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Protein

Kynureninase

Gene

bna5

Organism
Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.UniRule annotation

Catalytic activityi

L-kynurenine + H2O = anthranilate + L-alanine.UniRule annotation
L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathway:iL-kynurenine degradation

This protein is involved in step 1 of the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Kynureninase (bna5)
This subpathway is part of the pathway L-kynurenine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine, the pathway L-kynurenine degradation and in Amino-acid degradation.

Pathway:iNAD(+) biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Kynurenine 3-monooxygenase (bna4)
  2. Kynureninase (bna5)
  3. 3-hydroxyanthranilate 3,4-dioxygenase (bna1)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei141 – 1411Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei142 – 1421Pyridoxal phosphateUniRule annotation
Binding sitei254 – 2541Pyridoxal phosphateUniRule annotation
Binding sitei257 – 2571Pyridoxal phosphateUniRule annotation
Binding sitei279 – 2791Pyridoxal phosphateUniRule annotation
Binding sitei319 – 3191Pyridoxal phosphateUniRule annotation
Binding sitei347 – 3471Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

Names & Taxonomyi

Protein namesi
Recommended name:
KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
Alternative name(s):
Biosynthesis of nicotinic acid protein 5UniRule annotation
L-kynurenine hydrolaseUniRule annotation
Gene namesi
Name:bna5
ORF Names:SS1G_08223
OrganismiSclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
Taxonomic identifieri665079 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeSclerotinia
ProteomesiUP000001312 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:SS1G_08223.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 475475KynureninasePRO_0000360872Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei280 – 2801N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA7ESB8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni169 – 1724Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3844.
InParanoidiA7ESB8.
KOiK01556.
OMAiGWYGGDK.
OrthoDBiEOG7V1G0J.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.

Sequencei

Sequence statusi: Complete.

A7ESB8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSIAKEEQP SKVEKPTFSS KANTLEYAQS LDANDHMRRF RDQFIIPSKA
60 70 80 90 100
NIKATKLEKP GLSDESSIYF CGNSLGLQPK CVKEYLQAHL DTWSSIGVHG
110 120 130 140 150
HFRDLEDSPL TQWQLLAEHA SKQCAPIVGA KASEVAMMGT LTTNLHLLMA
160 170 180 190 200
SFYTPTPEKN KIIMEWKAFP SDHYAIESQI RGHGYNPQEA MVMIGPEEGS
210 220 230 240 250
YEISTEKILR TIDEHASTTA LVLLPGIQYY TGQLFDVKTI TAYAQSKGLI
260 270 280 290 300
VGWDLAHAAG NVPLQLHDWN VDFAVWCTYK YMNAGPGSIA GAFIHERHGE
310 320 330 340 350
VDYSEGEEKP KYRHRLMGWY GGDQSCRFLM NNKFRPSPGA SGYQVSNPSV
360 370 380 390 400
VDLTSLCAAL SIFNQTSMEE ISQKTLHLTA YLEHLLLTSN PSNTNPAFRI
410 420 430 440 450
ITPSDPSARG TQLSVLLKPG RLETLSDMLE EAGIVADKRK PDVIRVAPVP
460 470
LYNTYEDVWR FVQIFNAALE KCEEA
Length:475
Mass (Da):52,956
Last modified:September 11, 2007 - v1
Checksum:iDC42B2E8ED59B7C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476631 Genomic DNA. Translation: EDN92360.1.
RefSeqiXP_001590483.1. XM_001590433.1.

Genome annotation databases

EnsemblFungiiEDN92360; EDN92360; SS1G_08223.
GeneIDi5486837.
KEGGissl:SS1G_08223.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476631 Genomic DNA. Translation: EDN92360.1.
RefSeqiXP_001590483.1. XM_001590433.1.

3D structure databases

ProteinModelPortaliA7ESB8.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEDN92360; EDN92360; SS1G_08223.
GeneIDi5486837.
KEGGissl:SS1G_08223.

Organism-specific databases

EuPathDBiFungiDB:SS1G_08223.

Phylogenomic databases

eggNOGiCOG3844.
InParanoidiA7ESB8.
KOiK01556.
OMAiGWYGGDK.
OrthoDBiEOG7V1G0J.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea."
    Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., Quevillon E.
    , Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.
    PLoS Genet. 7:E1002230-E1002230(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 18683 / 1980 / Ss-1.

Entry informationi

Entry nameiKYNU_SCLS1
AccessioniPrimary (citable) accession number: A7ESB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: September 11, 2007
Last modified: July 22, 2015
This is version 52 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

Complete proteome, Reference proteome

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.