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ARMB_ARMOS
ID   ARMB_ARMOS              Reviewed;        2210 AA.
AC   A0A284RE13;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2017, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Orsellinic acid synthase ArmB {ECO:0000250|UniProtKB:I3ZNU9};
DE            Short=OAS {ECO:0000250|UniProtKB:I3ZNU9};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:I3ZNU9};
DE   AltName: Full=Melledonol synthase {ECO:0000250|UniProtKB:I3ZNU9};
DE   AltName: Full=Melleolides biosynthesis cluster protein armB {ECO:0000250|UniProtKB:I3ZNU9};
DE   AltName: Full=Non-reducing polyketide synthase ArmB {ECO:0000250|UniProtKB:I3ZNU9};
GN   Name=armB {ECO:0000250|UniProtKB:I3ZNU9}; ORFNames=ARMOST_10343;
OS   Armillaria ostoyae (Armillaria root rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Physalacriaceae; Armillaria.
OX   NCBI_TaxID=47428;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C18/9;
RX   PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA   Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA   Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA   Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA   Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA   Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA   Gueldener U., Muensterkoetter M., Nagy L.G.;
RT   "Genome expansion and lineage-specific genetic innovations in the forest
RT   pathogenic fungi Armillaria.";
RL   Nat. Ecol. Evol. 1:1931-1941(2017).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=21376582; DOI=10.1016/j.bmcl.2011.02.026;
RA   Bohnert M., Miethbauer S., Dahse H.M., Ziemen J., Nett M., Hoffmeister D.;
RT   "In vitro cytotoxicity of melleolide antibiotics: structural and
RT   mechanistic aspects.";
RL   Bioorg. Med. Chem. Lett. 21:2003-2006(2011).
RN   [3]
RP   BIOTECHNOLOGY.
RX   PubMed=23864890; DOI=10.1155/2013/459271;
RA   Chi C.W., Chen C.C., Chen Y.J.;
RT   "Therapeutic and radiosensitizing effects of armillaridin on human
RT   esophageal cancer cells.";
RL   Evid. Based Complement Alternat. Med. 2013:459271-459271(2013).
RN   [4]
RP   BIOTECHNOLOGY.
RX   PubMed=25746621; DOI=10.1615/intjmedmushrooms.v17.i2.70;
RA   Liu T.P., Chen C.C., Shiao P.Y., Shieh H.R., Chen Y.Y., Chen Y.J.;
RT   "Armillaridin, a honey medicinal mushroom, Armillaria mellea (higher
RT   basidiomycetes) component, inhibits differentiation and activation of human
RT   macrophages.";
RL   Int. J. Med. Mushrooms 17:161-168(2015).
RN   [5]
RP   BIOTECHNOLOGY.
RX   PubMed=26952552; DOI=10.1016/j.jep.2016.02.044;
RA   Li Z., Wang Y., Jiang B., Li W., Zheng L., Yang X., Bao Y., Sun L.,
RA   Huang Y., Li Y.;
RT   "Structure, cytotoxic activity and mechanism of protoilludane sesquiterpene
RT   aryl esters from the mycelium of Armillaria mellea.";
RL   J. Ethnopharmacol. 184:119-127(2016).
RN   [6]
RP   BIOTECHNOLOGY.
RX   PubMed=27592257; DOI=10.1007/s13277-016-5208-6;
RA   Chang W.H., Huang H.L., Huang W.P., Chen C.C., Chen Y.J.;
RT   "Armillaridin induces autophagy-associated cell death in human chronic
RT   myelogenous leukemia K562 cells.";
RL   Tumor Biol. 37:14291-14300(2016).
RN   [7]
RP   MISCELLANEOUS.
RX   PubMed=29614282; DOI=10.1016/j.cub.2018.01.026;
RA   Sipos G., Anderson J.B., Nagy L.G.;
RT   "Armillaria.";
RL   Curr. Biol. 28:R297-R298(2018).
RN   [8]
RP   BIOTECHNOLOGY.
RX   PubMed=31488037; DOI=10.1142/s0192415x19500708;
RA   Leu Y.S., Chen Y.J., Chen C.C., Huang H.L.;
RT   "Induction of autophagic death of human hepatocellular carcinoma cells by
RT   armillaridin from Armillaria mellea.";
RL   Am. J. Chin. Med. 47:1365-1380(2019).
RN   [9]
RP   MISCELLANEOUS.
RX   PubMed=31746694; DOI=10.1094/pdis-06-19-1147-re;
RA   Cromey M.G., Drakulic J., Beal E.J., Waghorn I.A.G., Perry J.N.,
RA   Clover G.R.G.;
RT   "Susceptibility of garden trees and shrubs to Armillaria root rot.";
RL   Plant Dis. 104:483-492(2020).
CC   -!- FUNCTION: Non-reducing polyketide synthase, part of the gene cluster
CC       that mediates the biosynthesis of melleolides, a range of antifungal
CC       and phytotoxic polyketide derivatives composed of an orsellinic acid
CC       (OA) moiety esterified to various sesquiterpene alcohols (By
CC       similarity). The first step in melleolides biosynthesis is performed by
CC       the delta(6)-protoilludene synthase PRO1 which catalyzes the
CC       cyclization of farnesyl diphosphate to protoilludene (By similarity).
CC       The orsellinic acid synthase armB produces OA by condensing acetyl-CoA
CC       with 3 malonyl-CoA units in a three-round chain elongation reaction
CC       folowed by a C2-C7 ring closure (By similarity). ArmB further catalyzes
CC       the trans-esterification of OA to the various sesquiterpene alcohols
CC       resulting from the hydroxylation of protoilludene (By similarity). The
CC       melleolides cluster also includes 5 cytochrome P450 monooxygenases, 4
CC       NAD(+)-dependent oxidoreductases, one flavin-dependent oxidoreductase,
CC       and one O-methyltransferase (By similarity). The cytochrome P450
CC       monooxygenases may be involved in protoilludene hydroxylation to
CC       elaborate melleolides with multiple alcohol groups, such as melleolide
CC       D, which carries alcohol functionalities at C-4, C-5, C-10, and C-13
CC       (By similarity). The role of the NAD(+)-dependent enzymes remains
CC       unknown (By similarity). Numerous melleolides, including arnamial, show
CC       5'-O-methylation of the aromatic moiety which may be catalyzed by the
CC       methyltransferase encoded in the cluster (By similarity). The flavin-
CC       dependent oxidoreductase might represent the dehydrogenase yielding the
CC       aldehyde in position 1 of arnamial and other melleolides (By
CC       similarity). Finally, several halogenase localized outside of the
CC       cluster (armH1 to armH5), are able to catalyze the transfer of a single
CC       chlorine atom to the melleolide backbone, resulting in a 6'-
CC       chloromelleolide product (By similarity).
CC       {ECO:0000250|UniProtKB:I3ZNU9, ECO:0000250|UniProtKB:P0DL13}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000250|UniProtKB:I3ZNU9}.
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:0000250|UniProtKB:I3ZNU9}.
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, which accepts the sesquiterpene
CC       alcohols as substrate to offload the finished ketide from the PKS
CC       assembly line. {ECO:0000250|UniProtKB:I3ZNU9}.
CC   -!- BIOTECHNOLOGY: Melleolide sesquiterpene aryl esters are cytotoxic
CC       secondary products with anti-cancer potential (PubMed:21376582,
CC       PubMed:26952552). Armillaridin shows therapeutic and radiosensitizing
CC       effects on human esophageal cancer cells (PubMed:23864890).
CC       Armillaridin induces autophagy-associated cell death in human chronic
CC       myelogenous leukemia as well as of hepatocellular carcinoma cells
CC       (PubMed:27592257, PubMed:31488037). Armillaridin can also inhibit the
CC       differentiation and activation of human macrophages and thus might have
CC       potential to be developed as a biological response modifier for
CC       inflammatory diseases (PubMed:25746621). {ECO:0000269|PubMed:21376582,
CC       ECO:0000269|PubMed:23864890, ECO:0000269|PubMed:25746621,
CC       ECO:0000269|PubMed:26952552, ECO:0000269|PubMed:27592257,
CC       ECO:0000269|PubMed:31488037}.
CC   -!- MISCELLANEOUS: Armillaria species are both devastating forest pathogens
CC       and some of the largest and oldest terrestrial organisms on Earth
CC       (PubMed:31746694) (Probable). They forage for hosts and achieve immense
CC       colony sizes via rhizomorphs, root-like multicellular structures of
CC       clonal dispersal (Probable). An A.ostoyae colony, known as the
CC       'humongous fungus' in the Malheur National Forest in the Strawberry
CC       Mountains of eastern Oregon, was found to be the largest fungal colony
CC       in the world, spanning an area of 9.1 square kilometers (Probable).
CC       This organism is estimated to be some 8,000 years old and may weigh as
CC       much as 35,000 tons (Probable). {ECO:0000269|PubMed:31746694,
CC       ECO:0000305, ECO:0000305|PubMed:29614282}.
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DR   EMBL; FUEG01000007; SJL07001.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A284RE13; -.
DR   SMR; A0A284RE13; -.
DR   STRING; 47428.A0A284RE13; -.
DR   OMA; PETFGCY; -.
DR   OrthoDB; 68112at2759; -.
DR   Proteomes; UP000219338; 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; -; 3.
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; IPR020802; PKS_thioesterase.
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   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF47336; SSF47336; 2.
DR   SUPFAM; SSF52151; SSF52151; 2.
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; 2.
PE   1: Evidence at protein level;
KW   Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase;
KW   Virulence.
FT   CHAIN           1..2210
FT                   /note="Orsellinic acid synthase ArmB"
FT                   /id="PRO_0000449402"
FT   DOMAIN          1660..1735
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1845..1922
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          38..261
FT                   /note="N-terminal acylcarrier protein transacylase domain
FT                   (SAT)"
FT                   /evidence="ECO:0000255"
FT   REGION          394..820
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          915..1240
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          1336..1611
FT                   /note="Product template (PT) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          1739..1761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1920..1946
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1963..2202
FT                   /note="Thioesterase (TE) domain"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1925..1946
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        561
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        1009
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000250|UniProtKB:J4UHQ6"
FT   MOD_RES         1694
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1882
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2210 AA;  237469 MW;  26ECB4E359B5D3F8 CRC64;
     MSPSLVVPVF AGHGTTAINS TSLRERAAAD ASSPSGALLL DACHYAFNVE LSTLSPSEAL
     AVGINPDHFT DPKSLLLLPS HEHYLTNSVV TAATLFLVQT LRYLASVQAS SSTSFASSLQ
     TNSEHGLGIV GFSSGILPAC VAGSSATTLE FISNAVETFR LAFWIGVRLQ IHKASVQTPE
     LLGESPLPWS LAFLGMSHAA AESAIQSFLK SFEGTPELRV TSVVSETSVT ISGRPDILAA
     FAAQLPLSGP VHKTTVDALY HSSSHHDGVR SQVLADVIRR NIRFPTHADI KVPVRSTYSG
     ELLSKGSEGS ASFVEQVVDM ILTQPVNWDK VTEALVRATP EGTVVHLLNF GPGAGLTKGI
     ERYFPSNKVS STDLSSEPVH TSTLQMPSSV QEPIAICGMS VNMPGAPSVA KLWEVLEKGI
     NTVSEVPEHR FKVSDYNDPK KKGRTMGAHT GNFIDEPDAF DNKFFNISPR EARSMDPQQR
     VLLHTAYEAL EDAGYVPNST PTNNPETFGC YVGVATNDYV QNLRNDIDVY YSTGTLRAFL
     SGRISYALQF SGPSIVVDTA CSSSLIAVYQ ACRALMNRDC NAAVAGGVNV ISSPDMFLGL
     DRGHFLSPTG QCKAFDASAD GYSRSEGCGI FVLKRLSDAV TENDQILGVI RGVEVNQSGN
     AYSITRPHAP TQENLFTQAL ERSGLDASRI SVVEAHGTGT QAGDPIELES IRGIFAKHRK
     ANNPLHITSV KANIGHLEAA SGAAALAKLL LMLRHRTIPR LVSLKNLNPR IKPLASDNVI
     IDTKQVAWTV PDESLPRVAL LNNFGAAGSN GALLLEEYIP KSSGKDTDVA STFIVGLSAK
     NEQVLVDLRA SYIEYLRSPA SAGVTLADIA YTATARRRIF SHRFAVTARS KEELTHKLEL
     ASGKTVSDNA PGKVVFVFSG QGGQYLGMGS ALYKTSALFK NAIDECEYFL KKNNFPGVLP
     IITSDGESSG LTPVEEFEAN QAAIFALEYG LAKLWMSWGV TPTAVVGHSL GEYAAHVITG
     VLSLESALTL VAHRVRIMMR TCELDTTGMI AINLGSGAVT DILSSSPDFS GISIACYNSA
     TDCVASGPIG QLDALKAHLD KAVHCKSVRL KVPFGYHSSA MQPLLEEFGA LAKRVTVHAP
     KIPVISNPLG RVIREGDKST FNAEYYLSHC ADPVQFESGI SALIDDASFA DIAAWIELGP
     HPTTLPMLTV HRGVSKEALL VGSLKKRQDD GLTLSSSLSQ LYTSNVPVRW RDVFADVSAA
     CVSLPSYPWQ KSKFWVAWKE DSPAPASSTE GSPASTKAFN PVNDFGMLQS WAQFPSAANS
     QIAIFETPIS LLKTSITGHI VGDVPLCPAS VYHELALAGI EASKAHLSLP LQGSHSALFN
     IDYVKPLVYS KDVARVIKTT IAMNTDGSGS FTVESYADSE AESVHCSGQF RPLLVVDTTT
     KFNRMAPVVS RRTAAICSGE DGEAEVFTTR TAYEIIFTRV VRYAKEYHTM KNVTISKNGM
     EGYAVVKLPK DHDKSKFVVH PVFMDTMLHV AGFLANMQGG DNDAYICSKV KSVKAVPSLI
     NNDATYGVFV VNAWVESEGM MLSDAIAVDI SGHGQIVAQL KGMCFKKLRL NTLQRSLAMH
     AGHTAPAPAQ KRSVAAAPKP KITEVAPALE PRSSPAKRSV DVQNTVLNIV GDTCGIEISA
     LDVNADLETY GVDSLMSIEI LRKFEESFPQ MQFDATIFST CNNITELVRE ISSTVGSQAA
     TAVNTPETAS TPEPTLQGDA SQSTDVRSIL LELISSFTGF EISNFDLNAD ADTAYGLDKF
     LFIPLFSKLQ TFFPDITLDP TKPSVCSTIG ELLDEVTAQV QAGPSSPSSD LVDTKPMFVS
     VLGLDESDIQ DDTEFETIGL DSLTAIEALH AIQTEYGLEL PSNLFELHTT AKAVNQYISS
     KRPGKSPKQV EETAMDPDRE EDLSDLTPEQ VQSVVRVLRL DEVPMSVQKS SSSGSPLFLF
     HDGSGAVNYL RRLGSVDREF WGFNNPNYAT GKPWGSVEAM ASAYADYAVK VAGSRPVIFG
     GWSFGGVVGF EAARQLMRRG VPVKGVVLID SPFPVDHVPS SNEFMAVTAG AFTRGGRTPI
     GRMMWKQLQQ NAPLLKTYDP RIAGGPYPPL VLLHNKEGIP PDAFLPYPVP RWMSEKGTDP
     CLLADDWSGL VGAPIKVIHL PGTHFTTFAT PHLGAVTQAL VDGCAYLDGL
 
 
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