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G0ET24 (G0ET24_CUPNN) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Catalytic activity

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. PIRNR PIRNR038800 HAMAP-Rule MF_01970

L-kynurenine + H2O = anthranilate + L-alanine. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Cofactor

Pyridoxal phosphate By similarity. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Subunit structure

Homodimer By similarity. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Sequence similarities

Belongs to the kynureninase family. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region131 – 1344Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site991Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site1001Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1741Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2031Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2061Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2281Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2581Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2841Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2291N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
G0ET24 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: 6FECE4D46C5C085A

FASTA41845,855
        10         20         30         40         50         60 
MTTFDREHCI RLDERDPLRP LRDQFALPEG VIYLDGNSLG ARPRAAAARA AQVVAEEWGE 

        70         80         90        100        110        120 
GLIRSWNTAG WFELPQRLGN KLAPLVGAGQ DEVVVTDTTS INLFKVLAAA LRVQQTRDPA 

       130        140        150        160        170        180 
RKVIVSEASN FPTDLYIAQG LADLLQQGYS LRLVNSPAEI DAAVGADTAV LMLTHVNYKT 

       190        200        210        220        230        240 
GEMLDMAALT DLAHARGALT VWDLCHSAGA VPVNLKAAGA DYAIGCTYKY LNGGPGSPAF 

       250        260        270        280        290        300 
VWVAPALRDA FWQPLSGWWG HAAPFAMEPQ YRPVDGVRRF LCGTQPVTSL AMVECGLDIF 

       310        320        330        340        350        360 
AQTTMQVLRA KSLLLTDLFI ELVEARCGHH PLTLVTPREH ARRGSQVSLE HPDGYALVQA 

       370        380        390        400        410 
LIERGVIGDY REPRIARFGF TPLYTSFTEV WDAVEILRDV LDSGAYRDAR FQTRGQVT 

« Hide

References

[1]"Complete Genome Sequence of the Type Strain Cupriavidus necator N-1."
Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.
J. Bacteriol. 193:5017-5017(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43291 / DSM 13513 / N-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002877 Genomic DNA. Translation: AEI78030.1.
RefSeqYP_004686511.1. NC_015726.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEI78030; AEI78030; CNE_1c27150.
GeneID10919106.
KEGGcnc:CNE_1c27150.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01556.

Enzyme and pathway databases

BioCycCNEC1042878:GH0Z-2715-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 nameG0ET24_CUPNN
AccessionPrimary (citable) accession number: G0ET24
Entry history
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: July 9, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)