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Protein

Non-reducing polyketide synthase pks27

Gene

pks27

Organism
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Non-reducing polyketide synthase (NRPKS); part of the gene cluster 27 that mediates the biosynthesis of asparasone A, a sclerotium-specific anthraquinone pigment important for sclerotial survival (PubMed:24405210, PubMed:24412484). Catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules (PubMed:24405210). Through its product template (PT) domain, catalyzes the cyclization of polyketide backbone via C6-C11 aldolcondensation (By similarity).By similarity2 Publications

Cofactori

pantetheine 4'-phosphateBy similarityNote: Binds 1 phosphopantetheine covalently.Sequence analysis

Pathwayi: Secondary metabolite biosynthesis

This protein is involved in Secondary metabolite biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in Secondary metabolite biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei552PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Non-reducing polyketide synthase pks27Curated (EC:2.3.1.-1 Publication)
Short name:
NRPKSCurated
Alternative name(s):
Asparasone A synthesis protein pks27Curated
Cluster 27 polyketide synthase1 Publication
Gene namesi
Name:pks271 Publication
ORF Names:AFLA_082150
OrganismiAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Taxonomic identifieri332952 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000001875 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:AFLA_082150

Pathology & Biotechi

Disruption phenotypei

Impairs the production of asparasone A and causess the formation of greyish-yellow sclerotia rather than the dark brown sclerotia normally produced (PubMed:24405210, PubMed:24412484). Leads to a significant decrease of resistance to insect predation and increased susceptibility to the deleterious effects of ultraviolet light and heat (PubMed:24412484).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004361101 – 2045Non-reducing polyketide synthase pks27Add BLAST2045

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1672O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Expressioni

Inductioni

Expression is induced by the developmental and secondary metabolism regulator veA, as well as by the cluster 27 transcription factor znf27 (PubMed:24412484).1 Publication

Interactioni

Protein-protein interaction databases

STRINGi5059.CADAFLAP00000995

Structurei

3D structure databases

ProteinModelPortaliB8MYS6
SMRiB8MYS6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1635 – 1712CarrierPROSITE-ProRule annotationAdd BLAST78

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni10 – 247N-terminal acylcarrier protein transacylase domain (SAT)Sequence analysisAdd BLAST238
Regioni380 – 756Ketosynthase (KS) domainSequence analysisAdd BLAST377
Regioni913 – 1213Malonyl-CoA:ACP transacylase (MAT) domainSequence analysisAdd BLAST301
Regioni1640 – 1709Product template (PT) domainSequence analysisAdd BLAST70
Regioni1798 – 2039ThioesteraseSequence analysisAdd BLAST242

Domaini

Multidomain protein; including a starter unit:ACP transacylase (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm.By similarity

Phylogenomic databases

HOGENOMiHOG000168774
OMAiYAEMALV
OrthoDBiEOG092C01EM

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR001227 Ac_transferase_dom_sf
IPR036736 ACP-like_sf
IPR014043 Acyl_transferase
IPR016035 Acyl_Trfase/lysoPLipase
IPR032821 KAsynt_C_assoc
IPR018201 Ketoacyl_synth_AS
IPR014031 Ketoacyl_synth_C
IPR014030 Ketoacyl_synth_N
IPR016036 Malonyl_transacylase_ACP-bd
IPR020801 PKS_acyl_transferase
IPR020841 PKS_Beta-ketoAc_synthase_dom
IPR020807 PKS_dehydratase
IPR020806 PKS_PP-bd
IPR009081 PP-bd_ACP
IPR030918 PT_fungal_PKS
IPR032088 SAT
IPR001031 Thioesterase
IPR016039 Thiolase-like
PfamiView protein in Pfam
PF00698 Acyl_transf_1, 1 hit
PF16197 KAsynt_C_assoc, 1 hit
PF00109 ketoacyl-synt, 1 hit
PF02801 Ketoacyl-synt_C, 1 hit
PF00550 PP-binding, 1 hit
PF14765 PS-DH, 1 hit
PF16073 SAT, 1 hit
PF00975 Thioesterase, 1 hit
SMARTiView protein in SMART
SM00827 PKS_AT, 1 hit
SM00825 PKS_KS, 1 hit
SM00823 PKS_PP, 1 hit
SUPFAMiSSF47336 SSF47336, 1 hit
SSF52151 SSF52151, 2 hits
SSF53474 SSF53474, 1 hit
SSF53901 SSF53901, 1 hit
SSF55048 SSF55048, 1 hit
TIGRFAMsiTIGR04532 PT_fungal_PKS, 1 hit
PROSITEiView protein in PROSITE
PS00606 B_KETOACYL_SYNTHASE, 1 hit
PS50075 CARRIER, 1 hit

Sequencei

Sequence statusi: Complete.

B8MYS6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVEERKQTI VFGDLTCDSV AGLRTLVTVK DNPLLISFFE RVTTGLREEI
60 70 80 90 100
GLLPFSQRQR FIRFTTFEEL LARVQRSTCP HPALEKALAC TYQLACFIRQ
110 120 130 140 150
YTSPGHKYPS TQQTCLVGLC TGLLSAAAVG CCQSITDLLP LATHTVLIAF
160 170 180 190 200
RAGLFVADVR DRLEPQTGAP LAWSVLIPGL DGDTASLTLQ KYNEEKGLPA
210 220 230 240 250
TSAPYISTYA NTGVTLSGLP SALNDLLDSS CLPKNRALTI PIYAPYHASH
260 270 280 290 300
LYGQKDIESI LRKASATEFA SYQCQFSILS SITGQSIQVD TFGALIDYAL
310 320 330 340 350
NAILREPLRL DRIVSSLGEA LLSDSPIRGC TIFPIATVIG QSLAAALRKH
360 370 380 390 400
GAPDITVDPC MNSSIAVRDD RTSTTGHLGH SKLAIIGYSG RFPDANNNEE
410 420 430 440 450
LWQLLHEGRD VASITPSNRW DVKTHVDPTL KKKNTMGTPY GCWLKEPGLF
460 470 480 490 500
DAKFFALSPR EAPQVDPAQR LALMTAYEAM EFAGLVPDST PSSQSDRIGV
510 520 530 540 550
FYGTTSNDWG ETNSSQNVDT YYIPGSCRAF IPGRQNFFYK FSGPSYSVDT
560 570 580 590 600
ACSSGLAALH LACNSLLKGD IDTAICGGTN VLTNPDITAG LDRGHFLSRT
610 620 630 640 650
GNCKTFDDDA DGYCRGEGVC TMVIKRLEDA KADNDPIIAV ILGAYTNHSA
660 670 680 690 700
EAESITRPHI GAQKAIFEKV LTSAGVDPYS VGYVEMHGTG TQAGDAREMK
710 720 730 740 750
SVLSVFAPET ERPRTDAERL FLGSAKANVG HGESVSGPIA LIKSLMMLER
760 770 780 790 800
NEIPPHCGIK TKINSGFPTD LMDRNVHIAK QPIPWERPEG GVRRIMINNF
810 820 830 840 850
SAAGGNSSVL IEDAPVFEPK SKEAEPRSTH VVAVSAKSST ALIANIKSLL
860 870 880 890 900
SYMNATKPEL PSLSYTTTAR RTHHPFRVMV SGPDLPEIHA LLENKLASPT
910 920 930 940 950
VQNRARAAQR AAFAFTGQGS QYIGMGESLL NFSTFRSDIE RFNGIAETLG
960 970 980 990 1000
FPSFLPLLES GNGDISELPP LVVQVGTVCT QIAMARLWRS WGIEPCAVVG
1010 1020 1030 1040 1050
HSLGEYAALN IAGVLSEADT IFLAGKRAQL LQEDISANTH AMLAIGTSVE
1060 1070 1080 1090 1100
ETRSLCDGLE YDIACINTPK ETVLSGTNKQ IDRILDILSS TSLKKTRLRV
1110 1120 1130 1140 1150
PFAFHSSQME PVLEKFKAAA RGVKFYEPKV PVISPLFGEV LTSKEPFGPE
1160 1170 1180 1190 1200
YLARHCRETV NFATALESAK ADGVISSALW VEIGAHPIVS GLLRNNLDST
1210 1220 1230 1240 1250
LKTVPTLQRN KDTWKVLTSS LSTLYESGVD IRWSEYHRDF IPGLSVLRLP
1260 1270 1280 1290 1300
SYNWDLKEYW MQYVNDWSLY KGDAQFLKGT PGLSTTCVHK LVEEKKDGNK
1310 1320 1330 1340 1350
ITVVGEVDVL RDDVDPFVRG HRVNNLPLVT PSVYAEMALV IGEYLRKQQT
1360 1370 1380 1390 1400
KLSGTLVDLQ HMDVQRPFAT KSKGKGPQLL QCHVVLDCET FQGSVEFWSV
1410 1420 1430 1440 1450
TPEGKKLVRH ALASITFPDA KAAQEEVQQR AQGIMKEMDD MAARLNTDDR
1460 1470 1480 1490 1500
VQKFTGKTGY NLVSSLASYD PEYMGVSSVL LDSGRLEAVA TVKFNNPRTD
1510 1520 1530 1540 1550
GVYHVNPYLI DNLGQPALFV MNANDQADLS KEVFVNHGWK SLHFYKPLSI
1560 1570 1580 1590 1600
QKTYRSHVRM SGPDADGLYG GDMVVFEDKE VVAVYKGIKA QGVPRRLMDY
1610 1620 1630 1640 1650
IVHMRDDTKA GAPAGGTLNA SQSAAANPAA DPSAQADSDN WQAALKIISE
1660 1670 1680 1690 1700
ESGVPIAELS PEAAFDDLGV DSLLALLCAS RFREELGLHY ESSIFLDHPT
1710 1720 1730 1740 1750
IKELEAFWKQ GAPETGAVTV SGRDAVLNSM FTEAEAEVDQ DKNSSDEDRS
1760 1770 1780 1790 1800
SLGTSSYEVI SPNTTETTPE ITKTSSPKIS ATSLLLQGNP ALPSTVKTLF
1810 1820 1830 1840 1850
LLPDGSGSCS SYAGLPRIHP SIAVVGVNCP FMKTPESYTC GIDEVTQMYI
1860 1870 1880 1890 1900
TEIRRRQPHG PYALGGWSVG GIFSYHIAQQ LAAQGEQVSE LILIDCPVPK
1910 1920 1930 1940 1950
GLDHLPRRYY EYCDTIGLLG DVNGVKRDPP PWLISHFEAC VNSLHTYHAT
1960 1970 1980 1990 2000
PFRPNNAPRT QIIWACDAID KHCEPKFDRR PDDPEGLKFL TSTRTDFGPC
2010 2020 2030 2040
GWETLLPEED MTLDRMTGAN HFSMMKGEFA KRLSEMIEGF LMIGN
Length:2,045
Mass (Da):223,487
Last modified:March 3, 2009 - v1
Checksum:i93638F36620BFC7B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ963472 Genomic DNA Translation: EED57518.1
RefSeqiXP_002373130.1, XM_002373089.1

Genome annotation databases

EnsemblFungiiEED57518; EED57518; AFLA_082150
GeneIDi7917173
KEGGiafv:AFLA_082150

Similar proteinsi

Entry informationi

Entry nameiPKS27_ASPFN
AccessioniPrimary (citable) accession number: B8MYS6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 11, 2016
Last sequence update: March 3, 2009
Last modified: February 28, 2018
This is version 57 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways

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