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A2QJI5

- KYNU2_ASPNC

UniProt

A2QJI5 - KYNU2_ASPNC

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Protein
Kynureninase 2
Gene
bna5-2, An04g07200
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 sitei134 – 1341Pyridoxal phosphate; via amide nitrogen By similarity
Binding sitei135 – 1351Pyridoxal phosphate By similarity
Binding sitei247 – 2471Pyridoxal phosphate By similarity
Binding sitei250 – 2501Pyridoxal phosphate By similarity
Binding sitei272 – 2721Pyridoxal phosphate By similarity
Binding sitei312 – 3121Pyridoxal phosphate By similarity
Binding sitei340 – 3401Pyridoxal 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 2 (EC:3.7.1.3)
Alternative name(s):
Biosynthesis of nicotinic acid protein 5-2
L-kynurenine hydrolase 2
Gene namesi
Name:bna5-2
ORF Names:An04g07200
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 6L

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 – 463463Kynureninase 2UniRule annotation
PRO_0000356968Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei273 – 2731N6-(pyridoxal phosphate)lysine By similarity

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi5061.CADANGAP00004336.

Structurei

3D structure databases

ProteinModelPortaliA2QJI5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni162 – 1654Pyridoxal phosphate binding By similarity

Sequence similaritiesi

Belongs to the kynureninase family.

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242438.
KOiK01556.
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.

A2QJI5-1 [UniParc]FASTAAdd to Basket

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MSKSNGVSLA FPAEAATKEY AASLDSSDRL AAFREKFIVP SKANIASKKL    50
AKPGLSPESC IYFCGNSLGI QPKATAKYLE AQLDTWSSIG VGGHFTDLEG 100
SPLKQWQLLS EQAADSMSKI VGAKPEEVAA MGTLTTNLHL LLASFYKPTQ 150
TKHKILMDWK AFPSDHYAIE SHIAWHDLDP KESMVLIGPD EGEYEISTQK 200
IFSYIDKHAD EAAMILLPGI QYYTGQLFDI QKITKYAHSR NMVVGWDLAH 250
AFANVELKLH DWNVDFAAWC TYKYGNAGPG AMGGLFVHEQ HGEVDYSAGE 300
DAPKFRHRLT GWYGGDRSVR FKMDNKFKPI PGAGGFQISN PSAIDLACLC 350
AALSVFDETS MADLRRKSLK LTAYLEFLLL RDYEEESRPF SIITPKDPEA 400
RGAQLSLLLK PGLLQNVAQK LQEAGIVCDK REPGVVRVAP VPLYNSFSEV 450
WTFVKIFKDA LQQ 463
Length:463
Mass (Da):51,300
Last modified:March 6, 2007 - v1
Checksum:i69BFF4F248B8AB07
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270081 Genomic DNA. Translation: CAK44720.1.
RefSeqiXP_001402081.1. XM_001402044.2.

Genome annotation databases

EnsemblFungiiCADANGAT00004431; CADANGAP00004336; CADANGAG00004431.
GeneIDi4991124.
KEGGiang:ANI_1_1148184.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270081 Genomic DNA. Translation: CAK44720.1 .
RefSeqi XP_001402081.1. XM_001402044.2.

3D structure databases

ProteinModelPortali A2QJI5.
ModBasei Search...

Protein-protein interaction databases

STRINGi 5061.CADANGAP00004336.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANGAT00004431 ; CADANGAP00004336 ; CADANGAG00004431 .
GeneIDi 4991124.
KEGGi ang:ANI_1_1148184.

Phylogenomic databases

eggNOGi COG3844.
HOGENOMi HOG000242438.
KOi K01556.
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 nameiKYNU2_ASPNC
AccessioniPrimary (citable) accession number: A2QJI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: March 6, 2007
Last modified: June 11, 2014
This is version 50 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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