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Protein

Versicolorin B synthase

Gene

vbs

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

Functioni

Catalyzes 2 dehydration steps in the aflatoxin biosynthesis pathway: (1) acts as an 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin (OAVN) to (2'S,5'S)-averufin (AVR) and (2) acts as a versicolorin B synthase by catalyzing conversion of versiconal (VHOH) to versicolorin B (VB).5 Publications

Catalytic activityi

Versiconal = versicolorin B + H2O.
5'-oxoaverantin = (1'S,5'S)-averufin + H2O.

Cofactori

FADBy similarity

Kineticsi

  1. KM=20 µM for 5'-oxoaverantin2 Publications
  2. KM=3.1 µM for versiconal (at pH 6.0 and 30 degrees Celsius)2 Publications

Vmax=6.67 nmol/min/mg enzyme with 5'-oxoaverantin as substrate2 Publications

Vmax=0.15 µmol/min/mg enzyme with versiconal (at pH 6.0 and 30 degrees Celsius) as substrate2 Publications

pH dependencei

Optimum pH is 5.5.2 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi76 – 10530FADBy similarityAdd
BLAST

GO - Molecular functioni

  1. choline dehydrogenase activity Source: InterPro
  2. flavin adenine dinucleotide binding Source: InterPro
  3. hydro-lyase activity Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. aflatoxin biosynthetic process Source: UniProtKB
  2. alcohol metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14040.
UniPathwayiUPA00287.

Names & Taxonomyi

Protein namesi
Recommended name:
Versicolorin B synthase (EC:4.2.1.143)
Alternative name(s):
5'-oxoaverantin cyclase (EC:4.2.1.142)
Aflatoxin biosynthesis protein K
Gene namesi
Name:vbs
Synonyms:aflK
OrganismiAspergillus parasiticus
Taxonomic identifieri5067 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

Cytoplasmcytosol 1 Publication

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 4141PRO_0000424163Add
BLAST
Chaini22 – 643622Versicolorin B synthasePRO_0000424164Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi221 – 2211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi507 – 5071N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homodimer.4 Publications

Structurei

3D structure databases

ProteinModelPortaliQ12062.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GMC oxidoreductase family.Curated

Family and domain databases

InterProiIPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000137. Alcohol_oxidase. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q12062-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGRNWFQVTA MAVVPVVGIM AAVNPTILSS AASSLPSLGA MFTSDDFASQ
60 70 80 90 100
MDGRIQAQGL LSSHFGMYGW PGQSFDYVIV GGGTAGLAMA RRLSQDGTAS
110 120 130 140 150
VAVIEAGGFY ETDAGNATEV PMYLFNYFFD NGKVKNPLFD WYQYTTPQPG
160 170 180 190 200
LAQREMFYMQ GKTLGGSTAR GAMLYHRGSK GAYDMWADHV GDDSYRWDKW
210 220 230 240 250
LPYFQKSVHF SGPETNPRPA NATALNDNTA FTASGGPVHV GYPFQVNAIS
260 270 280 290 300
SWVDRALAKM GFPEAQGFSN GNLLGRSYIT HTINPYTRRR ETASSSYLRE
310 320 330 340 350
ALMESNNLNI FTRTLVKRVL FDDQNRATGV TVNTDGFEWQ IGARKEVILS
360 370 380 390 400
AGVMRSPQLL MVSGIGPKDH LEQLGIPVRS DLSGVGQNMQ DTIILGPTVP
410 420 430 440 450
VKVESHSQLM GNKETLPRAI REYNEQRKGL LTNPGQDYFA FEKHQPGMLK
460 470 480 490 500
ESTAADIDAA FPDDWPTFSY IALDDTFVPQ YDGKNYFSMS AALMTPFSRG
510 520 530 540 550
TVTINSNDTA NPPIVDPQWL ADPRDQEMAV AAFRRCREIV ASDVMREVVA
560 570 580 590 600
GPEILPGPQY QTDEEILNYI AETSDAYYAG VGTCAMGKAD DPKAVVDSKA
610 620 630 640
RVLGVKGLRI VDASIFPFAI DGQPMGTVYA LAEKIAAEMM AGQ
Length:643
Mass (Da):70,271
Last modified:November 1, 1996 - v1
Checksum:i4B903BA6A0F39D11
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51327 Genomic DNA. Translation: AAC49318.1.
U51328 mRNA. Translation: AAC49319.1.
AY371490 Genomic DNA. Translation: AAS66012.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51327 Genomic DNA. Translation: AAC49318.1.
U51328 mRNA. Translation: AAC49319.1.
AY371490 Genomic DNA. Translation: AAS66012.1.

3D structure databases

ProteinModelPortaliQ12062.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00287.
BioCyciMetaCyc:MONOMER-14040.

Family and domain databases

InterProiIPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000137. Alcohol_oxidase. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Isolation and characterization of the versicolorin B synthase gene from Aspergillus parasiticus. Expansion of the aflatoxin b1 biosynthetic gene cluster."
    Silva J.C., Minto R.E., Barry C.E., Holland K.A., Townsend C.A.
    J. Biol. Chem. 271:13600-13608(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 163-180 AND 414-428, FUNCTION, SUBUNIT.
    Strain: ATCC 56775 / NRRL 5862 / Su-1 / SRRC 143.
  2. "Completed sequence of aflatoxin pathway gene cluster in Aspergillus parasiticus."
    Yu J., Bhatnagar D., Cleveland T.E.
    FEBS Lett. 564:126-130(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY.
    Strain: ATCC 56775 / NRRL 5862 / Su-1 / SRRC 143.
  3. "Aspergillus parasiticus cyclase catalyzes two dehydration steps in aflatoxin biosynthesis."
    Sakuno E., Wen Y., Hatabayashi H., Arai H., Aoki C., Yabe K., Nakajima H.
    Appl. Environ. Microbiol. 71:2999-3006(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 41-66, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT.
  4. "Purification and properties of versiconal cyclase from Aspergillus parasiticus."
    Lin B.K., Anderson J.A.
    Arch. Biochem. Biophys. 293:67-70(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: ATCC 56775 / NRRL 5862 / Su-1 / SRRC 143.
  5. "Purification and characterization of versicolorin B synthase from Aspergillus parasiticus. Catalysis of the stereodifferentiating cyclization in aflatoxin biosynthesis essential to DNA interaction."
    McGuire S.M., Silva J.C., Casillas E.G., Townsend C.A.
    Biochemistry 35:11470-11486(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
  6. "Heterologous expression, isolation, and characterization of versicolorin B synthase from Aspergillus parasiticus. A key enzyme in the aflatoxin B1 biosynthetic pathway."
    Silva J.C., Townsend C.A.
    J. Biol. Chem. 272:804-813(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION.
    Strain: ATCC 56775 / NRRL 5862 / Su-1 / SRRC 143.
  7. "Involvement of two cytosolic enzymes and a novel intermediate, 5'-oxoaverantin, in the pathway from 5'-hydroxyaverantin to averufin in aflatoxin biosynthesis."
    Sakuno E., Yabe K., Nakajima H.
    Appl. Environ. Microbiol. 69:6418-6426(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  8. Cited for: REVIEW.
    Strain: ATCC 56775 / NRRL 5862 / Su-1 / SRRC 143.

Entry informationi

Entry nameiAFLK_ASPPA
AccessioniPrimary (citable) accession number: Q12062
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 79 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

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.