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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.

Catalytic activityi

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

Cofactori

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei97 – 971Pyridoxal phosphate; via amide nitrogen1 PublicationUniRule annotation
Binding sitei98 – 981Pyridoxal phosphate1 PublicationUniRule annotation
Binding sitei172 – 1721Pyridoxal phosphate1 PublicationUniRule annotation
Binding sitei201 – 2011Pyridoxal phosphate1 PublicationUniRule annotation
Binding sitei204 – 2041Pyridoxal phosphate1 PublicationUniRule annotation
Binding sitei226 – 2261Pyridoxal phosphate1 Publication
Binding sitei256 – 2561Pyridoxal phosphate1 Publication
Binding sitei282 – 2821Pyridoxal phosphate1 Publication

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. anthranilate metabolic process Source: UniProtKB-HAMAP
  3. L-kynurenine catabolic process Source: UniProtKB-UniPathway
  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:
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

  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 – 416416KynureninasePRO_0000357010Add
BLAST

Amino acid modifications

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

Interactioni

Subunit structurei

Homodimer.1 PublicationUniRule annotation

Structurei

Secondary structure

1
416
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 129Combined sources
Helixi17 – 226Combined sources
Turni34 – 363Combined sources
Helixi44 – 5310Combined sources
Helixi54 – 596Combined sources
Helixi60 – 623Combined sources
Helixi63 – 664Combined sources
Helixi69 – 713Combined sources
Helixi72 – 8110Combined sources
Turni82 – 854Combined sources
Beta strandi90 – 934Combined sources
Helixi97 – 11519Combined sources
Beta strandi121 – 1255Combined sources
Helixi130 – 14314Combined sources
Beta strandi148 – 1547Combined sources
Helixi155 – 1573Combined sources
Helixi158 – 1614Combined sources
Beta strandi166 – 1749Combined sources
Turni176 – 1783Combined sources
Helixi184 – 19411Combined sources
Beta strandi197 – 2015Combined sources
Turni203 – 2086Combined sources
Helixi213 – 2164Combined sources
Beta strandi219 – 2235Combined sources
Beta strandi225 – 2273Combined sources
Beta strandi238 – 2414Combined sources
Turni243 – 2486Combined sources
Helixi256 – 2583Combined sources
Helixi275 – 2784Combined sources
Helixi285 – 29814Combined sources
Helixi303 – 32523Combined sources
Helixi338 – 3403Combined sources
Beta strandi343 – 3486Combined sources
Helixi352 – 3609Combined sources
Turni361 – 3633Combined sources
Beta strandi367 – 3693Combined sources
Turni370 – 3723Combined sources
Beta strandi373 – 3775Combined sources
Turni380 – 3823Combined sources
Helixi385 – 40117Combined sources
Turni402 – 4043Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QZ9X-ray1.85A1-416[»]
ProteinModelPortaliP83788.
SMRiP83788. Positions 2-405.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83788.

Family & Domainsi

Region

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

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.
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
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_dom.
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: November 26, 2014
This is version 52 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