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A4XAL2 (KYNU_SALTO) 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:Strop_3530
OrganismSalinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440) [Complete proteome] [HAMAP]
Taxonomic identifier369723 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeSalinispora

Protein attributes

Sequence length429 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 – 429429Kynureninase HAMAP-Rule MF_01970
PRO_0000357011

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
A4XAL2 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 49393A089963E960

FASTA42946,976
        10         20         30         40         50         60 
MREEELIQEE KAANRLDTAD PGHRHLFHVP PADGGRYQQA AYLAGNSLGL QPRATRDELF 

        70         80         90        100        110        120 
ADLEAWRRLG VEGHLAADRP WLPYHELLTA PTARLVGARP AEVVVMNSLT VNLHLLMVSF 

       130        140        150        160        170        180 
YRPTGVRTRI VIEDSAFPSD SYAVRSQARF HGLDPDSTVV RLAPRPGEDT LRTADVRDLL 

       190        200        210        220        230        240 
AAEGDTIALV LLGGVNYLTG ELMEIPEITA AGRAAGAVVG WDLAHAAGNV PLALHDWDVD 

       250        260        270        280        290        300 
FAAWCSYKYL NSGPGGLSGV FVHERHLADP TLPRFEGWWS TEAATRFEMS PVARPPATAE 

       310        320        330        340        350        360 
AWQVSNPPIL AMGPVRTSLE VFDSVGMTAL RERSVRLTGY LEWLLDQVTP GRPLAVVTPR 

       370        380        390        400        410        420 
DPDRRGAQLS VRIGTGSAAE LAKRLRLEHG VVADAREPDV VRFAPVPLYS TYHDCWRVAD 


ALAATVEVH 

« Hide

References

[1]"Complete sequence of Salinispora tropica CNB-440."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Jensen P.R., Moore B.S., Udwary D.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-916 / DSM 44818 / CNB-440.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000667 Genomic DNA. Translation: ABP55961.1.
RefSeqYP_001160339.1. NC_009380.1.

3D structure databases

ProteinModelPortalA4XAL2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING369723.Strop_3530.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP55961; ABP55961; Strop_3530.
GeneID5060004.
KEGGstp:Strop_3530.
PATRIC23446224. VBISalTro43511_3644.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAWLPYHEL.
OrthoDBEOG6N67XP.
ProtClustDBCLSK2459168.

Enzyme and pathway databases

BioCycSTRO369723:GI49-3575-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_SALTO
AccessionPrimary (citable) accession number: A4XAL2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: May 29, 2007
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