Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q62M98 (KYNU_BURMA)

Last modified November 3, 2009. Version 33. 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

Hide | Top

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: BMA0352
OrganismBurkholderia mallei (Pseudomonas mallei) [Complete proteome] [HAMAP]
Taxonomic identifier13373 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Hide | Top

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

Hide | Top

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.

Hide | Top

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...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Kynureninase
PRO_0000356997

Regions

Region129 – 1324Pyridoxal phosphate binding By similarity

Sites

Binding site971Pyridoxal phosphate; via amide nitrogen By similarity
Binding site981Pyridoxal phosphate By similarity
Binding site2011Pyridoxal phosphate By similarity
Binding site2041Pyridoxal phosphate By similarity
Binding site2261Pyridoxal phosphate By similarity
Binding site2561Pyridoxal phosphate By similarity
Binding site2821Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2271N6-(pyridoxal phosphate)lysine By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q62M98-1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 35E6734AC426EE17

FASTA41645,922
        10         20         30         40         50         60 
MKTREEALAL DRDDPLAPLR EQFALPAGVI YLDGNSLGAQ PRAAAARAQQ VIGAEWGEGL 

        70         80         90        100        110        120 
IRSWNTAGWF ALPRRLGDRL APLIGAADDE VAITDTISIN LFKLLAAMLR HQARHAPKRR 

       130        140        150        160        170        180 
VIVSERSNFP TDLYIAQGLI AQLDRDYELR LIDDPADLPD ALDDETAVAM ITHVNYRTGY 

       190        200        210        220        230        240 
MHDMPSVTQT VRQAGALMLW DLAHSAGAVP VDLNGALADG AVGCTYKYLN GGPGSPAFVW 

       250        260        270        280        290        300 
VPKRHQRAFE QPLSGWWGHR APFAMQPAFE PDPGIARFLC GTQPIVSMSM VECGLDVFAQ 

       310        320        330        340        350        360 
TDMHAIRRKS LALTDAFVAL VESRCAGQPL KLVTPRAHHQ RGSQASFEHP HGYEVMQALI 

       370        380        390        400        410 
ARGVIGDYRE PRILRFGFTP LYTRFVDVWD AVETLRDILD TEAWRAPEFA TRAAVT

« Hide

Hide | Top

Cross-references

Sequence databases

CP000010 Genomic DNA. Translation: AAU49147.1.
RefSeqYP_102170.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3088987.
GenomeReviewsGene locus BMA0352 in contig CP000010_GR.
KEGGbma:BMA0352.
TIGRBMA0352.

Phylogenomic databases

HOGENOMQ62M98.
OMAWQPLSGW.

Enzyme and pathway databases

BioCycBMAL243160:BMA_0352-MON.

Family and domain databases

InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
PANTHERPTHR14084. Kynureninase. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Hide | Top

Entry information

Entry nameKYNU_BURMA
AccessionPrimary (citable) accession number: Q62M98
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: October 25, 2004
Last modified: November 3, 2009
This is version 33 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)

Hide | Top

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