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Protein

Kynureninase 2

Gene

bna5-2

Organism
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
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

Pathway:iL-kynurenine degradation

This protein is involved in step 1 of the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Kynureninase 1 (bna5-1), Kynureninase 2 (bna5-2)
This subpathway is part of the pathway L-kynurenine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine, the pathway L-kynurenine degradation and in Amino-acid degradation.

Pathway:iNAD(+) biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Kynurenine 3-monooxygenase (bna4)
  2. Kynureninase 1 (bna5-1), Kynureninase 2 (bna5-2)
  3. 3-hydroxyanthranilate 3,4-dioxygenase (bna1)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

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

GO - Biological processi

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:ATEG_00758
OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
Taxonomic identifieri341663 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000007963 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:ATEG_00758.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463Kynureninase 2PRO_0000356972Add
BLAST

Amino acid modifications

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

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ0CZX6.
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.
OMAiGWYGGDK.
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.

Q0CZX6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSENNCSKPS FPDNAASKEY AASLDAADPL ASFRDQFIIP SKANIACKRL
60 70 80 90 100
AKPNLSPEPC IYFCGNSLGI QPKATAKYLE AQLDTWSSIG VCGHFTNLED
110 120 130 140 150
SPMKSWQLLA EQAAESMSKI VGADPAEVAA MGTLTANLHL LMASFYKPTA
160 170 180 190 200
TKHKILMDWK AFPSDHYAIE SHIAWHNLDP KESMVLIGPD EGEYEISTDK
210 220 230 240 250
ILSYIDQHAE DAALLLLPGI QYYTGQLFDI PKITEYAKSR NLVVGWDLAH
260 270 280 290 300
AYGNVELKLH DWNVDFAAWC TYKYGNAGPG AMAGLFVHDK HGQVDYSQGE
310 320 330 340 350
DSPKFRHRLT GWYGGDRSVR FKMDNKFKPI PGAGGFQISN PSAIDLSCLC
360 370 380 390 400
AALSVFDQTS VSELRRKSLK LTAYLEYLLL KDTTEDSRPF RIITPTNPEA
410 420 430 440 450
RGAQLSLLLK PGLLQGVSER LQDAGIICDK REPGVVRVAP VPLYNTYSEV
460
WEFVQQFRAA LQL
Length:463
Mass (Da):51,310
Last modified:October 17, 2006 - v1
Checksum:i402C2BC2BD9A167A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476594 Genomic DNA. Translation: EAU39404.1.
RefSeqiXP_001210844.1. XM_001210844.1.

Genome annotation databases

EnsemblFungiiCADATEAT00007194; CADATEAP00007194; CADATEAG00007194.
GeneIDi4355513.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476594 Genomic DNA. Translation: EAU39404.1.
RefSeqiXP_001210844.1. XM_001210844.1.

3D structure databases

ProteinModelPortaliQ0CZX6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADATEAT00007194; CADATEAP00007194; CADATEAG00007194.
GeneIDi4355513.

Organism-specific databases

EuPathDBiFungiDB:ATEG_00758.

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242438.
OMAiGWYGGDK.
OrthoDBiEOG7V1G0J.

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. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NIH 2624 / FGSC A1156.

Entry informationi

Entry nameiKYNU2_ASPTN
AccessioniPrimary (citable) accession number: Q0CZX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: October 17, 2006
Last modified: July 22, 2015
This is version 48 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

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.