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Protein

Kynureninase

Gene

kynU

Organism
Stenotrophomonas maltophilia (strain K279a)
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 (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. Kynurenine 3-monooxygenase (kmo)
  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 sitei105Pyridoxal phosphate; via amide nitrogenUniRule annotation1
Binding sitei106Pyridoxal phosphateUniRule annotation1
Binding sitei218Pyridoxal phosphateUniRule annotation1
Binding sitei221Pyridoxal phosphateUniRule annotation1
Binding sitei243Pyridoxal phosphateUniRule annotation1
Binding sitei274Pyridoxal phosphateUniRule annotation1
Binding sitei302Pyridoxal phosphateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processPyridine nucleotide biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciSMAL522373:G1GK1-4986-MONOMER
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
Ordered Locus Names:Smlt3160
OrganismiStenotrophomonas maltophilia (strain K279a)
Taxonomic identifieri522373 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group
Proteomesi
  • UP000008840 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003570131 – 424KynureninaseAdd BLAST424

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei244N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi522373.Smlt3160

Structurei

3D structure databases

ProteinModelPortaliB2FL97
SMRiB2FL97
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni133 – 136Pyridoxal phosphate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CKY Bacteria
COG3844 LUCA
HOGENOMiHOG000242438
KOiK01556
OMAiVCSLHAS

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.

B2FL97-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDLLSRTHA IALDAADPLR PLRNEFLIPR HGGGEQTYFV GNSLGLQPRG
60 70 80 90 100
AQAAVQEVMK QWGELAVEGH FTGPTQWLSY HRLVSAQLAR VVGALPSEVV
110 120 130 140 150
AMNTLSVNLH LMMVSFYRPT AQRPVILMEA GAFPTDRHAV EAQIRFHGFD
160 170 180 190 200
PAECLVEVQP DEANGTISLT AIERAIAEHG PRLALVLWPG VQYRTGQAFD
210 220 230 240 250
LDAITRAARL QGARIGFDLA HSVGNLPLRL HDVAPDFAVW CHYKYLNSGP
260 270 280 290 300
GAVAGAFVHE RHHRDTTLPR FAGWWGHEEA TRFQMAPQFT PAIGAEGWQL
310 320 330 340 350
SNPPILGLAP LRASLDLFER AGMEALRSKS LALTGMLEAL VRARLSGVLD
360 370 380 390 400
IITPAEPQRR GCQLSLRVIG GRERGRALFE HLRGIGVLGD WREPDVIRIS
410 420
PTPLYNRYLD VHHFVEEVEA WAGL
Length:424
Mass (Da):46,800
Last modified:June 10, 2008 - v1
Checksum:i9B81C2D46958FDC4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM743169 Genomic DNA Translation: CAQ46604.1
RefSeqiWP_012480764.1, NC_010943.1

Genome annotation databases

EnsemblBacteriaiCAQ46604; CAQ46604; Smlt3160
GeneIDi6391370
KEGGisml:Smlt3160
PATRICifig|522373.3.peg.2956

Similar proteinsi

Entry informationi

Entry nameiKYNU_STRMK
AccessioniPrimary (citable) accession number: B2FL97
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: June 10, 2008
Last modified: May 23, 2018
This is version 63 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

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