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A2R7T0

- KYNU1_ASPNC

UniProt

A2R7T0 - KYNU1_ASPNC

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Protein
Kynureninase 1
Gene
bna5-1, An16g04630
Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
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 sitei146 – 1461Pyridoxal phosphate; via amide nitrogen By similarity
Binding sitei147 – 1471Pyridoxal phosphate By similarity
Binding sitei231 – 2311Pyridoxal phosphate By similarity
Binding sitei260 – 2601Pyridoxal phosphate By similarity
Binding sitei263 – 2631Pyridoxal phosphate By similarity
Binding sitei285 – 2851Pyridoxal phosphate By similarity
Binding sitei326 – 3261Pyridoxal phosphate By similarity
Binding sitei354 – 3541Pyridoxal phosphate By similarity

GO - Molecular functioni

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

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 1 (EC:3.7.1.3)
Alternative name(s):
Biosynthesis of nicotinic acid protein 5-1
L-kynurenine hydrolase 1
Gene namesi
Name:bna5-1
ORF Names:An16g04630
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 5R

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 – 472472Kynureninase 1UniRule annotation
PRO_0000356967Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei286 – 2861N6-(pyridoxal phosphate)lysine By similarity

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi5061.CADANGAP00012690.

Structurei

3D structure databases

ProteinModelPortaliA2R7T0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni174 – 1774Pyridoxal phosphate binding By similarity

Sequence similaritiesi

Belongs to the kynureninase family.

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242438.
OrthoDBiEOG7V1G0J.

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.

A2R7T0-1 [UniParc]FASTAAdd to Basket

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MSSQLGHESS VSSPLSYKTD SNAFTREYAE SLDAQDPLRD FRKEFIIPSK    50
VDLKRKTLAI DDSSKDESDP RCIYLCGNSL GVQPRNARKY IDYYLRTWAI 100
KGVTGHFLPH EDQLLPPFVD VDDAGAKLMA PIVGALESEV AVMGTLTANL 150
HFLMASFYRP TQERYKIILE GKAFPSDHYA IESQIRHHNL RPEDAMVLIE 200
PEDRLKPILR TEQILRVIDE HASSTALVLL SGIQFYTGQY FDIEKITAHA 250
QSKGILVGWD CAHAAGNVDL RLHDWNVDFA AWCNYKYLNS GPGGMAALFV 300
HERHGRVDMD KVGSDEEPFR PRLSGWWGGD KKTRFLMNNN FLPQTGAAGF 350
QLSNPSVLDM NAVVASLELF NRTSMAEIRQ KSLNATGYLE HLLLNYPADF 400
STGKRPFSII TPSNPAERGA QLSLLLEPGL LDSVLETLEE HGVVVDERKP 450
DVIRVAPAPL YNTYTEYPTY RT 472
Length:472
Mass (Da):53,008
Last modified:March 6, 2007 - v1
Checksum:i36CAC1D632AA5607
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270369 Genomic DNA. Translation: CAK42891.1.

Genome annotation databases

EnsemblFungiiCADANGAT00012932; CADANGAP00012690; CADANGAG00012932.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270369 Genomic DNA. Translation: CAK42891.1 .

3D structure databases

ProteinModelPortali A2R7T0.
ModBasei Search...

Protein-protein interaction databases

STRINGi 5061.CADANGAP00012690.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANGAT00012932 ; CADANGAP00012690 ; CADANGAG00012932 .

Phylogenomic databases

eggNOGi COG3844.
HOGENOMi HOG000242438.
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/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. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiKYNU1_ASPNC
AccessioniPrimary (citable) accession number: A2R7T0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: March 6, 2007
Last modified: June 11, 2014
This is version 46 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

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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