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Protein

Kynureninase 1

Gene

bna5-1

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
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 sitei149Pyridoxal phosphate; via amide nitrogenUniRule annotation1
Binding sitei150Pyridoxal phosphateUniRule annotation1
Binding sitei234Pyridoxal phosphateUniRule annotation1
Binding sitei263Pyridoxal phosphateUniRule annotation1
Binding sitei266Pyridoxal phosphateUniRule annotation1
Binding sitei288Pyridoxal phosphateUniRule annotation1
Binding sitei329Pyridoxal phosphateUniRule annotation1
Binding sitei357Pyridoxal 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:AN5952
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome I
  • UP000005890 Componenti: Unassembled WGS sequence

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003569771 – 487Kynureninase 1Add BLAST487

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei289N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi162425.CADANIAP00007075

Structurei

3D structure databases

ProteinModelPortaliQ5B0H8
SMRiQ5B0H8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni177 – 180Pyridoxal phosphate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000242438
InParanoidiQ5B0H8
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.

Q5B0H8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSRLHVQQI KNGPPLPYKD DIRAFTRDYA ASLDAQDPLS HFREEFIIPS
60 70 80 90 100
VKDLKRKTLD PSEGEYSSMY LDARCIYLCG NSLGLQPRNT KKYINYYLRT
110 120 130 140 150
WAIKGVTGHF THHDDELLPP FVDVDSAGAK LMAPVVGALE SEVAVMGSLT
160 170 180 190 200
TNLHLLMASF YRPTTERYKI IIEGKAFPSD HYAVESQIKH HNLQPKDAMV
210 220 230 240 250
LIEPQDPEHP ILETDRILRV IDEHASTTAL LLLSAIQYYT GQYFNIEKIT
260 270 280 290 300
AHAQSKGIVV GWDCAHAAGN VDLKLHDWNV DFAAWCNYKY LNSGPGGMAG
310 320 330 340 350
IFVHEKHGEV KAGQGDGELE LFRPRLSGWW GGDKATRFLM DNHFVPQSGA
360 370 380 390 400
AGYQLSNPSV LDMNAVVASL ELFNRTSMAE IRQKSLNLTG YLEHLLLASL
410 420 430 440 450
DGVSDKPFSI ITPPNPSERG AQLSLRLAPG LLDSVLETLE EYAVVIDERK
460 470 480
PDVIRVAPAP LYNTYEEVWQ FCQIFSEACR KALEKKD
Length:487
Mass (Da):54,517
Last modified:April 26, 2005 - v1
Checksum:i0E77B19E6DCFE55D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACD01000101 Genomic DNA Translation: EAA57815.1
BN001301 Genomic DNA Translation: CBF70497.1
RefSeqiXP_663556.1, XM_658464.1

Genome annotation databases

EnsemblFungiiCBF70497; CBF70497; ANIA_05952
EAA57815; EAA57815; AN5952.2
GeneIDi2870933
KEGGiani:AN5952.2

Similar proteinsi

Entry informationi

Entry nameiKYNU1_EMENI
AccessioniPrimary (citable) accession number: Q5B0H8
Secondary accession number(s): C8V3G6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: April 26, 2005
Last modified: June 20, 2018
This is version 75 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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