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Q02LM7 (Q02LM7_PSEAB) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 52. 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 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
Q02LM7 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 105600F7FFCEC3D7

FASTA41646,265
        10         20         30         40         50         60 
MTTRDDCLAL DAGDPLADLR QLFALPDGVI YLDGNSLGAR PRAAVERAAE VVAAEWGEGL 

        70         80         90        100        110        120 
IRSWNSADWR GLPERLGDKL APLIGARAGE VVITDTTSIN LFKVLSAALR IQEEEAPGRK 

       130        140        150        160        170        180 
VIVSESSNFP TDLYIAEGLT DMLQRGYRLR LVDGPEQLPA AIDADTAVVM LSHVNYKTGY 

       190        200        210        220        230        240 
LHDMREVTRL VHENGALAIW DLAHSAGALP LDLHAAEADY AIGCTYKYLN GGPGSPAYVW 

       250        260        270        280        290        300 
VAPRLRERVW QPLSGWFGHS RQFAMEPRYQ PGEGITRFLC GTQPITSLAL VECGLDIFAR 

       310        320        330        340        350        360 
TDMQRLRDKS LALADLFIEL VESRCERFGL TLVTPREHAR RGSHVSFEHA QGYAIVQALI 

       370        380        390        400        410 
DRGVIGDYRE PGILRFGFTP LYTRFVEVWD AVQALLEILQ SEAWKEPRYQ VRHKVT 

« Hide

References

[1]"Genomic analysis reveals that Pseudomonas aeruginosa virulence is combinatorial."
Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S., Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.
Genome Biol. 7:R90.1-R90.14(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UCBPP-PA14 EMBL ABJ11263.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000438 Genomic DNA. Translation: ABJ11263.1.
RefSeqYP_791159.1. NC_008463.1.

3D structure databases

ProteinModelPortalQ02LM7.
SMRQ02LM7. Positions 2-404.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208963.PA14_37610.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ11263; ABJ11263; PA14_37610.
GeneID4380322.
KEGGpau:PA14_37610.
PATRIC19852254. VBIPseAer79785_3076.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242437.
KOK01556.
OMAVWDLAHS.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycPAER208963:GI5K-3045-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 nameQ02LM7_PSEAB
AccessionPrimary (citable) accession number: Q02LM7
Entry history
Integrated into UniProtKB/TrEMBL: November 14, 2006
Last sequence update: November 14, 2006
Last modified: July 9, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)