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Protein

Kynureninase

Gene

kynU

Organism
Achromobacter xylosoxidans (strain A8)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-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-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)
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)
  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 sitei201Pyridoxal phosphateUniRule annotation1
Binding sitei204Pyridoxal phosphateUniRule annotation1
Binding sitei226Pyridoxal phosphateUniRule annotation1
Binding sitei256Pyridoxal phosphateUniRule annotation1
Binding sitei282Pyridoxal phosphateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolaseUniRule annotationImported
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 annotationImported
Ordered Locus Names:AXYL_05263Imported
OrganismiAchromobacter xylosoxidans (strain A8)Imported
Taxonomic identifieri762376 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeAchromobacter
Proteomesi
  • UP000006876 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei227N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi762376.AXYL_05263.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini155 – 351Aminotran_5InterPro annotationAdd BLAST197

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni129 – 132Pyridoxal phosphate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CKY. Bacteria.
COG3844. LUCA.
HOGENOMiHOG000242437.
KOiK01556.
OMAiVCSLHAS.
OrthoDBiPOG091H0D63.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase. 1 hit.
InterProiView protein in InterPro
IPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_sub2.
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.

E3HSW2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTRDACVNA DRQDPLAPLK DRFDLPPGVL YMDGNSLGVL PKDAAARAAA
60 70 80 90 100
VIGQEWGTGL IRSWNTAGWF ELPARLGDKL GRLLGAREGE LVVTDTTSLN
110 120 130 140 150
IFKALAAALR IQQHQHPQRR VILSERDNFP TDLYMIQGMI DLLQQGYEMR
160 170 180 190 200
LIDDELPLEK ALDESVAVML LSHVNYRSGQ MHDMAAVTAL AHERGALAIW
210 220 230 240 250
DLAHAAGAVP VDLNGANADF AVGCTYKYLN GGPGSPAFIW VAPRHTKDFW
260 270 280 290 300
QPLSGWWGHT RPFDMAVAYE PAGGVRRYLC GTQPIVSLSL VECGLDVAHA
310 320 330 340 350
ADMAEVRKKS LALGDLFIAL VEERCAEHPL TLVTPRKHAD RGSHVSFRHP
360 370 380 390 400
NGFEVMQALI ARGVIGDYRE PEVLRFGLTP LYFGYADVWD AVDILKDVLD
410
TRSWDKPEFK HRAAVT
Length:416
Mass (Da):45,951
Last modified:January 11, 2011 - v1
Checksum:iAE2B2EED914FF224
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002287 Genomic DNA. Translation: ADP18563.1.
RefSeqiWP_013395866.1. NC_014640.1.

Genome annotation databases

EnsemblBacteriaiADP18563; ADP18563; AXYL_05263.
KEGGiaxy:AXYL_05263.
PATRICifig|762376.5.peg.5263.

Similar proteinsi

Entry informationi

Entry nameiE3HSW2_ACHXA
AccessioniPrimary (citable) accession number: E3HSW2
Entry historyiIntegrated into UniProtKB/TrEMBL: January 11, 2011
Last sequence update: January 11, 2011
Last modified: September 27, 2017
This is version 49 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation

Keywords - Technical termi

Complete proteomeImported