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E8U823 (E8U823_DEIML) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 20. Feed History...

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

Sequence length394 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. 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

Region104 – 1074Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site761Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site771Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1811Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1841Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2061Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2351Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2631Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2071N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
E8U823 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: 7A26BB2B818E921D

FASTA39443,243
        10         20         30         40         50         60 
MKRDAFPLPP GVYMDGNSLG LMPHAARAAV LRRLDEWATR AVNGWDSWFG LAESLAPSVA 

        70         80         90        100        110        120 
RLVGAEPHEV AVTGSITSNL HALLATLYRP HGERRHLLAT ALDFPSDVYA LQSWAERYGA 

       130        140        150        160        170        180 
EVRFVPSRDG HTLDDADIEA SLTYDVAVAL LPSVLYRSGQ LLDIPRLTRA AHERGILIGW 

       190        200        210        220        230        240 
DAAHSAGSVP HELHAWDADF AVWCHYKYVN AGPGAPGGLF LHERHHDLAP GLRGWWGNHK 

       250        260        270        280        290        300 
GTQFDMTHTY HKAEGAGAYQ QGTPPILALA ALEGALEVFD EVGMPAIRAR SLDLTAHFMR 

       310        320        330        340        350        360 
AVDAHLPELR VVTPREEARR GGHVALAHPD AHLLSLGLRA RGITPDFRAP DILRLAPVAL 

       370        380        390 
YNDERDIDLT VQALRALLDA GHLEQYRAHE QAVR 

« Hide

References

[1]"The complete genome of Deinococcus maricopensis DSM 21211."
US DOE Joint Genome Institute (JGI-PGF)
Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P. expand/collapse author list , Woyke T., Wu D., Pukall R., Gehrich-Schroeter G., Brambilla E., Klenk H.-P., Eisen J.A.
Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002454 Genomic DNA. Translation: ADV67212.1.
RefSeqYP_004170877.1. NC_014958.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADV67212; ADV67212; Deima_1563.
GeneID10150916.
KEGGdmr:Deima_1563.
PATRIC46924192. VBIDeiMar159729_1571.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000242438.
KOK01556.

Enzyme and pathway databases

BioCycDMAR709986:GHZG-1607-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 nameE8U823_DEIML
AccessionPrimary (citable) accession number: E8U823
Entry history
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: February 19, 2014
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)