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OTAA_ASPNC
ID   OTAA_ASPNC              Reviewed;        2550 AA.
AC   A2R6H1;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Highly reducing polyketide synthase otaA {ECO:0000303|PubMed:27959549};
DE            EC=2.3.1.- {ECO:0000269|PubMed:27959549};
DE   AltName: Full=Ochratoxin biosynthesis cluster protein 1 {ECO:0000303|PubMed:27667988};
DE   AltName: Full=Ochratoxin biosynthesis cluster protein A {ECO:0000303|PubMed:33391201};
GN   Name=otaA {ECO:0000303|PubMed:33391201};
GN   Synonyms=ota1 {ECO:0000303|PubMed:27667988}; ORFNames=An15g07920;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
RN   [2]
RP   IDENTIFICATION, AND DOMAIN.
RX   PubMed=22341916; DOI=10.1016/j.ijfoodmicro.2012.01.020;
RA   Ferracin L.M., Fier C.B., Vieira M.L., Monteiro-Vitorello C.B.,
RA   Varani A.M., Rossi M.M., Mueller-Santos M., Taniwaki M.H.,
RA   Thie Iamanaka B., Fungaro M.H.;
RT   "Strain-specific polyketide synthase genes of Aspergillus niger.";
RL   Int. J. Food Microbiol. 155:137-145(2012).
RN   [3]
RP   FUNCTION.
RX   PubMed=27667988; DOI=10.3389/fmicb.2016.01412;
RA   Susca A., Proctor R.H., Morelli M., Haidukowski M., Gallo A.,
RA   Logrieco A.F., Moretti A.;
RT   "Variation in fumonisin and ochratoxin production associated with
RT   differences in biosynthetic gene content in Aspergillus niger and A.
RT   welwitschiae isolates from multiple crop and geographic origins.";
RL   Front. Microbiol. 7:1412-1412(2016).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND PATHWAY.
RX   PubMed=27959549; DOI=10.1021/acs.jafc.6b03907;
RA   Zhang J., Zhu L., Chen H., Li M., Zhu X., Gao Q., Wang D., Zhang Y.;
RT   "A polyketide synthase encoded by the gene An15g07920 is involved in the
RT   biosynthesis of ochratoxin A in Aspergillus niger.";
RL   J. Agric. Food Chem. 64:9680-9688(2016).
RN   [5]
RP   NOMENCLATURE, AND FUNCTION.
RX   PubMed=33391201; DOI=10.3389/fmicb.2020.581309;
RA   Ferrara M., Gallo A., Perrone G., Magista D., Baker S.E.;
RT   "Comparative genomic analysis of ochratoxin A biosynthetic cluster in
RT   producing fungi: new evidence of a cyclase gene involvement.";
RL   Front. Microbiol. 11:581309-581309(2020).
RN   [6]
RP   INDUCTION.
RX   PubMed=35143724; DOI=10.1021/acs.jafc.1c08160;
RA   Zhang J., Li L., Yang Y., Zhao C., Hu J., Xue X., Gao Q., Wang D.,
RA   Zhuang Z., Zhang Y.;
RT   "Deletion and overexpression of the AnOTAbzip gene, a positive regulator of
RT   ochratoxin A biosynthesis in Aspergillus niger.";
RL   J. Agric. Food Chem. 70:2169-2178(2022).
CC   -!- FUNCTION: Highly reducing polyketide synthase; part of the gene cluster
CC       that mediates the biosynthesis of ochratoxin A (OTA), a mycotoxin
CC       composed of a chlorinated type I polyketide dihydroisocoumarin moiety
CC       linked to L-phenylalanine, and demonstrated to have nephrotoxic,
CC       immunotoxic, genotoxic, neurotoxic, and teratogenic properties
CC       (PubMed:27667988, PubMed:27959549). OtaA catalyzes the condensation of
CC       one acetate and 4 malonate units to form the isocoumarin group
CC       (PubMed:27959549). The pathway begins with the highly reducing
CC       polyketide synthase otaA that catalyzes the formation of the
CC       isocoumarin group during the initial stages of biosynthesis, starting
CC       from one acetate and 4 malonate units, to originate the characteristic
CC       pentaketide skeleton 7-methylmellein (7-MM) of the OTA molecule. The
CC       newly identified cyclase otaY might be involved in the polyketide
CC       cyclization reaction during the initial steps of the OTA biosynthesis.
CC       7-MM is then oxidized into 7-carboxymellein (also called ochratoxin
CC       beta) by the cytochrome P450 monooxygenase otaC. The NRPS encoded by
CC       the otaB gene is involved in the linking of phenylalanine to the
CC       dihydroisocoumarin ring. The reaction catalyzed by NRPS results in the
CC       production of ochratoxin B (OTB), which is the non-chlorinated analog
CC       of OTA and which subsequently serves as the substrate of the halogenase
CC       otaD for chlorination activity to form the final molecular structure of
CC       OTA, containing a chlorine atom in the C-5 position of the molecule
CC       (PubMed:27667988, PubMed:33391201) (Probable).
CC       {ECO:0000269|PubMed:27667988, ECO:0000269|PubMed:27959549,
CC       ECO:0000305|PubMed:27667988, ECO:0000305|PubMed:33391201}.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000255};
CC       Note=Binds 1 phosphopantetheine covalently. {ECO:0000255};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:27959549}.
CC   -!- INDUCTION: Expression reaches reached its maximum level before
CC       ochratoxin A accumulation reaches its highest level (PubMed:27959549).
CC       Expression is positively regulated by the ochratoxin cluster
CC       transcription factor otaR1, probably via its binding to the conserved
CC       5'-ACGT-3' bZIP binding motifs found in multiple copies (3 to 4) in the
CC       promoters of the OTA biosynthetic genes (PubMed:35143724).
CC       {ECO:0000269|PubMed:27959549, ECO:0000269|PubMed:35143724}.
CC   -!- DOMAIN: Multidomain protein; including a ketosynthase (KS) that
CC       catalyzes repeated decarboxylative condensation to elongate the
CC       polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects
CC       and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain
CC       that reduces hydroxyl groups to enoyl groups; a methyltransferase
CC       (CMeT) domain responsible for the incorporation of methyl groups; an
CC       enoylreductase (ER) domain that reduces enoyl groups to alkyl group; a
CC       ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and
CC       an acyl-carrier protein (ACP) that serves as the tether of the growing
CC       and completed polyketide via its phosphopantetheinyl arm.
CC       {ECO:0000305|PubMed:22341916}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the production of ochratoxin alpha,
CC       ochratoxin beta, and ochratoxin A (PubMed:27959549).
CC       {ECO:0000269|PubMed:27959549}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAK42679.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AM270352; CAK42679.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A2R6H1; -.
DR   SMR; A2R6H1; -.
DR   PaxDb; A2R6H1; -.
DR   EnsemblFungi; CAK42679; CAK42679; An15g07920.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   Proteomes; UP000006706; Chromosome 3R.
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:0016491; F:oxidoreductase 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:1900818; P:ochratoxin A biosynthetic process; IMP:GO_Central.
DR   GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.10.129.110; -; 1.
DR   Gene3D; 3.40.366.10; -; 1.
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; IPR011032; GroES-like_sf.
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; 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; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF00698; Acyl_transf_1; 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; 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; 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.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW   Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..2550
FT                   /note="Highly reducing polyketide synthase otaA"
FT                   /id="PRO_0000440589"
FT   DOMAIN          2454..2531
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          12..434
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:22341916"
FT   REGION          572..894
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:22341916"
FT   REGION          959..1252
FT                   /note="Dehydrogenase (DH) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:22341916"
FT   REGION          1433..1612
FT                   /note="Methyltransferase (CMeT) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:22341916"
FT   REGION          1859..1919
FT                   /note="Enoyl reductase (ER) (ER) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:22341916"
FT   REGION          2166..2345
FT                   /note="Ketoreductase (KR) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:22341916"
FT   ACT_SITE        182
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   BINDING         1420
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         1442
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   MOD_RES         2491
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2550 AA;  277318 MW;  F57292F2476EFE23 CRC64;
     MSSAPIPQSE PLAIIGLACK YANGIDSPEA LYEQVMAARC MHGAMPSNRM DASFYYHPTS
     EATGTSYSKG GYFLNCDLNA FDSPFFQLSE IDVMAMDPQQ KMLLENVYHA LENAGIPLKN
     AISSPTSVFV GCSNNDHLAL ANSDLLLSLK GKGTGTSPSI LANRVSWFYD FQGTSQTIDT
     ACSSSLVAFH QGCMDVRAGK SAMSIISGIN LIEHPGPTLY LSSLGVLSPD GKSMSFDARA
     NGYGRGEGVG TVIVKPLQAA LRDGNRIRAI VRSTGSNQDG RTPGITVPNP SAQERLIHDV
     YRVADLDPRR TGYVEAHGTG TQVGDPLEVQ AILAALGVAR DSPLYVGSVK SVLGHLEGGA
     GLAGLISATL AVESKMIPPV AGLQSLNPKI PQRDDLKFAR EATPWPRWDV RRASINSFGF
     GGTNAHAVVE DVEGFFADLF GQYIPGALPA PEVDTSLETT PMLSKPLMSG NASNQSVQSW
     STSRLFVISA FDEAGIQRNT SALAEYLDSK STTADTDGED RLLNNLCHTL NEKRTRFDWR
     SYHVADSIAS LRESLQHSRA IRQSSAPKPI RFVFTGQGAN WAGMACDMLK YPLFRRRIQE
     AAAYLRELGS GWDLFERMTS KAGELDEPTF AQSSCVAVQV ALVDLLASWK VVPETVVGHS
     SGEIAAAYCA GHISRQAAWK VAFCRGKVCA RRTDGQGRML AAAMPVHQLE RVVARVNKGQ
     PTSVKIGCYN SPRNLTLTGR YDDILRLKLE LDDVGALNRM LPVKVAYHSD YMQDAAPEYL
     SLLGEILDGG DTIHKDASIQ MISSVTGQPV PAGDVQQASY WVKNLVSPVR FCTALLASME
     FPGTTGKRED TLIEIGPHST LRSAIKESFA EVPEYQSVQY GSLLKRYETN GSTILHTLGM
     MFCSGHEISL AAINDRRVGT RKIPMLLTGL PGYAFDHSRS VRGTSRRIEQ VKFPTYNRHE
     LLGVPVEDSN PYEQRWRNVL RPDDLPWLRM NRMKGQIHFP GVAYILMATE ALQQRVARTM
     TIPRVRIANM SILAPLQVPD SPSGVEIQVS IYPTNVRANG ATDWATFRII SYDTAEKTWV
     EHCVGSVRAE TGPPDLCVNT ALRKQCAEPV DIAQMYHGFT AAGMDFGENL RNIQAMKVSP
     DRTACTATIT APSIAPQAHD QYPLHPCSFE SILHALLYLC EASQSPMVTN YIEEVVIVNP
     NDTGAREFES FARRQRTSAT TWTCDVSITT NVGDQDIQIK GLDLVQLPAN NDDAVDAESF
     YTVNWRPDVK LLASADALHN SAPVDAAQHL PTFDEHEGYQ LASAIFLQEA KEYVTRTGLP
     PLPTHHQAFM DWMEEEYQSI NNGTTPLLDK SLLDGIRADP DRRKSLLDRV ARQSARGELL
     VRVGTRMIDI LEQKIDCLEV MFGPDNLMER TYEEGLPGQI APAVAGYLHC LAHAQTGIKI
     LEVGAGTGSA TKVMLDSLRP TEAQDGGGLV SSVSSYDFTD ISAAFFEKAR ARFHDWADIL
     RPKLLNIEQD PAAQGFELGS YDLVIATHVL HATADLNVSL KNIRALLKEG GDLIVIENIQ
     PKFMCSQLPF GLLPGWWRSV EPYRKTNPLI LKEHWTEELQ NAGLRPRLII NDTDDGINEM
     SAFVASPMPK VLDGSQPCSI IYSSTYPGQQ QLALEVADRL PRSCTAAVVD LADISLDHSD
     TVGIVLVGCQ GLDLSELTSS EYDRVKFILT SFQKLLWVTC DPTDVPKSAL ATGLVRSTRW
     EREHDNVNII LLSVSLSRPT PLTISSEIVR LCENAFISCK RVPPNSEYRI EGSNGVLLTN
     RLFPAAGINE CIGLGSRPRS RQVPLGTVDH PIKLTSIGSQ QPNGFHFIED PQAHEPLDPD
     EVKIRIHAAG LDEEDADQLS RLIPGHGFGD QGSGTVVEIG HGVQGIQVGD QVMALRTGPS
     CALQTFFRTH SATVAKIPDG IRLSDAAALP LPWVTAYHSL VTVARLDSQE KVLIHPAIGA
     TGQAAVQVAS MLGATVYATV ETDAQRQTLA EYGVEESHIL DSASVEKQFG TQTSTQGVDV
     LLNLRRDGLE FLHLSCLSPF GRLVDISGSR AFPSQVNSPS NQSYYRVNMR ELSQLKPESI
     RQTLRTVAQL LASPTIRPVA PFRVGYSQLQ RVLSEIRRGS RGPWVIQPLP NDPIPPLGSH
     QFDPSASYLL IGGFGGLGRS VARWMHHRGA KHFIFFSRSG ASSAAARELC ADLRAAGCAV
     SDMICDTTDA QAVAKAMAQC EASMPPIRGC LQASMVLEDS MLSNMDHTRF LGAITPKVQG
     TINVASALAP IKSNLDFFVM LSSSAGIVGN RGQANYAAAN TFLDAFAGQL VTQGYPATSV
     SLGSVLSVGW VAENQHKLRI AFAFGALSED LLLSILEYHM DPAWGAAQSI QTCHTVVGVR
     SARDFQRQSI PLPGFMAHPL FSPLLAIAGR SQTAEQAAEA PVSQGLREAS SMEAAVEVVT
     RAIVHKLARI MALSVQEIDP QRSLGSYGVD SLVTVDLKAW FQREVGVSIG SGELLGEMAM
     TQLAQQAADA SQFLPAELRG KLRKNTDIHV
 
 
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