Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B2FL97 (KYNU_STRMK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kynureninase

EC=3.7.1.3
Alternative name(s):
L-kynurenine hydrolase
Gene names
Name:kynU
Ordered Locus Names:Smlt3160
OrganismStenotrophomonas maltophilia (strain K279a) [Complete proteome] [HAMAP]
Taxonomic identifier522373 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01970

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine. HAMAP-Rule MF_01970

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. HAMAP-Rule MF_01970

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01970

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. HAMAP-Rule MF_01970

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. HAMAP-Rule MF_01970

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01970

Sequence similarities

Belongs to the kynureninase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424Kynureninase HAMAP-Rule MF_01970
PRO_0000357013

Regions

Region133 – 1364Pyridoxal phosphate binding By similarity

Sites

Binding site1051Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1061Pyridoxal phosphate By similarity
Binding site2181Pyridoxal phosphate By similarity
Binding site2211Pyridoxal phosphate By similarity
Binding site2431Pyridoxal phosphate By similarity
Binding site2741Pyridoxal phosphate By similarity
Binding site3021Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2441N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B2FL97 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 9B81C2D46958FDC4

FASTA42446,800
        10         20         30         40         50         60 
MSDLLSRTHA IALDAADPLR PLRNEFLIPR HGGGEQTYFV GNSLGLQPRG AQAAVQEVMK 

        70         80         90        100        110        120 
QWGELAVEGH FTGPTQWLSY HRLVSAQLAR VVGALPSEVV AMNTLSVNLH LMMVSFYRPT 

       130        140        150        160        170        180 
AQRPVILMEA GAFPTDRHAV EAQIRFHGFD PAECLVEVQP DEANGTISLT AIERAIAEHG 

       190        200        210        220        230        240 
PRLALVLWPG VQYRTGQAFD LDAITRAARL QGARIGFDLA HSVGNLPLRL HDVAPDFAVW 

       250        260        270        280        290        300 
CHYKYLNSGP GAVAGAFVHE RHHRDTTLPR FAGWWGHEEA TRFQMAPQFT PAIGAEGWQL 

       310        320        330        340        350        360 
SNPPILGLAP LRASLDLFER AGMEALRSKS LALTGMLEAL VRARLSGVLD IITPAEPQRR 

       370        380        390        400        410        420 
GCQLSLRVIG GRERGRALFE HLRGIGVLGD WREPDVIRIS PTPLYNRYLD VHHFVEEVEA 


WAGL 

« Hide

References

[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM743169 Genomic DNA. Translation: CAQ46604.1.
RefSeqYP_001972895.1. NC_010943.1.

3D structure databases

ProteinModelPortalB2FL97.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING522373.Smlt3160.

Proteomic databases

PRIDEB2FL97.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ46604; CAQ46604; Smlt3160.
GeneID6391370.
KEGGsml:Smlt3160.
PATRIC23701787. VBISteMal45202_2956.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAYLATWRT.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycSMAL522373:GJE8-3057-MONOMER.
UniPathwayUPA00253; UER00329.
UPA00334; UER00455.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_01970. Kynureninase.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR14084. PTHR14084. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF038800. KYNU. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU_STRMK
AccessionPrimary (citable) accession number: B2FL97
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways