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

A5FMM4 (KYNU_FLAJ1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:Fjoh_0506
OrganismFlavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) (Cytophaga johnsonae) [Complete proteome] [HAMAP]
Taxonomic identifier376686 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeFlavobacterium

Protein attributes

Sequence length425 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 – 425425Kynureninase HAMAP-Rule MF_01970
PRO_0000357005

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
A5FMM4 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 0070DB3521B3E741

FASTA42548,720
        10         20         30         40         50         60 
MTFQNTREFA KQLDAQDALN HYQEQFIFPK VNDKRVIYFT GNSLGLQPKR TKAYIDEVMN 

        70         80         90        100        110        120 
DWAELAVEGH FYAEKPWWDY QERFSEPLSK IVGALPSEVT VMNTLTVNLH LLMVSFYQPK 

       130        140        150        160        170        180 
GKRYKIICEE KAFPSDQYMF QSQVHFHGYK PEDAIVEIKR REGEHNIRLE DVLAKIEEVG 

       190        200        210        220        230        240 
DELALVLIGG VNYYTGQVFD IKTITAAGQK AGAKVGWDLA HAAGNIKLEL HDWNVDFAAW 

       250        260        270        280        290        300 
CSYKYMNSGP GNASGVFVHE RHHNDPDLPR FAGWWGHNKE RRFKMEPNFD PVHGAGGWQI 

       310        320        330        340        350        360 
SNLPVLSLAP YLASVEMFAE VGMDALIAKR DHITSYLEFI LHEIDKEVES TFEIITPSNP 

       370        380        390        400        410        420 
EERASQLSVF LHGEGRSLFD YLMKNGVITD WREPNVIRLA PVPLYCSYED MYDFGQILKK 


GILGK 

« Hide

References

[1]"Novel features of the polysaccharide-digesting gliding bacterium Flavobacterium johnsoniae as revealed by genome sequence analysis."
McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G., Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R., Cheng Y.Q., Stein J.L.
Appl. Environ. Microbiol. 75:6864-6875(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17061 / DSM 2064 / UW101.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000685 Genomic DNA. Translation: ABQ03541.1.
RefSeqYP_001192860.1. NC_009441.1.

3D structure databases

ProteinModelPortalA5FMM4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING376686.Fjoh_0506.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ03541; ABQ03541; Fjoh_0506.
GeneID5089819.
KEGGfjo:Fjoh_0506.
PATRIC21895273. VBIFlaJoh53613_0523.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAVWDLAHS.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycFJOH376686:GIXN-525-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_FLAJ1
AccessionPrimary (citable) accession number: A5FMM4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: June 12, 2007
Last modified: May 14, 2014
This is version 50 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