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Reviewed, UniProtKB/Swiss-Prot A4IT57 (KYNU_GEOTN)

Last modified September 22, 2009. Version 20. 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: GTNG_3166
OrganismGeobacillus thermodenitrificans (strain NG80-2) [Complete proteome] [HAMAP]
Taxonomic identifier420246 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length428 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 – 428428Kynureninase
PRO_0000357007

Regions

Region132 – 1354Pyridoxal phosphate binding By similarity

Sites

Binding site1041Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1051Pyridoxal phosphate By similarity
Binding site2131Pyridoxal phosphate By similarity
Binding site2161Pyridoxal phosphate By similarity
Binding site2381Pyridoxal phosphate By similarity
Binding site2671Pyridoxal phosphate By similarity
Binding site2951Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2391N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4IT57-1 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: 19579C1F454D452B

FASTA42848,333
        10         20         30         40         50         60 
MNSTALEPTL EFARKLDQED PLRHFRDEFY LPPNSIYMDG NSLGLLSKRA EKTLFTILQD 

        70         80         90        100        110        120 
WKLLGIDGWT KGTYPWFDLS EKIGAMLAPL VGASPEEVIA TGSTTVNLHQ LVSTFYQPEG 

       130        140        150        160        170        180 
KRTKILADEL TFPSDIYALQ SQLRIHGYDP STHLIRVKSR DGRFLEEEDI IAAMSEDVAL 

       190        200        210        220        230        240 
VVLPTVLYRS GQILDIQLLT DEAHKRGILI GFDACHSIGA IPHSFSEWGV DFAFWCNYKY 

       250        260        270        280        290        300 
MNGGPGCVAG LYVHRKHFGS APGLAGWFGS KKDKQFDMEH TFTPSLTAGA YQIGTPHLLS 

       310        320        330        340        350        360 
LAPLIGSLEI FQEAGIERIR QKSLQLTNYF MYLIEQELSH FGFIIGNPKD DVRRGGHISL 

       370        380        390        400        410        420 
EHEEAARICK SLKENGVIPD FRAPNIIRLA PIALYTSYEE VWNVVQIMKK IMQEKQYKKF 


SNEREVVA 

« Hide

References

[1]"Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir."
Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., Han W., Peng X., Liu R., Wang L.
Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007) [PubMed: 17372208] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000557 Genomic DNA. Translation: ABO68511.1. Different initiation.
RefSeqYP_001127256.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA4IT57.

Genome annotation databases

GeneID4968092.
GenomeReviewsGene locus GTNG_3166 in contig CP000557_GR.
KEGGgtn:GTNG_3166.
NMPDRfig|420246.5.peg.3029.

Organism-specific databases

CMRSearch...

Family and domain databases

InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU_GEOTN
AccessionPrimary (citable) accession number: A4IT57
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 16, 2008
Last modified: September 22, 2009
This is version 20 of the entry and version 2 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