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Protein

Kynureninase 2

Gene

bna5-2

Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Status
Reviewed-Annotation score: -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: L-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 2 (bna5-2), Kynureninase 1 (bna5-1)
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.

Pathwayi: NAD(+) 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 2 (bna5-2), Kynureninase 1 (bna5-1)
  3. 3-hydroxyanthranilate 3,4-dioxygenase 1 (bna1-1), 3-hydroxyanthranilate 3,4-dioxygenase 2 (bna1-2)
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)DescriptionActionsGraphical viewLength
Binding sitei135Pyridoxal phosphate; via amide nitrogenUniRule annotation1
Binding sitei136Pyridoxal phosphateUniRule annotation1
Binding sitei248Pyridoxal phosphateUniRule annotation1
Binding sitei251Pyridoxal phosphateUniRule annotation1
Binding sitei273Pyridoxal phosphateUniRule annotation1
Binding sitei313Pyridoxal phosphateUniRule annotation1
Binding sitei341Pyridoxal phosphateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processPyridine nucleotide biosynthesis
LigandPyridoxal 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:ACLA_049070
OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Taxonomic identifieri344612 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006701 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:ACLA_049070

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003569621 – 464Kynureninase 2Add BLAST464

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei274N6-(pyridoxal phosphate)lysineUniRule annotation1

Proteomic databases

PRIDEiA1CHT0

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi5057.CADACLAP00004943

Structurei

3D structure databases

ProteinModelPortaliA1CHT0
SMRiA1CHT0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni163 – 166Pyridoxal phosphate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000242438
KOiK01556
OMAiGWYGGDK
OrthoDBiEOG092C20ON

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
HAMAPiMF_01970 Kynureninase, 1 hit
InterProiView protein in InterPro
IPR000192 Aminotrans_V_dom
IPR010111 Kynureninase
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PANTHERiPTHR14084 PTHR14084, 1 hit
PfamiView protein in Pfam
PF00266 Aminotran_5, 1 hit
PIRSFiPIRSF038800 KYNU, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR01814 kynureninase, 1 hit

Sequencei

Sequence statusi: Complete.

A1CHT0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTTTTSSKP EFPADAATKE YAASLDASDP LAGFREKFII PSKANIASKK
60 70 80 90 100
LAKPGLSSEP CIYFCGNSLG IQPKATAKYL EAQLDTWSSI GVSGHFTNVE
110 120 130 140 150
DSPLREWQNL AEQAAESMSR VVGAAPEEVA AMGTLTMNLH LLLASFYRPT
160 170 180 190 200
ATKHKILMDW KAFPSDHYAI ESHIAWHDLD PKESMVLIGP DEGTFEIPTE
210 220 230 240 250
KILSYIDQHA DDAALILLPG IQYYTGQLFD IQKITEYAQS RGLVVGWDLA
260 270 280 290 300
HAYGNVHLKL HDWNVDFAAW CTYKYGNAGP GAMAGLFVHE RHGRVDYREG
310 320 330 340 350
EDSPKFRHRL TGWYGGDKSV RFKMDNNFKP IPGAGGYQIS NPSAIDLASL
360 370 380 390 400
CAALSVFDET SMAELRRKSV LMTAYLEHLL LKDTTDESRL FDIITPSEPA
410 420 430 440 450
ARGAQLSLLL RPGLLHKVAQ RLQEAGIICD KREPGVVRVA PVPLYNTFTE
460
VWTFVEQLKA ALEE
Length:464
Mass (Da):51,324
Last modified:January 23, 2007 - v1
Checksum:i011392A1F27E2766
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027054 Genomic DNA Translation: EAW10435.1
RefSeqiXP_001271861.1, XM_001271860.1

Genome annotation databases

EnsemblFungiiCADACLAT00005044; CADACLAP00004943; CADACLAG00005044
GeneIDi4704039
KEGGiact:ACLA_049070

Similar proteinsi

Entry informationi

Entry nameiKYNU2_ASPCL
AccessioniPrimary (citable) accession number: A1CHT0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 62 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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