that serves as the tether of the growing and completed polyketide via
CC       its phosphopantetheinyl arm; and a C-terminal choline/carnitine
CC       acyltransferase (cAT) domain that acts like a thioesterase domain,
CC       using water as a nucleophile to release the polyketide product.
CC       {ECO:0000305|PubMed:33991663}.
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DR   EMBL; JNNZ01000213; KFG78606.1; -; Genomic_DNA.
DR   SMR; P0DUT7; -.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase 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:0009058; P:biosynthetic process; IEA:UniProt.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.10.129.110; -; 1.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 3.30.559.70; -; 1.
DR   Gene3D; 3.40.366.10; -; 1.
DR   Gene3D; 3.40.47.10; -; 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; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR039551; Cho/carn_acyl_trans.
DR   InterPro; IPR042231; Cho/carn_acyl_trans_2.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020807; PKS_dehydratase.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020843; PKS_ER.
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   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00755; Carn_acyltransf; 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   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; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 2.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW   Oxidoreductase; Phosphopantetheine; Phosphoprotein; Transferase.
FT   CHAIN           1..3068
FT                   /note="Highly reducing polyketide synthase 17"
FT                   /id="PRO_0000453547"
FT   DOMAIN          2345..2423
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:33991663"
FT   REGION          103..529
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:33991663"
FT   REGION          627..938
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:33991663"
FT   REGION          1027..1311
FT                   /note="Dehydratase (DH) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:33991663"
FT   REGION          1735..2037
FT                   /note="Enoylreductase (ER) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:33991663"
FT   REGION          2062..2240
FT                   /note="Catalytic ketoreductase (KR) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:33991663"
FT   REGION          2831..3062
FT                   /note="Choline/carnitine acyltransferase (cAT) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:33991663"
FT   ACT_SITE        274
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000250|UniProtKB:L7X8J4"
FT   ACT_SITE        721
FT                   /note="For malonyltransferase activity"
FT                   /evidence="ECO:0000250|UniProtKB:L7X8J4"
FT   ACT_SITE        1059
FT                   /note="For beta-hydroxyacyl dehydratase activity"
FT                   /evidence="ECO:0000250|UniProtKB:L7X8J4"
FT   MOD_RES         2383
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   3068 AA;  334489 MW;  B6054A700DE67DF9 CRC64;
     MLQKSYHGVV SQASYDNTCG RGSQIRRDRS RAGVRFNTEY NPVLLTVSKQ IAQDGEGYHC
     RANLINKITT KQQLAFISEL QPTQSTLKVL PVADGRKMPI EPIAIVGASC RLPGSSNSLD
     SLWELLADGG EAWSSVPADR FNEAAFHHPN ASDPNGTNNH QGGHFIDGDI RDFDHAFFHL
     SPQHAAAMDP QQRILLELVY EAFESAGWAR EACAGSRTAV FAAIFGTDYD RNLCKDLLDL
     PVYHSVGTGI AILANRISHA FDLRGPSLTL DTGCSGGLVA LHEACQSLRN GESDAALVAA
     ANLQLMPDHY IGMSSQHMVS STGRCYPFDL RGDGYGRGEG FAVVALKRLS DALRDQDPIR
     SVILNSGINQ DGYTASGITH PNRVAQADLI RDTYDRVHLH PQDTVYVEAH GTGTVAGDNE
     ELAAIAEVFA GPDRSLPLHV GSNKGSIGHT ESTSGLASLL KVILMLDHQV IPPVAGFTNP
     KPGLPLDRIK IPTQRLPWPL TEGMVPRISI NSFGYGGTNA HAIMERGPRT YDASCNTTPT
     YSPRLFVLSA NNKGSLRSLL ESYVNWIQKH PNIPLADISY TLCHRRSALP WRFSCVADSE
     SSLLDTLERG VKLISTRPPP SKRQVIYVFT GQGAQWAGMG HELLLETTPS SVFRDSIRTS
     RDILYELGAT WDLEAELLGQ DGGGRINKAE LAQPATTAVQ IGIVMLLRSQ GVRPWAVVGH
     SSGEIAAAYA AGRLSHRMAL RVAFHRGFMA GVSKDRGLPP GAMLSIGLGQ GDAAPYLHDL
     THGEAVIACI NSPNSVTVSG DAAAVDEVMA RIIARGDGTF CRKLHVDTAY HSHHMRAVAD
     EYCIRLGDLD LGIDERISAP GGQRDKEEVK YFSSNSGLAW VSGFAASYWV DNLISPVRFS
     DAIQTVAREH HKHNGGLALF VEIGPHAALA GPIRQCLAAS NVPKLEYNYL SALKRGAGAV
     ETMLQVVGHL FERGVRVNFD EISALTPGFH TAAVRPDLPS YCWDYSSKHW HESRLSREYR
     MRREPYHHLL GVRMTELAST EPRWRHMVGL ATLPWLAHHI IDGLIIFPGA CYVCMVIEAV
     RQLAKEQYSD QALEAVSLRD VSFLRALVVP DAPSRVEMQL SLKHRADASP LGFTFSVTAL
     SDGKWHVFCT GVVEGVMTLD KPETEPVMLD PRPKQDWLNR TMVIPEELYN EMTADGNTYG
     PSFRGLSSLT MSTDGSMATA VIEVPDIAAS MPAQYQASHI LHPTTLDSMF HVGIPMMKRR
     HGAGSVMPVH IGELLISTQT PALNSQGSKL DVSAKLTSSH FRASNIDMTI VSGGFPVMYA
     SAIESRSLAA HVDGAHGTQD EHGICYELAW RCDLNFLRTS DLTRSSILAD LVSFLCFKTA
     HLSIAELGES PGVLAPAFLA AVGVHRGTVT SYDVVERGNQ PIDEGCKRLT GYPIRRRALD
     PDSSLESQGF APNTYDVVLA SDLGSLCYVS TLVKNDGVVV VVLKPGSDDN WQSTLRKTWP
     SHDIQLTVVD SVNGNRIILA RNDKTKDSHS SSRVHILTHS ALQTTPSWAT ALIGKLHEMG
     YEMSSGSLSQ DVIQRSSDAR NTCIMVIDDL AQPILSDRAC FNSAITLLRQ EHRIIWLSLD
     SPSSMHQITG VARTAHAEND NLRLTVVHAA LEAIGSPPLV DLLCHCLTYA QNRDSLAPYE
     REYRVSRDAA VLIPRLRSSD CLNRAIRASE KASEPSSNIE TEPHHYINTT RSLALGPVQS
     SKGDGDIVFI DSHTVELAEG QVEVETEAFV LSKSQNLTSS QLGEYSGIVR RVGKGVRDFS
     PGDAVVALAL DGVVGANHAR VPSSHVSRRP DSLSPAVAAA LFLPTIAASY AIHHLAQISK
     GKSIVLIHGV LTDIGRASVA VARVLGATIT ATAISRQEAL EITQQLNIQL ENIIVSRPSL
     LRPQLDELFQ LDAIIHISKD SVPVAAWSCL KPFGQVVVFN SSSSIAFPSP PPENATIHYC
     HITNLVQAQP DRLADLVSLA APALERIPFK GIDLCIQDVA QVPEAIRLVR QGGKVILQAS
     PSSLVRTVIP SSISMDWEAV DAAYVVAGGM GDLGRRLLLL MARRGAMHLV TLSRRSIEPE
     DHRSFQGQLQ LVQPGCRLYC LVCDITSESS VQNAADTLTR TGVPPVRGVI QSAVTLHDRT
     LETMTFDDFF AVAHAKVDGT LVLERVFASP HLHFFLMLSS AVNITGASGQ ANYNAGNAVQ
     DAIAHDRGPG FLSMNIGWIE DAINTSNNKT ILQGLWRTGL RPILGQELSR YFDHLLGAAS
     SHSRMRQAII GFNAASLSHT SASNSNVHSA MFCHIRGSLA AEESSSSTNN VRSFGEVVEG
     GDLDTIIDFI SSAITRRLMT LISMDDDQIK DRNGSILDLG LDSLVAIELR NWITREFKSP
     LQSSEILTDQ PIRDLAEKVA SRSSLLASGL DKEVPAGSLE NGDVEDRHSA GAIRPSTSAH
     STVKYVSENL PPLPLPPLAD TLRLFEDSRR AIDTANHRRN TSDAVHDFLK GPGPRLYNSL
     QETNSDVIAD AYDRQVYLER REPLPEQGPF IFIHSIQAPV HSQARRAAIL TIAAFDFIRL
     LARGDIATDT LHGEPITTEG RNWLFYATRR PGIGIDRMER HVPNNTVAVL RRGHVFQLRL
     PDVEQALDML AVTRVYDDIL AASCDAIPPI CTLTADERDS WALFRLDLER HPQNAAVLAC
     IDTAAFVMCL DDESPTSSGE RYTQFMINGA HRPFANRWLD KTLQFAVTAN GISAEIYEHS
     KLDGIDTNRL HAHIARAILA HPPSETADIS SFSSPYAVQE LMWEPSSATL QRIEHVRTQC
     QVYGPLDHQV FDVASLGLRS LRGFRLQPNA TAHLTVLLAL YLVDGEIRPA WEKVSLGTFA
     RGRVEWVQTI SPAARAFIEA AAASYTDSNN RTRVRALLHQ ATSTHSRSLV AAGRGLGAVR
     ALYALRGAAQ EQEKELPELF RTHSWDATRR GGPGQDVKLG FMRLAPDDDA NGNVGATPGD
     DDINGRWDEA GFLVCGERGV YVHCNVWEKH ARFAASGRPA YVTKLCKAMR RASCMITSLL
     EDPSKRPT
 
 
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