Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Kynureninase

Gene

kynU

Organism
Streptomyces antibioticus
Status
Unreviewed-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

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Catalytic activityi

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation
L-kynurenine + H2O = anthranilate + 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 (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU)
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. no protein annotated in this organism
  2. Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU)
  3. 3-hydroxyanthranilate 3,4-dioxygenase (nbaC)
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 sitei97Pyridoxal phosphate; via amide nitrogenUniRule annotation1
Binding sitei98Pyridoxal phosphateUniRule annotation1
Binding sitei195Pyridoxal phosphateUniRule annotation1
Binding sitei198Pyridoxal phosphateUniRule annotation1
Binding sitei220Pyridoxal phosphateUniRule annotation1
Binding sitei250Pyridoxal phosphateUniRule annotation1
Binding sitei276Pyridoxal phosphateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolaseUniRule annotation
Biological processPyridine nucleotide biosynthesisUniRule annotation
LigandPyridoxal phosphateUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329
UPA00334; UER00455

Names & Taxonomyi

Protein namesi
Recommended name:
KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
Alternative name(s):
L-kynurenine hydrolaseUniRule annotation
Gene namesi
Name:kynUUniRule annotation
ORF Names:ADK77_21640Imported
OrganismiStreptomyces antibioticusImported
Taxonomic identifieri1890 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces
Proteomesi
  • UP000037372 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei221N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini137 – 326Aminotran_5InterPro annotationAdd BLAST190

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni126 – 129Pyridoxal phosphate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

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.

A0A0L8NMZ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSELPLLAKE LDEADELAAL RDRFVLDEVV YLDGNSLGAL PAHVPDRVAD
60 70 80 90 100
VVRRQWGELR IRSWEESGWW TAPERIGDRI APLVGAAPGQ VVVGDSTSVN
110 120 130 140 150
VFKALVAAIR MAGDGRDELL VDATTFPTDG YIAESAARLT GRTLRAVTPA
160 170 180 190 200
EVPSALGDRT AAVLLNHVDY RTGRLHDLPA LTAAVHACGA LAVWDLCHSA
210 220 230 240 250
GALPVGLDEH GVDLAVGCTY KYLNGGPGSP AYLYVRRELQ DRFDSPLPGW
260 270 280 290 300
NSHAEPFGMS PSYAPAAGAV RGRVGTPDIL SLLALEAALD VWDGVSVDAV
310 320 330 340 350
RAKSLALTDF FLRCVEEYTE PGRVECVTPE RHAERGSQIA LRCPDAGEVM
360 370 380 390
KRLIARGVVG DFRHPDVLRF GFTPLYVGFR DVERAARVLG EELA
Length:394
Mass (Da):42,492
Last modified:November 11, 2015 - v1
Checksum:iD4EA02B1F8EBAFC9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
LGUX01000253 Genomic DNA Translation: KOG64043.1
RefSeqiWP_030648301.1, NZ_LGUX01000253.1

Genome annotation databases

EnsemblBacteriaiKOG64043; KOG64043; ADK77_21640
PATRICifig|1890.24.peg.4764

Similar proteinsi

Entry informationi

Entry nameiA0A0L8NMZ0_STRAT
AccessioniPrimary (citable) accession number: A0A0L8NMZ0
Entry historyiIntegrated into UniProtKB/TrEMBL: November 11, 2015
Last sequence update: November 11, 2015
Last modified: March 28, 2018
This is version 14 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health