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Reviewed, UniProtKB/Swiss-Prot Q5WY16 (KMO_LEGPL)

Last modified November 3, 2009. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Kynurenine 3-monooxygenase
    EC=1.14.13.9
Alternative name(s):
    Kynurenine 3-hydroxylase
Gene names
Name: kmo
Ordered Locus Names: lpl0923
OrganismLegionella pneumophila (strain Lens) [Complete proteome] [HAMAP]
Taxonomic identifier297245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length449 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid By similarity.

Catalytic activity

L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O.

Cofactor

FAD By similarity.

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3.

Sequence similarities

Belongs to the aromatic-ring hydroxylase family. KMO subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449Kynurenine 3-monooxygenase
PRO_0000361940

Sequences

Sequence LengthMass (Da)Tools
Q5WY16-1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: BFF51B7443F9E38B

FASTA44951,334
        10         20         30         40         50         60 
MKHITIIGAG LAGTLCGLYL ARRGYEVELF ESRPDIRNSP TDYGRSINLA LSCRGITALK 

        70         80         90        100        110        120 
AMNLLSEVNK IMVPMRARAI HEANGEIHYQ PFGRHIDEYI NAISRSDLNA LLLNKAKLCP 

       130        140        150        160        170        180 
NIKLHFNMKL HSLDIHNKKI KFENKNGDFV EASYHRLIGA DGAPSHVRDM LKNEGIVSAS 

       190        200        210        220        230        240 
RDFLSHGYKE LSISKKHTKG MAREHLHLWP RDSFMLLGNP NPDDSITGSL FLANEGKDSF 

       250        260        270        280        290        300 
AELNNEEKLH LFFKTQFPDA YAAMPNLVQE FFGNPTGHLS TIQCSPWYYK DECLLIGDAA 

       310        320        330        340        350        360 
HGIIPFFGQG MNSAFEDCRI LDELLDEYQD DWSRVNSVFY EHRKVNTDAI AKMSMDNYHE 

       370        380        390        400        410        420 
IHSDIRNPKF ILQKQIEREL MLRYPEHYVS MHVLVMFTNT PYAKAMAIGE LQSGLLEQIC 

       430        440 
FPITDIKELN WQEVEKLLSL YDKKLAKII 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed: 15467720] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CR628337 Genomic DNA. Translation: CAH15157.1.
RefSeqYP_126282.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5WY16.

Genome annotation databases

GeneID3114288.
GenomeReviewsGene locus lpl0923 in contig CR628337_GR.
KEGGlpf:lpl0923.
NMPDRfig|297245.3.peg.1773.

Organism-specific databases

LegioListlpl0923.
CMRSearch...

Phylogenomic databases

HOGENOMQ5WY16.
OMALHAIMPS.

Enzyme and pathway databases

BioCycLPNE297245:LPL0923-MON.

Family and domain databases

InterProIPR006076. FAD-dep_OxRdtase.
IPR003042. Rng_hydrolase-like.
[Graphical view]
PfamPF01266. DAO. 1 hit.
[Graphical view]
PRINTSPR00420. RNGMNOXGNASE.
ProtoNetSearch...

Entry information

Entry nameKMO_LEGPL
AccessionPrimary (citable) accession number: Q5WY16
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: November 23, 2004
Last modified: November 3, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents