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Protein

Kynureninase 1

Gene

bna5-1

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 sitei146Pyridoxal phosphate; via amide nitrogenUniRule annotation1
Binding sitei147Pyridoxal phosphateUniRule annotation1
Binding sitei231Pyridoxal phosphateUniRule annotation1
Binding sitei260Pyridoxal phosphateUniRule annotation1
Binding sitei263Pyridoxal phosphateUniRule annotation1
Binding sitei285Pyridoxal 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:ACLA_069390
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_069390

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003569611 – 486Kynureninase 1Add BLAST486

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei286N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi5057.CADACLAP00006290

Structurei

3D structure databases

ProteinModelPortaliA1C688
SMRiA1C688
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni174 – 177Pyridoxal phosphate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000242438
KOiK01556
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.

A1C688-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSRLHTREI QNGPPLPYND DIRAFSKEYA ESLDAQDPLH RFRNEFVIPS
60 70 80 90 100
KEDLKRTTLD PNQEPEHSPT PSLYLCGNSL GLQPQSTRKY IEYYLRAWAT
110 120 130 140 150
KGVTGHFVQH DDQLLPPFVD VDAAGARLMA PIVGAMESEV AVMGTLTTNL
160 170 180 190 200
HILMASFYQP TQERYKIIIE GKAFPSDHYA VESQIKHHNF DPKDGMVLIE
210 220 230 240 250
PEDHTRPVLD TEHIIRTIDE HASSTAVILL SAIQYYTGQY FDIKRITAHA
260 270 280 290 300
QSKGILVGWD CAHAAGNVDL QLHDWNVDFA AWCTYKYLNS GPGGTAALFV
310 320 330 340 350
HERHGRVNLE QVNSESEPFR PRLSGWWGGD KKTRFLMDNN FIPQPGAAGF
360 370 380 390 400
QLSNPSVLDM NAVVASLELF KQASMAEIRK KSLHITGYLE HLLLNYPLDT
410 420 430 440 450
PSEKKPFTII TPSNPAERGA QLSVRLQPGL LDHVLETLED NAVVIDERKP
460 470 480
DVIRVAPAPL YNTYTDVWEF CRIFHEACQK ALKARG
Length:486
Mass (Da):54,747
Last modified:January 23, 2007 - v1
Checksum:iB4275CBDF28D6821
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027045 Genomic DNA Translation: EAW13909.1
RefSeqiXP_001275335.1, XM_001275334.1

Genome annotation databases

EnsemblFungiiEAW13909; EAW13909; ACLA_069390
GeneIDi4707638
KEGGiact:ACLA_069390

Similar proteinsi

Entry informationi

Entry nameiKYNU1_ASPCL
AccessioniPrimary (citable) accession number: A1C688
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 64 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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