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Reviewed, UniProtKB/Swiss-Prot A5FMM4 (KYNU_FLAJ1)

Last modified November 3, 2009. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 lineageBacteriaBacteroidetesFlavobacteriaFlavobacterialesFlavobacteriaceaeFlavobacterium

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine.

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

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

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

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the kynureninase family.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   LigandPyridoxal phosphate
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processNAD biosynthetic process

Inferred from electronic annotation. Source: InterPro

tryptophan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functionkynureninase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 425425Kynureninase
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
A5FMM4-1 [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]"Complete sequence of Flavobacterium johnsoniae UW101."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E., Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Xie G., McBride M., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000685 Genomic DNA. Translation: ABQ03541.1.
RefSeqYP_001192860.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5FMM4.

Genome annotation databases

GeneID5089819.
GenomeReviewsGene locus Fjoh_0506 in contig CP000685_GR.
KEGGfjo:Fjoh_0506.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMANLHLLLX.

Family and domain databases

InterProIPR010111. Kynureninase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR14084. Kynureninase. 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: November 3, 2009
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents