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Protein

Kynureninase 1

Gene

bna5-1

Organism
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
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 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.

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 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)DescriptionActionsGraphical viewLength
Binding sitei147Pyridoxal phosphate; via amide nitrogenUniRule annotation1
Binding sitei148Pyridoxal phosphateUniRule annotation1
Binding sitei232Pyridoxal phosphateUniRule annotation1
Binding sitei261Pyridoxal phosphateUniRule annotation1
Binding sitei264Pyridoxal phosphateUniRule annotation1
Binding sitei286Pyridoxal phosphateUniRule annotation1
Binding sitei326Pyridoxal phosphateUniRule annotation1
Binding sitei354Pyridoxal 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 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:ATEG_04474
OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
Taxonomic identifieri341663 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000007963 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:ATEG_04474

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003569711 – 483Kynureninase 1Add BLAST483

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei287N6-(pyridoxal phosphate)lysineUniRule annotation1

Proteomic databases

PRIDEiQ0CPB0

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi33178.CADATEAP00009046

Structurei

3D structure databases

ProteinModelPortaliQ0CPB0
SMRiQ0CPB0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni175 – 178Pyridoxal phosphate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000242438
OMAiVCSLHAS
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.

Q0CPB0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSRLHLRDI KHGPPLPYHD DIRAFTKEYA ESLDAQDPLR KFRDEFIIPS
60 70 80 90 100
KKDLKRTVLA ADENTDDSTD PRCIYLCGNS LGLQPRSTRK YIDRYLRTWA
110 120 130 140 150
IKGVTGHFTP HDDQLLPPFV DVDVAGAKLM APVVGALESE VAVMDTLTTN
160 170 180 190 200
LHLLMASFYR PTQERYKIII EGKAFPSDHY AVESQIRHHN REPSEAMVLI
210 220 230 240 250
EPEDPKHPIL TTDQILRVID ENASSAALIL LSAIQFYTGQ YFDIKTITAH
260 270 280 290 300
AQSKGIIVGW DCAHAAGNVD LQLHDWNVDF AAWCNYKYLN SGPGGMAGLF
310 320 330 340 350
VHERHGHVES KNGAQNEGFR PRLSGWWGGD KETRFLMDNN FRPQVGAAGF
360 370 380 390 400
QLSNPSVLDM NAVVASLEIF SRASMEKIRQ KSLHLTGYLE HLLVTYPLDA
410 420 430 440 450
PPEEKPFTII TPSNPAERGA QLSLRLGPGL LEKVLEVLEE QGVIIDERKP
460 470 480
DVIRVAPAPL YNTYAELSSS GIHIAYSSYN QYS
Length:483
Mass (Da):54,112
Last modified:October 17, 2006 - v1
Checksum:i6BCC62116EAB97BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476599 Genomic DNA Translation: EAU34921.1
RefSeqiXP_001213652.1, XM_001213652.1

Genome annotation databases

EnsemblFungiiCADATEAT00009046; CADATEAP00009046; CADATEAG00009046
GeneIDi4320432

Similar proteinsi

Entry informationi

Entry nameiKYNU1_ASPTN
AccessioniPrimary (citable) accession number: Q0CPB0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: October 17, 2006
Last modified: May 23, 2018
This is version 59 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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