Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A7ESB8

- KYNU_SCLS1

UniProt

A7ESB8 - KYNU_SCLS1

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Kynureninase

Gene

bna5

Organism
Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
Status
Reviewed - 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

Pathwayi

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

  1. kynureninase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
  2. anthranilate metabolic process Source: UniProtKB-HAMAP
  3. L-kynurenine catabolic process Source: UniProtKB-UniPathway
  4. quinolinate biosynthetic process Source: UniProtKB-HAMAP
  5. tryptophan catabolic process Source: UniProtKB-HAMAP
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: Unassembled WGS sequence

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
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

Protein-protein interaction databases

STRINGi665079.A7ESB8.

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 .
RefSeqi XP_001590483.1. XM_001590433.1.

3D structure databases

ProteinModelPortali A7ESB8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 665079.A7ESB8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii EDN92360 ; EDN92360 ; SS1G_08223 .
GeneIDi 5486837.
KEGGi ssl:SS1G_08223.

Phylogenomic databases

eggNOGi COG3844.
InParanoidi A7ESB8.
KOi K01556.
OMAi GWYGGDK.
OrthoDBi EOG7V1G0J.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00329 .
UPA00334 ; UER00455 .

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPi MF_01970. Kynureninase.
InterProi IPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
PANTHERi PTHR14084. PTHR14084. 1 hit.
Pfami PF00266. Aminotran_5. 1 hit.
[Graphical view ]
PIRSFi PIRSF038800. KYNU. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR01814. kynureninase. 1 hit.
ProtoNeti Search...

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: November 26, 2014
This is version 48 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