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A2QJI5

- KYNU2_ASPNC

UniProt

A2QJI5 - KYNU2_ASPNC

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Protein

Kynureninase 2

Gene

bna5-2

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.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 sitei134 – 1341Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei135 – 1351Pyridoxal phosphateUniRule annotation
Binding sitei247 – 2471Pyridoxal phosphateUniRule annotation
Binding sitei250 – 2501Pyridoxal phosphateUniRule annotation
Binding sitei272 – 2721Pyridoxal phosphateUniRule annotation
Binding sitei312 – 3121Pyridoxal phosphateUniRule annotation
Binding sitei340 – 3401Pyridoxal 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:
Kynureninase 2UniRule annotation (EC:3.7.1.3UniRule annotation)
Alternative name(s):
Biosynthesis of nicotinic acid protein 5-2UniRule annotation
L-kynurenine hydrolase 2UniRule annotation
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 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 – 463463Kynureninase 2PRO_0000356968Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei273 – 2731N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi5061.CADANGAP00004336.

Structurei

3D structure databases

ProteinModelPortaliA2QJI5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni162 – 1654Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

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_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.

A2QJI5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKSNGVSLA FPAEAATKEY AASLDSSDRL AAFREKFIVP SKANIASKKL
60 70 80 90 100
AKPGLSPESC IYFCGNSLGI QPKATAKYLE AQLDTWSSIG VGGHFTDLEG
110 120 130 140 150
SPLKQWQLLS EQAADSMSKI VGAKPEEVAA MGTLTTNLHL LLASFYKPTQ
160 170 180 190 200
TKHKILMDWK AFPSDHYAIE SHIAWHDLDP KESMVLIGPD EGEYEISTQK
210 220 230 240 250
IFSYIDKHAD EAAMILLPGI QYYTGQLFDI QKITKYAHSR NMVVGWDLAH
260 270 280 290 300
AFANVELKLH DWNVDFAAWC TYKYGNAGPG AMGGLFVHEQ HGEVDYSAGE
310 320 330 340 350
DAPKFRHRLT GWYGGDRSVR FKMDNKFKPI PGAGGFQISN PSAIDLACLC
360 370 380 390 400
AALSVFDETS MADLRRKSLK LTAYLEFLLL RDYEEESRPF SIITPKDPEA
410 420 430 440 450
RGAQLSLLLK PGLLQNVAQK LQEAGIVCDK REPGVVRVAP VPLYNSFSEV
460
WTFVKIFKDA LQQ
Length:463
Mass (Da):51,300
Last modified:March 6, 2007 - v1
Checksum:i69BFF4F248B8AB07
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AM270081 Genomic DNA. Translation: CAK44720.1 .
RefSeqi XP_001402081.1. XM_001402044.2.

3D structure databases

ProteinModelPortali A2QJI5.
ModBasei Search...
MobiDBi 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_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. "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: November 26, 2014
This is version 53 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