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Protein

Noranthrone synthase

Gene

pksL1

Organism
Aspergillus parasiticus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor norsolorinic acid anthrone (noranthrone) in the aflatoxin biosynthesis pathway. The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by a dedicated fungal fatty acid synthase.2 Publications

Catalytic activityi

7 malonyl-CoA + hexanoyl-[acyl-carrier protein] = 7 CoA + norsolorinate anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O.1 Publication

Cofactori

pantetheine 4'-phosphateNote: Binds 1 phosphopantetheine covalently.

Pathwayi: aflatoxin biosynthesis

This protein is involved in the pathway aflatoxin biosynthesis, which is part of Mycotoxin biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway aflatoxin biosynthesis and in Mycotoxin biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei543 – 5431For beta-ketoacyl synthase activityBy similarity
Active sitei993 – 9931For acyl/malonyl transferase activityBy similarity
Active sitei1937 – 19371For thioesterase activity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.1.221. 523.
UniPathwayiUPA00287.

Protein family/group databases

ESTHERiaspor-PKSL1. Thioesterase.

Names & Taxonomyi

Protein namesi
Recommended name:
Noranthrone synthase (EC:2.3.1.221)
Alternative name(s):
Aflatoxin biosynthesis polyketide synthase
Short name:
PKS
Aflatoxin biosynthesis protein C
Polyketide synthase A
Gene namesi
Name:pksL1
Synonyms:aflC, pksA
OrganismiAspergillus parasiticus
Taxonomic identifieri5067 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1345 – 13451H → A: Abolishes catalytic activity. 1 Publication
Mutagenesisi1491 – 14911G → L: Abolishes catalytic activity. 1 Publication
Mutagenesisi1543 – 15431D → A: Abolishes catalytic activity. 1 Publication
Mutagenesisi1546 – 15461T → A: 40% decrease in catalytic activity. 1 Publication
Mutagenesisi1547 – 15471Q → A: Abolishes catalytic activity. 1 Publication
Mutagenesisi1554 – 15541N → A: Abolishes catalytic activity. 1 Publication
Mutagenesisi1937 – 19371S → A: Abolishes hydrolytic activity. 1 Publication
Mutagenesisi1964 – 19641D → N: Abolishes hydrolytic activity. 1 Publication
Mutagenesisi2070 – 20701D → N: Slight reduction in hydrolytic activity. 1 Publication
Mutagenesisi2088 – 20881H → F: Abolishes hydrolytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21092109Noranthrone synthasePRO_0000180303Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1746 – 17461O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1 Publication

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Protein-protein interaction databases

DIPiDIP-59286N.

Structurei

Secondary structure

1
2109
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1314 – 13218Combined sources
Beta strandi1324 – 13329Combined sources
Turni1336 – 13383Combined sources
Helixi1339 – 13424Combined sources
Beta strandi1345 – 13473Combined sources
Beta strandi1350 – 13523Combined sources
Helixi1355 – 137218Combined sources
Beta strandi1386 – 13949Combined sources
Beta strandi1407 – 14159Combined sources
Helixi1421 – 14233Combined sources
Beta strandi1426 – 14349Combined sources
Beta strandi1442 – 145211Combined sources
Helixi1455 – 14628Combined sources
Helixi1464 – 147916Combined sources
Beta strandi1483 – 14875Combined sources
Helixi1488 – 14958Combined sources
Turni1496 – 14983Combined sources
Helixi1503 – 15053Combined sources
Beta strandi1508 – 15147Combined sources
Helixi1515 – 15173Combined sources
Beta strandi1519 – 15257Combined sources
Helixi1526 – 15283Combined sources
Helixi1539 – 155416Combined sources
Turni1561 – 15633Combined sources
Beta strandi1564 – 157613Combined sources
Beta strandi1585 – 15917Combined sources
Beta strandi1600 – 160910Combined sources
Beta strandi1612 – 162615Combined sources
Helixi1627 – 16359Combined sources
Helixi1712 – 172615Combined sources
Helixi1730 – 17323Combined sources
Helixi1739 – 17424Combined sources
Helixi1746 – 175813Combined sources
Turni1770 – 17723Combined sources
Helixi1777 – 17859Combined sources
Beta strandi1853 – 18597Combined sources
Turni1861 – 18633Combined sources
Beta strandi1864 – 18718Combined sources
Helixi1878 – 18814Combined sources
Beta strandi1888 – 189710Combined sources
Turni1899 – 19024Combined sources
Helixi1904 – 19063Combined sources
Helixi1911 – 192515Combined sources
Beta strandi1931 – 19366Combined sources
Helixi1938 – 195215Combined sources
Beta strandi1957 – 19648Combined sources
Helixi1976 – 19849Combined sources
Turni1985 – 19906Combined sources
Beta strandi1991 – 19944Combined sources
Beta strandi1996 – 19983Combined sources
Helixi2006 – 201611Combined sources
Turni2017 – 20193Combined sources
Beta strandi2032 – 20409Combined sources
Turni2045 – 20473Combined sources
Turni2056 – 20583Combined sources
Helixi2069 – 20724Combined sources
Beta strandi2078 – 208710Combined sources
Helixi2090 – 20923Combined sources
Turni2094 – 20974Combined sources
Helixi2098 – 210710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KR5NMR-A1705-1791[»]
3HRQX-ray1.80A/B1305-1660[»]
3HRRX-ray1.90A/B1305-1660[»]
3ILSX-ray1.70A1845-2109[»]
ProteinModelPortaliQ12053.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12053.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1714 – 178572Acyl carrierPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 374374Starter unit:ACP transacylase (SAT)Add
BLAST
Regioni374 – 805432Beta-ketoacyl synthase (KS)Add
BLAST
Regioni903 – 1205303Malonyl-CoA:ACP transacylase (MAT)Add
BLAST
Regioni1206 – 1713508Product template (PT)Add
BLAST
Regioni1867 – 2102236Thioesterase/Claisen cyclase (TE/CLC)Add
BLAST

Domaini

The domain architecture includes starter unit:ACP transacylase (SAT), beta-ketoacyl synthase (KS), malonyl-CoA:ACP transacylase (MAT), product template (PT), acyl-carrier domain (ACP), and thioesterase/Claisen cyclase (TE/CLC) domains. The SAT domain receives a C6-fatty acid starter unit and transfers it onto the ACP for chain elongation. The KS accepts the hexanoyl-ACP unit and subsequent malonate extender units are loaded onto the ACP from the MAT domain for chain extension to generate the linear poly-beta-keto ACP-bound intermediate. The linear intermediate is then cyclized and aromatized in the PT domain. The resulting bicyclic intermediate is ultimately transferred from the ACP to the TE/CLC domain and undergoes Claisen-type C-C bond cyclization to release the product norsolorinic acid anthrone (noranthrone), which spontaneously oxidizes in vitro to norsolorinic acid (PubMed:18403714, PubMed:19847268, PubMed:20332208).3 Publications

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 2 hits.
3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR032821. KAsynt_C_assoc.
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.
[Graphical view]
PfamiPF00698. 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.
[Graphical view]
SMARTiSM00827. PKS_AT. 1 hit.
SM00825. PKS_KS. 1 hit.
SM00823. PKS_PP. 1 hit.
[Graphical view]
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.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12053-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQSRQLFLF GDQTADFVPK LRSLLSVQDS PILAAFLDQS HYVVRAQMLQ
60 70 80 90 100
SMNTVDHKLA RTADLRQMVQ KYVDGKLTPA FRTALVCLCQ LGCFIREYEE
110 120 130 140 150
SGNMYPQPSD SYVLGFCMGS LAAVAVSCSR SLSELLPIAV QTVLIAFRLG
160 170 180 190 200
LCALEMRDRV DGCSDDRGDP WSTIVWGLDP QQARDQIEVF CRTTNVPQTR
210 220 230 240 250
RPWISCISKN AITLSGSPST LRAFCAMPQM AQHRTAPIPI CLPAHNGALF
260 270 280 290 300
TQADITTILD TTPTTPWEQL PGQIPYISHV TGNVVQTSNY RDLIEVALSE
310 320 330 340 350
TLLEQVRLDL VETGLPRLLQ SRQVKSVTIV PFLTRMNETM SNILPDSFIS
360 370 380 390 400
TETRTDTGRA IPASGRPGAG KCKLAIVSMS GRFPESPTTE SFWDLLYKGL
410 420 430 440 450
DVCKEVPRRR WDINTHVDPS GKARNKGATK WGCWLDFSGD FDPRFFGISP
460 470 480 490 500
KEAPQMDPAQ RMALMSTYEA MERAGLVPDT TPSTQRDRIG VFHGVTSNDW
510 520 530 540 550
METNTAQNID TYFITGGNRG FIPGRINFCF EFAGPSYTND TACSSSLAAI
560 570 580 590 600
HLACNSLWRG DCDTAVAGGT NMIYTPDGHT GLDKGFFLSR TGNCKPYDDK
610 620 630 640 650
ADGYCRAEGV GTVFIKRLED ALADNDPILG VILDAKTNHS AMSESMTRPH
660 670 680 690 700
VGAQIDNMTA ALNTTGLHPN DFSYIEMHGT GTQVGDAVEM ESVLSVFAPS
710 720 730 740 750
ETARKADQPL FVGSAKANVG HGEGVSGVTS LIKVLMMMQH DTIPPHCGIK
760 770 780 790 800
PGSKINRNFP DLGARNVHIA FEPKPWPRTH TPRRVLINNF SAAGGNTALI
810 820 830 840 850
VEDAPERHWP TEKDPRSSHI VALSAHVGAS MKTNLERLHQ YLLKNPHTDL
860 870 880 890 900
AQLSYTTTAR RWHYLHRVSV TGASVEEVTR KLEMAIQNGD GVSRPKSKPK
910 920 930 940 950
ILFAFTGQGS QYATMGKQVY DAYPSFREDL EKFDRLAQSH GFPSFLHVCT
960 970 980 990 1000
SPKGDVEEMA PVVVQLAITC LQMALTNLMT SFGIRPDVTV GHSLGEFAAL
1010 1020 1030 1040 1050
YAAGVLSASD VVYLVGQRAE LLQERCQRGT HAMLAVKATP EALSQWIQDH
1060 1070 1080 1090 1100
DCEVACINGP EDTVLSGTTK NVAEVQRAMT DNGIKCTLLK LPFAFHSAQV
1110 1120 1130 1140 1150
QPILDDFEAL AQGATFAKPQ LLILSPLLRT EIHEQGVVTP SYVAQHCRHT
1160 1170 1180 1190 1200
VDMAQALRSA REKGLIDDKT LVIELGPKPL ISGMVKMTLG DKISTLPTLA
1210 1220 1230 1240 1250
PNKAIWPSLQ KILTSVYTGG WDINWKKYHA PFASSQKVVD LPSYGWDLKD
1260 1270 1280 1290 1300
YYIPYQGDWC LHRHQQDCKC AAPGHEIKTA DYQVPPESTP HRPSKLDPSK
1310 1320 1330 1340 1350
EAFPEIKTTT TLHRVVEETT KPLGATLVVE TDISRKDVNG LARGHLVDGI
1360 1370 1380 1390 1400
PLCTPSFYAD IAMQVGQYSM QRLRAGHPGA GAIDGLVDVS DMVVDKALVP
1410 1420 1430 1440 1450
HGKGPQLLRT TLTMEWPPKA AATTRSAKVK FATYFADGKL DTEHASCTVR
1460 1470 1480 1490 1500
FTSDAQLKSL RRSVSEYKTH IRQLHDGHAK GQFMRYNRKT GYKLMSSMAR
1510 1520 1530 1540 1550
FNPDYMLLDY LVLNEAENEA ASGVDFSLGS SEGTFAAHPA HVDAITQVAG
1560 1570 1580 1590 1600
FAMNANDNVD IEKQVYVNHG WDSFQIYQPL DNSKSYQVYT KMGQAKENDL
1610 1620 1630 1640 1650
VHGDVVVLDG EQIVAFFRGL TLRSVPRGAL RVVLQTTVKK ADRQLGFKTM
1660 1670 1680 1690 1700
PSPPPPTTTM PISPYKPANT QVSSQAIPAE ATHSHTPPQP KHSPVPETAG
1710 1720 1730 1740 1750
SAPAAKGVGV SNEKLDAVMR VVSEESGIAL EELTDDSNFA DMGIDSLSSM
1760 1770 1780 1790 1800
VIGSRFREDL GLDLGPEFSL FIDCTTVRAL KDFMLGSGDA GSGSNVEDPP
1810 1820 1830 1840 1850
PSATPGINPE TDWSSSASDS IFASEDHGHS SESGADTGSP PALDLKPYCR
1860 1870 1880 1890 1900
PSTSVVLQGL PMVARKTLFM LPDGGGSAFS YASLPRLKSD TAVVGLNCPY
1910 1920 1930 1940 1950
ARDPENMNCT HGAMIESFCN EIRRRQPRGP YHLGGWSSGG AFAYVVAEAL
1960 1970 1980 1990 2000
VNQGEEVHSL IIIDAPIPQA MEQLPRAFYE HCNSIGLFAT QPGASPDGST
2010 2020 2030 2040 2050
EPPSYLIPHF TAVVDVMLDY KLAPLHARRM PKVGIVWAAD TVMDERDAPK
2060 2070 2080 2090 2100
MKGMHFMIQK RTEFGPDGWD TIMPGASFDI VRADGANHFT LMQKEHVSII

SDLIDRVMA
Length:2,109
Mass (Da):230,716
Last modified:November 1, 1997 - v1
Checksum:iCB701372A16D8551
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42766 mRNA. Translation: AAC41675.1.
L42765 Genomic DNA. Translation: AAC41674.1.
AY371490 Genomic DNA. Translation: AAS66004.1.
PIRiT17490.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42766 mRNA. Translation: AAC41675.1.
L42765 Genomic DNA. Translation: AAC41674.1.
AY371490 Genomic DNA. Translation: AAS66004.1.
PIRiT17490.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KR5NMR-A1705-1791[»]
3HRQX-ray1.80A/B1305-1660[»]
3HRRX-ray1.90A/B1305-1660[»]
3ILSX-ray1.70A1845-2109[»]
ProteinModelPortaliQ12053.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59286N.

Protein family/group databases

ESTHERiaspor-PKSL1. Thioesterase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00287.
BRENDAi2.3.1.221. 523.

Miscellaneous databases

EvolutionaryTraceiQ12053.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 2 hits.
3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR032821. KAsynt_C_assoc.
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.
[Graphical view]
PfamiPF00698. 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.
[Graphical view]
SMARTiSM00827. PKS_AT. 1 hit.
SM00825. PKS_KS. 1 hit.
SM00823. PKS_PP. 1 hit.
[Graphical view]
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.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPKSL1_ASPPA
AccessioniPrimary (citable) accession number: Q12053
Secondary accession number(s): Q6UEH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.