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A4IT57 (KYNU_GEOTN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:GTNG_3166
OrganismGeobacillus thermodenitrificans (strain NG80-2) [Complete proteome] [HAMAP]
Taxonomic identifier420246 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length428 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 caution

The sequence ABO68511.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Kynureninase HAMAP-Rule MF_01970
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 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NG80-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000557 Genomic DNA. Translation: ABO68511.1. Different initiation.
RefSeqYP_001127256.1. NC_009328.1.

3D structure databases

ProteinModelPortalA4IT57.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING420246.GTNG_3166.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO68511; ABO68511; GTNG_3166.
GeneID4968092.
KEGGgtn:GTNG_3166.
PATRIC21982971. VBIGeoThe136879_3328.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OrthoDBEOG6N67XP.
ProtClustDBCLSK904618.

Enzyme and pathway databases

BioCycGTHE420246:GIXT-3262-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_GEOTN
AccessionPrimary (citable) accession number: A4IT57
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 16, 2008
Last modified: February 19, 2014
This is version 51 of the entry and version 2 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