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Protein

Kynureninase

Gene

kynU

Organism
Stenotrophomonas maltophilia (strain K279a)
Status
Reviewed-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-kynurenine + H2O = anthranilate + L-alanine.UniRule annotation
L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei105 – 1051Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei106 – 1061Pyridoxal phosphateUniRule annotation
Binding sitei218 – 2181Pyridoxal phosphateUniRule annotation
Binding sitei221 – 2211Pyridoxal phosphateUniRule annotation
Binding sitei243 – 2431Pyridoxal phosphateUniRule annotation
Binding sitei274 – 2741Pyridoxal phosphateUniRule annotation
Binding sitei302 – 3021Pyridoxal phosphateUniRule annotation

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

BioCyciSMAL522373:GJE8-3057-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
ProteomesiUP000008840: Chromosome

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424KynureninasePRO_0000357013Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei244 – 2441N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiB2FL97.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi522373.Smlt3160.

Structurei

3D structure databases

ProteinModelPortaliB2FL97.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni133 – 1364Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242438.
KOiK01556.
OMAiRFWQPLS.
OrthoDBiEOG6N67XP.

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.

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.
YP_001972895.1. NC_010943.1.

Genome annotation databases

EnsemblBacteriaiCAQ46604; CAQ46604; Smlt3160.
GeneIDi6391370.
KEGGisml:Smlt3160.
PATRICi23701787. VBISteMal45202_2956.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM743169 Genomic DNA. Translation: CAQ46604.1.
RefSeqiWP_012480764.1. NC_010943.1.
YP_001972895.1. NC_010943.1.

3D structure databases

ProteinModelPortaliB2FL97.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi522373.Smlt3160.

Proteomic databases

PRIDEiB2FL97.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAQ46604; CAQ46604; Smlt3160.
GeneIDi6391370.
KEGGisml:Smlt3160.
PATRICi23701787. VBISteMal45202_2956.

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242438.
KOiK01556.
OMAiRFWQPLS.
OrthoDBiEOG6N67XP.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.
BioCyciSMAL522373:GJE8-3057-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

  1. "The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
    Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A.
    , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
    Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K279a.

Entry informationi

Entry nameiKYNU_STRMK
AccessioniPrimary (citable) accession number: B2FL97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: June 10, 2008
Last modified: February 4, 2015
This is version 50 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.