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C4KRM8 (C4KRM8_BURPE) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length416 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

Region129 – 1324Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site971Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site981Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1721Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2011Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2041Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2261Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2561Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2821Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2271N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
C4KRM8 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: E48940B4AB277FB4

FASTA41645,864
        10         20         30         40         50         60 
MKTREEALAL DRDDPLAPLR EQFALPAGVI YLDGNSLGAQ PRAAAARAQQ VIGAEWGEGL 

        70         80         90        100        110        120 
IRSWNTAGWF ALPRRLGDRL APLIGAADGE VAITDTISIN LFKLLAAMLR HQARHAPKRR 

       130        140        150        160        170        180 
VIVSERSNFP TDLYIAQGLI AQLDRDYELR LIDDPADLPD ALDDETAVAM ITHVNYRTGY 

       190        200        210        220        230        240 
MHDMPSVTQT VRQAGALMLW DLAHSAGAVP VDLNGALADG AVGCTYKYLN GGPGSPAFVW 

       250        260        270        280        290        300 
VPKRHQRAFE QPLSGWWGHR APFAMQPAFE PDPGIARFLC GTQPIVSMSM VECGLDVFAQ 

       310        320        330        340        350        360 
TDMHAIRRKS LALTDAFVAL VESRCAGQPL KLVTPRAHHQ RGSQASFEHP HGYEVMQALI 

       370        380        390        400        410 
ARGVIGDYRE PRILRFGFTP LYTRFVDVWD AVETLRDILD TEAWRAPEFA TRAAVT 

« Hide

References

[1]Harkins D.M., Brinkac L.M., Rogers Y.C., Detter J.C., Munk A.C., Bruce D.C., Keim P., Sims D.R., Brettin T.S.
Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: MSHR346 EMBL ACQ95775.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001408 Genomic DNA. Translation: ACQ95775.1.
RefSeqYP_002895544.1. NC_012695.1.

3D structure databases

ProteinModelPortalC4KRM8.
SMRC4KRM8. Positions 3-404.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING536230.GBP346_A0820.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ95775; ACQ95775; GBP346_A0820.
GeneID7889100.
KEGGbpr:GBP346_A0820.
PATRIC32570831. VBIBurPse130472_0755.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242437.
KOK01556.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycBPSE536230:GHVQ-819-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 nameC4KRM8_BURPE
AccessionPrimary (citable) accession number: C4KRM8
Entry history
Integrated into UniProtKB/TrEMBL: July 7, 2009
Last sequence update: July 7, 2009
Last modified: July 9, 2014
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)