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Protein

Kynureninase

Gene

kynU

Organism
Pseudomonas fluorescens
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.

Catalytic activityi

L-kynurenine + H2O = anthranilate + L-alanine.UniRule annotation1 Publication
L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation1 Publication

Cofactori

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), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (HZ99_03140)
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), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (HZ99_03140)
  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 Publication1
Binding sitei98Pyridoxal phosphateUniRule annotation1 Publication1
Binding sitei172Pyridoxal phosphateUniRule annotation1 Publication1
Binding sitei201Pyridoxal phosphateUniRule annotation1 Publication1
Binding sitei204Pyridoxal phosphateUniRule annotation1 Publication1
Binding sitei226Pyridoxal phosphate1 Publication1
Binding sitei256Pyridoxal phosphate1 Publication1
Binding sitei282Pyridoxal phosphate1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-7065.
BRENDAi3.7.1.3. 5121.
SABIO-RKP83788.
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
OrganismiPseudomonas fluorescens
Taxonomic identifieri294 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi132D → A: Reduces binding to pyridoxal phosphate and strongly reduces catalytic activity. 1 Publication1
Mutagenesisi132D → E: Enhances binding to pyridoxal phosphate. 1 Publication1
Mutagenesisi201D → E: Enhances binding to pyridoxal phosphate. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003570101 – 416KynureninaseAdd BLAST416

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei227N6-(pyridoxal phosphate)lysine1

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Structurei

Secondary structure

1416
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 12Combined sources9
Helixi17 – 22Combined sources6
Turni34 – 36Combined sources3
Helixi44 – 53Combined sources10
Helixi54 – 59Combined sources6
Helixi60 – 62Combined sources3
Helixi63 – 66Combined sources4
Helixi69 – 71Combined sources3
Helixi72 – 81Combined sources10
Turni82 – 85Combined sources4
Beta strandi90 – 93Combined sources4
Helixi97 – 115Combined sources19
Beta strandi121 – 125Combined sources5
Helixi130 – 143Combined sources14
Beta strandi148 – 154Combined sources7
Helixi155 – 157Combined sources3
Helixi158 – 161Combined sources4
Beta strandi166 – 174Combined sources9
Turni176 – 178Combined sources3
Helixi184 – 194Combined sources11
Beta strandi197 – 201Combined sources5
Turni203 – 208Combined sources6
Helixi213 – 216Combined sources4
Beta strandi219 – 223Combined sources5
Beta strandi225 – 227Combined sources3
Beta strandi238 – 241Combined sources4
Turni243 – 248Combined sources6
Helixi256 – 258Combined sources3
Helixi275 – 278Combined sources4
Helixi285 – 298Combined sources14
Helixi303 – 325Combined sources23
Helixi338 – 340Combined sources3
Beta strandi343 – 348Combined sources6
Helixi352 – 360Combined sources9
Turni361 – 363Combined sources3
Beta strandi367 – 369Combined sources3
Turni370 – 372Combined sources3
Beta strandi373 – 377Combined sources5
Turni380 – 382Combined sources3
Helixi385 – 401Combined sources17
Turni402 – 404Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QZ9X-ray1.85A1-416[»]
ProteinModelPortaliP83788.
SMRiP83788.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83788.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni129 – 132Pyridoxal phosphate binding4

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.

Sequencei

Sequence statusi: Complete.

P83788-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTRNDCLAL DAQDSLAPLR QQFALPEGVI YLDGNSLGAR PVAALARAQA
60 70 80 90 100
VIAEEWGNGL IRSWNSAGWR DLSERLGNRL ATLIGARDGE VVVTDTTSIN
110 120 130 140 150
LFKVLSAALR VQATRSPERR VIVTETSNFP TDLYIAEGLA DMLQQGYTLR
160 170 180 190 200
LVDSPEELPQ AIDQDTAVVM LTHVNYKTGY MHDMQALTAL SHECGALAIW
210 220 230 240 250
DLAHSAGAVP VDLHQAGADY AIGCTYKYLN GGPGSQAFVW VSPQLCDLVP
260 270 280 290 300
QPLSGWFGHS RQFAMEPRYE PSNGIARYLC GTQPITSLAM VECGLDVFAQ
310 320 330 340 350
TDMASLRRKS LALTDLFIEL VEQRCAAHEL TLVTPREHAK RGSHVSFEHP
360 370 380 390 400
EGYAVIQALI DRGVIGDYRE PRIMRFGFTP LYTTFTEVWD AVQILGEILD
410
RKTWAQAQFQ VRHSVT
Length:416
Mass (Da):45,905
Last modified:March 15, 2004 - v1
Checksum:i50C3DE62A20C779D
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QZ9X-ray1.85A1-416[»]
ProteinModelPortaliP83788.
SMRiP83788.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.
BioCyciMetaCyc:MONOMER-7065.
BRENDAi3.7.1.3. 5121.
SABIO-RKP83788.

Miscellaneous databases

EvolutionaryTraceiP83788.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiKYNU_PSEFL
AccessioniPrimary (citable) accession number: P83788
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: March 15, 2004
Last modified: November 2, 2016
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.