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A6RSP5

- KYNU_BOTFB

UniProt

A6RSP5 - KYNU_BOTFB

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Protein
Kynureninase
Gene
bna5, BC1G_03468
Organism
Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Pyridoxal phosphate By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei142 – 1421Pyridoxal phosphate; via amide nitrogen By similarity
Binding sitei143 – 1431Pyridoxal phosphate By similarity
Binding sitei255 – 2551Pyridoxal phosphate By similarity
Binding sitei258 – 2581Pyridoxal phosphate By similarity
Binding sitei280 – 2801Pyridoxal phosphate By similarity
Binding sitei320 – 3201Pyridoxal phosphate By similarity
Binding sitei348 – 3481Pyridoxal phosphate By similarity

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. L-kynurenine catabolic process Source: UniProtKB-UniPathway
  3. anthranilate metabolic process Source: UniProtKB-HAMAP
  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:
Kynureninase (EC:3.7.1.3)
Alternative name(s):
Biosynthesis of nicotinic acid protein 5
L-kynurenine hydrolase
Gene namesi
Name:bna5
ORF Names:BC1G_03468
OrganismiBotryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
Taxonomic identifieri332648 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeBotrytis

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 475475KynureninaseUniRule annotation
PRO_0000360867Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei281 – 2811N6-(pyridoxal phosphate)lysine By similarity

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi332648.A6RSP5.

Structurei

3D structure databases

ProteinModelPortaliA6RSP5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni170 – 1734Pyridoxal phosphate binding By similarity

Sequence similaritiesi

Belongs to the kynureninase family.

Phylogenomic databases

eggNOGiCOG3844.
KOiK01556.
OMAiGWYGGDK.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V/Cys_dSase.
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.

A6RSP5-1 [UniParc]FASTAAdd to Basket

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MGSIAKEEQP STKVEKPTFS SKANTLEFAQ SLDAKDHMRR FRDQYIIPSK    50
ANIKTKKLAK PGLSDEPSIY FCGNSLGLQP KCVQEYLQAH LDTWSSIAVH 100
GHFRDLEDSP LTQWQLLAEH AAKQCAPIVG AKASEVAIMG TLTTNLHLLM 150
ASFYTPTPEK SKIIMEWKAF PSDHYAIESQ IRGHGYNPEE AMVMIAPDEG 200
SYEISTEKIL RTIDEHASTT ALLLLPGIQY YTGQLFDIKT ITAYAQSKGL 250
TVGWDLAHAA GNVPLQLHDW NVDFAVWCTY KYMNAGPGSI AGAYVHERHG 300
EVDYSEGEEK PKYRHRLMGW YGGDQSCRFL MNNKFRPSPG ASGYQVSNPS 350
VVDLTSLCAA LSIFNQTSMA EISQKTLHLT AYLEHLLLST NSSDSPAFRI 400
ITPSDPSARG TQLSVLLKPG RLETLSDMLE EAGIVADKRK PDVIRVAPVP 450
LYNTYEDVWN FVQIFNKALE KCEEA 475
Length:475
Mass (Da):52,872
Last modified:August 21, 2007 - v1
Checksum:i42BFAB823F77B9F2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH476854 Genomic DNA. Translation: EDN20078.1.
RefSeqiXP_001557886.1. XM_001557836.1.

Genome annotation databases

GeneIDi5438547.
KEGGibfu:BC1G_03468.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH476854 Genomic DNA. Translation: EDN20078.1 .
RefSeqi XP_001557886.1. XM_001557836.1.

3D structure databases

ProteinModelPortali A6RSP5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 332648.A6RSP5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5438547.
KEGGi bfu:BC1G_03468.

Phylogenomic databases

eggNOGi COG3844.
KOi K01556.
OMAi GWYGGDK.

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/Cys_dSase.
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: B05.10.

Entry informationi

Entry nameiKYNU_BOTFB
AccessioniPrimary (citable) accession number: A6RSP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: August 21, 2007
Last modified: July 9, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

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

External Data

Dasty 3

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