位置:首页 > 蛋白库 > EUPA_PHOSX
EUPA_PHOSX
ID   EUPA_PHOSX              Reviewed;        2682 AA.
AC   A0A4P8GHJ1;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-JUL-2019, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=3-methylorcinaldehyde synthase {ECO:0000303|PubMed:30980906};
DE            Short=MOS {ECO:0000303|PubMed:30980906};
DE            EC=2.3.1.- {ECO:0000305|PubMed:30980906};
DE   AltName: Full=Eupenifeldin biosynthesis cluster protein A {ECO:0000303|PubMed:30980906};
DE   AltName: Full=Non-reducing polyketide synthase eupA {ECO:0000303|PubMed:30980906};
DE            Short=NR-PKS eupA {ECO:0000303|PubMed:30980906};
GN   Name=eupA {ECO:0000303|PubMed:30980906}; ORFNames=gme12632;
OS   Phoma sp.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Phoma.
OX   NCBI_TaxID=1707701;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   PATHWAY.
RC   STRAIN=XZ068 / CGMCC No. 10481;
RX   PubMed=30980906; DOI=10.1016/j.fgb.2019.04.004;
RA   Zhai Y., Li Y., Zhang J., Zhang Y., Ren F., Zhang X., Liu G., Liu X.,
RA   Che Y.;
RT   "Identification of the gene cluster for bistropolone-humulene meroterpenoid
RT   biosynthesis in Phoma sp.";
RL   Fungal Genet. Biol. 129:7-15(2019).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=8360103; DOI=10.7164/antibiotics.46.1082;
RA   Mayerl F., Gao Q., Huang S., Klohr S.E., Matson J.A., Gustavson D.R.,
RA   Pirnik D.M., Berry R.L., Fairchild C., Rose W.C.;
RT   "Eupenifeldin, a novel cytotoxic bistropolone from Eupenicillium
RT   brefeldianum.";
RL   J. Antibiot. 46:1082-1088(1993).
RN   [3]
RP   BIOTECHNOLOGY.
RX   PubMed=18095654; DOI=10.1021/np070513k;
RA   Ayers S., Zink D.L., Powell J.S., Brown C.M., Grund A., Bills G.F.,
RA   Platas G., Thompson D., Singh S.B.;
RT   "Noreupenifeldin, a tropolone from an unidentified ascomycete.";
RL   J. Nat. Prod. 71:457-459(2008).
RN   [4]
RP   BIOTECHNOLOGY.
RX   DOI=10.1016/j.phytol.2008.09.008;
RA   Bunyapaiboonsri T., Veeranondha S., Boonruangprapa T., Somrithipol S.;
RT   "Ramiferin, a bisphenol-sesquiterpene from the fungus Kionochaeta ramifera
RT   BCC 7585.";
RL   Phytochem. Lett. 1:204-206(2008).
CC   -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC       that mediates the biosynthesis of eupenifeldin, a bistropolone
CC       meroterpenoid that acts as an antitumor agent (PubMed:30980906). The
CC       first step of eupenifeldin biosynthesis is the biosynthesis of 3-
CC       methylorcinaldehyde performed by the non-reducing polyketide synthase
CC       eupA (PubMed:30980906). Oxidative dearomatization of 3-
CC       methylorcinaldehyde likely catalyzed by the FAD-dependent monooxygenase
CC       eupB is followed by oxidative ring expansion by the 2-oxoglutarate-
CC       dependent dioxygenase eupC to provide the first tropolone metabolite,
CC       tropolone stipitaldehyde (Probable). In parallel, generation of
CC       sesquiterpene alpha-humulene from farnesylpyrophosphate (FPP) is
CC       catalyzed by the terpene cyclase eupE (PubMed:30980906). The cytochrome
CC       P450 monooxygenase eupD then hydroxylates humulene to humulenol
CC       (PubMed:30980906). The putative Diels-Alderase eupF probably catalyzes
CC       the formation of the tropolone-humulene skeleton by linking humulenol
CC       and the polyketide moiety (Probable). The short-chain
CC       dehydrogenase/reductase eupG and the flavin-dependent monooxygenase
CC       eupH are also essential for eupenifeldin biosynthesis and are likely
CC       the additional decorating enzymes of the tropolone-humulene skeleton to
CC       produce final eupenifeldin or derivatives (Probable).
CC       {ECO:0000269|PubMed:30980906, ECO:0000305|PubMed:30980906}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:30980906}.
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; an acyl-carrier protein (ACP) that serves
CC       as the tether of the growing and completed polyketide via its
CC       phosphopantetheinyl arm; a C-methylation (C-Met) domain; and a C-
CC       terminal reductase (R) domain (By similarity). Methylation occurs
CC       during the processive construction of the carbon backbone, directly
CC       after the second extension at the triketide stage (By similarity). The
CC       C-terminal R domain is involved in a reductive release mechanism,
CC       reducing the thiolester intermediate to the observed aldehyde and
CC       concomitantly releasing the free holo-ACP thiol (By similarity).
CC       {ECO:0000250|UniProtKB:A5PHD6, ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of eupenifeldin.
CC       {ECO:0000269|PubMed:30980906}.
CC   -!- BIOTECHNOLOGY: Eupenifeldin is a bistropolone-humulene meroterpenoid
CC       first discovered as an antitumor and anti-leukemia agent
CC       (PubMed:8360103). This metabolite shows also anthelmintic activity
CC       against the parasitic worm Hemonchus contortus, anti-malarial activity
CC       as well as antifungal activity (PubMed:18095654, Ref.4).
CC       {ECO:0000269|PubMed:18095654, ECO:0000269|PubMed:8360103,
CC       ECO:0000269|Ref.4}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MK400120; QCO93110.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4P8GHJ1; -.
DR   SMR; A0A4P8GHJ1; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.10.129.110; -; 1.
DR   Gene3D; 3.40.366.10; -; 2.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 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; IPR013120; Far_NAD-bd.
DR   InterPro; IPR041068; HTH_51.
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; IPR013217; Methyltransf_12.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR032088; SAT.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF18558; HTH_51; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   Pfam; PF16073; SAT; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW   Phosphopantetheine; Phosphoprotein; Transferase.
FT   CHAIN           1..2682
FT                   /note="3-methylorcinaldehyde synthase"
FT                   /id="PRO_0000449149"
FT   DOMAIN          1723..1797
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          111..272
FT                   /note="N-terminal acylcarrier protein transacylase domain
FT                   (SAT)"
FT                   /evidence="ECO:0000255"
FT   REGION          404..829
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          947..1237
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          1367..1649
FT                   /note="Product template (PT) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          2021..2211
FT                   /note="Methyltransferase domain"
FT                   /evidence="ECO:0000255"
FT   REGION          2303..2548
FT                   /note="NADPH-binding (R) domain"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        154
FT                   /note="Nucleophile; for transacylase activity"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0K0MCJ4"
FT   ACT_SITE        272
FT                   /note="Proton donor/acceptor; for transacylase activity"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0K0MCJ4"
FT   ACT_SITE        573
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         1757
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2682 AA;  295551 MW;  7ABE910BE4C84775 CRC64;
     MQTEEWKMAN QDNNKPQRDS ERCVFLFGSL SLSFDASAFA QVRKAIANDE RNSWLVNAAR
     QLPQDLETIL SGLPSLNNSN TRARKQLADL HNAIIGGRPL DTPFPLPNTV LIPLVVIEQL
     SQYADFARQK GVERSGTPDG WPAIEADTKS LGLCTGNLAA FATSSARSWG DFQKYGAAAV
     RLGLLVGLVI DSQDEAFDSR RWRSLSVAWS GSQGGEELQR ILPEFDETYV SVYYDACRST
     ITTPVSSLPT LVHRLKAAGL GVTEITLYGA FHSAARNSAV LEQLTVFCDS HADFQLSTSA
     ASVAALQAND NTDHKDIIRK QGALHAKALR RILVEPAQWF DALAAVLGEE GERARVVSFG
     SERSVPLSLA MRSNVRVVHA TDTHDGNRGT NADGGERMWA ESDIAVIGMA CKVAGAEGVE
     EFWELLVEGH SQHRDISASE RFSFDDTAFR TASDSNMQRK WYANLVDGHD QFDHRFFKKS
     ARESAAMDPQ QRQLLQVAYQ AAEQAGCFTR TNSVCDGNVG CFVGVCLSDY ESNVGCHPAN
     AFTATGNLQG FIAGKVSHFL GWTGPALTID TACSSSLVAV HQACASILAG ECNSALAGGT
     HIMTTAGWFQ NLAAGAFVSP TGQCKPFDAA ADGYCRGEGV GAVVLKKLSQ AIADGDRVLG
     VIGATAVQQN QNCTPIFVPN VPSLSALFTT VTAKAHVKPA SVSVVEAHGT GTAVGDPAEW
     ASIRQTLGGL NRPPERPLMV SSTKGLVGHL ECTSGIISLI KVLLMVQKRM LPPQASFDTL
     NPVLNAQPSD HMFVPRRAQP WDAEFRVALI NNYGASGSNA SMIVMQPPTF DTVAPIHLAA
     AVRSPDCRYP FWLSGLDSSS LRRRAKALRR FLSRGLGPAS SLAPSLASIS YNLAHQGDRA
     LDQRITFTAA SVTELDQHLA ACEDGSDNKP AAPASTAASK QTVVMCFGGQ VSTHIGLDPH
     VYNSVGLLRQ HLDNVDTIIQ SLGYTTIFPA IFQRVPLADT VHLQTMLFAM QFACAQAWID
     SGLRPTVLVG HSFGELTALC VSGALSLVDA VKMIARRAAI VRDAWGIDRG TMMAVEGDLY
     EVEQLLVDVN SSISPAVPIS IACYNGPRSF TLAGSTDTIN EVDARLCAQP GRSIKSRRLN
     VTNAFHSALV DPLLHRLEES CEDLTFRRPV LYLERALDST SSGPEWSARS VAEHMRNPVY
     FHHALQRIVQ IDPSSSFVFV EAGTNSSITA MTSRALDNKI IKGTSTFHGL SIANCDDGWN
     KLTDSIMSLW KAGLNVQHWA HHQRQRRYQA DIEPLLLPPY QFDPNARHWM DLKPLPRQLP
     ALIEEATKTE ADKKPEGLLT FVGFQDSSTQ MQAQFQINTN TEEYKSLLLG HMTIQTAPIC
     PATMQISFVI EAIVTIRHEL QTEQEPQIQD VQYRSPVCAN LSRKTWIEIK DENERGLAWR
     FEVFSTESHS GPRTIHTTGK IKFTNARDAT LQRQLMQFER LFGHHRATDL LKSAEVDEVL
     ANRSIYLIFS EIVDYGEEYR GLQKFASKGH ESAGHVVRRH SHDRKTPRFD AHLADTFCQL
     GGIWINCMTE RSQDDIYLAN SIDQWIRSPH NAGAAGSTVE PSKEYHVYAT HHRPSDKLSL
     TDVFVFDVKA GKLVEVILGI AYVKIPKLSM QKMLTRLTGS EWLNNTPATS MNQAPVSAPN
     PATRPSIVDL PSAVTQVPVL LPQGVKPSAE IRPSEPPSRS LLENITERVK AVVADLSGVE
     VTEIGDECDL ADLGIDSLAG MQMVHEIEGA LHVTLPEKEI LLVVTMRDLM KVVTGVVEVD
     FEATDSLSSD NDLPSIATSS EGERVATNLT TPAPQSDVDK DEHEAFESND LRLPAAVVLE
     AFKETRELTD EHVLGVGQAS YVSEALPLQT ELSISLTLEA FEALGAGLRN AGPGEQLFRI
     VHDEEHARFV DYMYDMLEIE TQIIKVDRGI ITRTAVPFPE RSSTVVYAEL RRRFPDQRAA
     DELTYYAGTH LMQVLSGETT GVKLIFGTTE GRELVSTFYG EWPLNQVMYT QMEDFFTRLA
     SKLPATNDNK PLRILEMGAG TGGTTKRLVP LLARLQIPVE YTFTDLAPSF VRAARNKWEK
     LYPWMRFRVH DIEKAPGEDL VNTQHFVLAS NAIHATRSIR ESTLNVRKFL RSDGYLLMGE
     MTRTPYWVDI IFGLFEGWWL FDDGRRHALT HESRWETDLQ SAGYGHVYWT EGTRPESEIE
     KLILAAASLT NLAGSDFVQS ERNPITKRHQ FDNEVSGGCA EREKLIMEYV CDSTQDFAKT
     FKVPMSSIPR SLHHKSKGKW IVVTGATGGL GAHLVAKAAV RSDVERVVCL NRRSKQNALE
     RQMHALRKQG ISLDSECLAK LDVHVTELAQ PSSLGLPNEL YNLLLDNVTH IVHNAWLMNS
     KWTVKRFEPQ IRIMKHMIHF ARDISLRHTE SDPVTFIFVS SIATVGFHPL LAKSPIVPED
     RVSIDSVLPT GYGEAKYICE RMLDTSLHRY PSRFRAAAVR LGQIAGSSLN GYWNPMEHVS
     FLIKSSQTLR ALPNLPGSLG WTPADAIADS LLDICTQPGD VALHPLYHID NPVRQNWDEM
     LAVLADVLNI SQGASGIVPF DEWLRRVRDW PHTEDNASDG KNPAYVLVDF LEDHFVRMSC
     GGLLLGTRKA REHSETLACV GPVDAQAIKL YVRSWKDMGF LD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024