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

Q1ITW5 (KYNU_KORVE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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:Acid345_0680
OrganismKoribacter versatilis (strain Ellin345) [Reference proteome] [HAMAP]
Taxonomic identifier204669 [NCBI]
Taxonomic lineageBacteriaAcidobacteriaCandidatus Koribacter

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_0000356985

Regions

Region137 – 1404Pyridoxal phosphate binding By similarity

Sites

Binding site1091Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1101Pyridoxal phosphate By similarity
Binding site2221Pyridoxal phosphate By similarity
Binding site2251Pyridoxal phosphate By similarity
Binding site2471Pyridoxal phosphate By similarity
Binding site2781Pyridoxal phosphate By similarity
Binding site3061Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2481N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1ITW5 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: DDE23AF052AE8A83

FASTA42447,776
        10         20         30         40         50         60 
MAAAAFDTTE NFAIEMDARD PMSRFRGRFH IPPAPDGSAS VYLVGHSLGL QPKTVRAYLE 

        70         80         90        100        110        120 
QELKDWETLG VEGHFRGKHP WMPYHRLLTE QTARLVCAQP SEVVVMNSLT VNLHLMMVSF 

       130        140        150        160        170        180 
YRPTRERHNI LIEGSAFPSD QYAVQSQIKF HGFDPASSLL ELCPRVGEAT MRDEDILELI 

       190        200        210        220        230        240 
EREGQSIALI LLGGVNYATG QAFDMAEITK AGHAQGCVVA FDCAHAAGNL ELKLHEWDVD 

       250        260        270        280        290        300 
WAAWCSYKYL NGGPGCIGGC FVHERYARDF ELPRFAGWWG HDQETRFKMG PEFHPMAGAE 

       310        320        330        340        350        360 
GWQLSNPSIL TMAALRASME IFDEAGIGKL RQRSIALTGY LEFLLDQQKS ARFEIITPRE 

       370        380        390        400        410        420 
PERRGAQLSI RVAAGNRSVC DRLVEEGALC DWREPDILRV APVPLYCSYR DCYRFVQRFV 


ANLN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000360 Genomic DNA. Translation: ABF39685.1.
RefSeqYP_589759.1. NC_008009.1.

3D structure databases

ProteinModelPortalQ1ITW5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING204669.Acid345_0680.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF39685; ABF39685; Acid345_0680.
GeneID4068770.
KEGGaba:Acid345_0680.
PATRIC31978152. VBICanKor57425_0727.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAVWDLAHS.
OrthoDBEOG6N67XP.
ProtClustDBCLSK2486953.

Enzyme and pathway databases

BioCycKVER204669:GHL8-687-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_KORVE
AccessionPrimary (citable) accession number: Q1ITW5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: June 13, 2006
Last modified: February 19, 2014
This is version 55 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