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P83788

- KYNU_PSEFL

UniProt

P83788 - KYNU_PSEFL

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Protein
Kynureninase
Gene
kynU
Organism
Pseudomonas fluorescens
Status
Reviewed - 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.UniRule annotation

Catalytic activityi

L-kynurenine + H2O = anthranilate + L-alanine.1 Publication
L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.1 Publication

Cofactori

Pyridoxal phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei97 – 971Pyridoxal phosphate; via amide nitrogen
Binding sitei98 – 981Pyridoxal phosphate
Binding sitei172 – 1721Pyridoxal phosphate
Binding sitei201 – 2011Pyridoxal phosphate
Binding sitei204 – 2041Pyridoxal phosphate
Binding sitei226 – 2261Pyridoxal phosphate Inferred
Binding sitei256 – 2561Pyridoxal phosphate Inferred
Binding sitei282 – 2821Pyridoxal phosphate Inferred

GO - Molecular functioni

  1. kynureninase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
  2. L-kynurenine catabolic process Source: UniProtKB-UniPathway
  3. anthranilate metabolic process Source: UniProtKB-HAMAP
  4. quinolinate biosynthetic process Source: UniProtKB-HAMAP
  5. tryptophan catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Kynureninase (EC:3.7.1.3)
Alternative name(s):
L-kynurenine hydrolase
Gene namesi
Name:kynU
OrganismiPseudomonas fluorescens
Taxonomic identifieri294 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi132 – 1321D → A: Reduces binding to pyridoxal phosphate and strongly reduces catalytic activity. 1 Publication
Mutagenesisi132 – 1321D → E: Enhances binding to pyridoxal phosphate. 1 Publication
Mutagenesisi201 – 2011D → E: Enhances binding to pyridoxal phosphate. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416KynureninaseUniRule annotation
PRO_0000357010Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei227 – 2271N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 129
Helixi17 – 226
Turni34 – 363
Helixi44 – 5310
Helixi54 – 596
Helixi60 – 623
Helixi63 – 664
Helixi69 – 713
Helixi72 – 8110
Turni82 – 854
Beta strandi90 – 934
Helixi97 – 11519
Beta strandi121 – 1255
Helixi130 – 14314
Beta strandi148 – 1547
Helixi155 – 1573
Helixi158 – 1614
Beta strandi166 – 1749
Turni176 – 1783
Helixi184 – 19411
Beta strandi197 – 2015
Turni203 – 2086
Helixi213 – 2164
Beta strandi219 – 2235
Beta strandi225 – 2273
Beta strandi238 – 2414
Turni243 – 2486
Helixi256 – 2583
Helixi275 – 2784
Helixi285 – 29814
Helixi303 – 32523
Helixi338 – 3403
Beta strandi343 – 3486
Helixi352 – 3609
Turni361 – 3633
Beta strandi367 – 3693
Turni370 – 3723
Beta strandi373 – 3775
Turni380 – 3823
Helixi385 – 40117
Turni402 – 4043

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QZ9X-ray1.85A1-416[»]
ProteinModelPortaliP83788.
SMRiP83788. Positions 2-405.

Miscellaneous databases

EvolutionaryTraceiP83788.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni129 – 1324Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V/Cys_dSase.
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

MTTRNDCLAL DAQDSLAPLR QQFALPEGVI YLDGNSLGAR PVAALARAQA    50
VIAEEWGNGL IRSWNSAGWR DLSERLGNRL ATLIGARDGE VVVTDTTSIN 100
LFKVLSAALR VQATRSPERR VIVTETSNFP TDLYIAEGLA DMLQQGYTLR 150
LVDSPEELPQ AIDQDTAVVM LTHVNYKTGY MHDMQALTAL SHECGALAIW 200
DLAHSAGAVP VDLHQAGADY AIGCTYKYLN GGPGSQAFVW VSPQLCDLVP 250
QPLSGWFGHS RQFAMEPRYE PSNGIARYLC GTQPITSLAM VECGLDVFAQ 300
TDMASLRRKS LALTDLFIEL VEQRCAAHEL TLVTPREHAK RGSHVSFEHP 350
EGYAVIQALI DRGVIGDYRE PRIMRFGFTP LYTTFTEVWD AVQILGEILD 400
RKTWAQAQFQ VRHSVT 416
Length:416
Mass (Da):45,905
Last modified:March 15, 2004 - v1
Checksum:i50C3DE62A20C779D
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QZ9 X-ray 1.85 A 1-416 [» ]
ProteinModelPortali P83788.
SMRi P83788. Positions 2-405.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00329 .
UPA00334 ; UER00455 .
BioCyci MetaCyc:MONOMER-7065.
SABIO-RK P83788.

Miscellaneous databases

EvolutionaryTracei P83788.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPi MF_01970. Kynureninase.
InterProi IPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
PANTHERi PTHR14084. PTHR14084. 1 hit.
Pfami PF00266. Aminotran_5. 1 hit.
[Graphical view ]
PIRSFi PIRSF038800. KYNU. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR01814. kynureninase. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Three-dimensional structure of kynureninase from Pseudomonas fluorescens."
    Momany C., Levdikov V., Blagova L., Lima S., Phillips R.S.
    Biochemistry 43:1193-1203(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, CATALYTIC ACTIVITY, HOMODIMERIZATION, MUTAGENESIS OF ASP-132 AND ASP-201.

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: February 19, 2014
This is version 49 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

External Data

Dasty 3

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