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B1KJM4 (KYNU_SHEWM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:Swoo_1405
OrganismShewanella woodyi (strain ATCC 51908 / MS32) [Complete proteome] [HAMAP]
Taxonomic identifier392500 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length430 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 – 430430Kynureninase HAMAP-Rule MF_01970
PRO_0000357012

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
B1KJM4 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: BCF6BDB84CF10CDC

FASTA43048,545
        10         20         30         40         50         60 
MIFENTLAFA QQQDRNDPLA HYSDQFHHPV IDGKEVLYFT GNSLGLQPKT AKEHINQELE 

        70         80         90        100        110        120 
DWAKWGVEGH FHAVNPWVSY HEILTPASAE LVGANESEVV CMNSLTTNLH LLFVSFYKPT 

       130        140        150        160        170        180 
AKRFKIISEA KMFPSDRYLL ETQVRHHGLD PDDAIIEISP REGEYLIREE DIIAAVNDNA 

       190        200        210        220        230        240 
DELALLFFGG VNYFTGQLFD MQRLTKAAHG VGALAGFDLA HAVGNVPMHL HDWDVDFAAW 

       250        260        270        280        290        300 
CTYKYLNSSA GNVGGIFVND RHGNNTKINR FGGWWGHNKE RRFLMENSFE PMTGAEGWQI 

       310        320        330        340        350        360 
SNAPVMGMAI LKSSLDIFHE AGIENLRAKS LKLTAYLEFV FNDIVNQFTD IKLEIITPTD 

       370        380        390        400        410        420 
PTQRGCQLSI KLVGTNKEFF EALTKAGVIA DFREPDVIRL APTPLYNSFE DVYLLGQTLK 

       430 
VLAQNWRQHG 

« Hide

References

[1]"Complete sequence of Shewanella woodyi ATCC 51908."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Zhao J.-S., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51908 / MS32.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000961 Genomic DNA. Translation: ACA85697.1.
RefSeqYP_001759792.1. NC_010506.1.

3D structure databases

ProteinModelPortalB1KJM4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING392500.Swoo_1405.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA85697; ACA85697; Swoo_1405.
GeneID6115645.
KEGGswd:Swoo_1405.
PATRIC23605145. VBISheWoo126588_1463.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAHEAGIEN.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycSWOO392500:GI2C-1428-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_SHEWM
AccessionPrimary (citable) accession number: B1KJM4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: April 29, 2008
Last modified: May 14, 2014
This is version 46 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