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Protein

Kynureninase 1

Gene

bna5-1

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: 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 sitei169 – 1691Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei170 – 1701Pyridoxal phosphateUniRule annotation
Binding sitei283 – 2831Pyridoxal phosphateUniRule annotation
Binding sitei286 – 2861Pyridoxal phosphateUniRule annotation
Binding sitei308 – 3081Pyridoxal phosphateUniRule annotation
Binding sitei349 – 3491Pyridoxal phosphateUniRule annotation
Binding sitei377 – 3771Pyridoxal 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 1UniRule annotation (EC:3.7.1.3UniRule annotation)
Alternative name(s):
Biosynthesis of nicotinic acid protein 5-1UniRule annotation
L-kynurenine hydrolase 1UniRule annotation
Gene namesi
Name:bna5-1
ORF Names:AFUB_026170
OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Taxonomic identifieri451804 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000001699: Unassembled WGS sequence

Subcellular locationi

Cytoplasm 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 – 509509Kynureninase 1PRO_0000356963Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei309 – 3091N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB0XS72.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni197 – 2004Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000242438.
OrthoDBiEOG7V1G0J.
PhylomeDBiB0XS72.

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. 2 hits.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.

Sequencei

Sequence statusi: Complete.

B0XS72-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSRLHVQVI HGGPPLPYKD DIRAFGKEYA EQLDAQDPLR RFRDEFIIPS
60 70 80 90 100
KKDLKRKTLF PNDGMYSCGH PICFANTSCA CVHAAETEET SDEKCIYLCG
110 120 130 140 150
NSLGLQPRST RKYIDHYLRT WATKGVTGHF VPHDDQLLPP FVDVDEAGAK
160 170 180 190 200
LMAPIVGALK SEVAVMGTLT ANLHLLMASF YRPTPERNKI IIEGKAFPSD
210 220 230 240 250
HYAVESQIRH HNLDPKDAMV LIEPEDLDRP ILDTKYILRV IDENAHSTAL
260 270 280 290 300
ILLPAIQFYT GQYFDIQRIT AHAQSKGILV GWDCAHAAGN VDLRLHDWNV
310 320 330 340 350
DFAAWCTYKY LNAGPGGMAA LFVHERHGRV DIEQAASGKE AFHPRFSGWW
360 370 380 390 400
GGDKQTRFLM NNHFVPQQGA AGFQLSNPSV LDMNAVVASL ELFNQTSMAE
410 420 430 440 450
IRKKSLNLTG YLEHLLLRDP QTENSEKRPF SIITPSNPAE RGAQLSIRLQ
460 470 480 490 500
PGLLDRVLES LNEDAVIIDE RKPDVIRVAP APLYNTYAEV WRFAQLFHLA

CDKALCGRK
Length:509
Mass (Da):57,148
Last modified:April 8, 2008 - v1
Checksum:iFAB6BF3A24F37D13
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499595 Genomic DNA. Translation: EDP54558.1.

Genome annotation databases

EnsemblFungiiCADAFUBT00002611; CADAFUBP00002557; CADAFUBG00002611.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499595 Genomic DNA. Translation: EDP54558.1.

3D structure databases

ProteinModelPortaliB0XS72.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUBT00002611; CADAFUBP00002557; CADAFUBG00002611.

Phylogenomic databases

HOGENOMiHOG000242438.
OrthoDBiEOG7V1G0J.
PhylomeDBiB0XS72.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

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. 2 hits.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CEA10 / CBS 144.89 / FGSC A1163.

Entry informationi

Entry nameiKYNU1_ASPFC
AccessioniPrimary (citable) accession number: B0XS72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: April 8, 2008
Last modified: January 7, 2015
This is version 41 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.