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A5IG23 (KMO_LEGPC) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:LPC_2401
OrganismLegionella pneumophila (strain Corby) [Complete proteome] [HAMAP]
Taxonomic identifier400673 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella

Protein attributes

Sequence length449 AA.
Sequence statusComplete.
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

Keywords
   Biological processPyridine nucleotide biosynthesis
   LigandFAD
Flavoprotein
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpyridine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionkynurenine 3-monooxygenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449Kynurenine 3-monooxygenase
PRO_0000361939

Sequences

Sequence LengthMass (Da)Tools
A5IG23 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 369B9E31E8C50D7E

FASTA44951,309
        10         20         30         40         50         60 
MKHITIIGAG LAGTLCGLYL ARRGYEVELF ESRPDIRNSP TDYGRSINLA LSCRGITALK 

        70         80         90        100        110        120 
AMNLLSEVNK IMVPMRARAI HEANGEVHYQ PFGRHIDEYI NAISRSDLNA LLLNKAELCP 

       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 DWSRVTPVFY EQRKVNTDAI AKMSMDNYHE 

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

       430        440 
FPITDIKELN WQEVEKLLSI YDKKLAKII

« Hide

References

[1]"Identification and characterization of a new conjugation/ type IVA secretion system (trb/tra) of L. pneumophila Corby localized on a mobile genomic island."
Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E., Steinert M., Buchrieser C., Hacker J., Heuner K.
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Corby.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000675 Genomic DNA. Translation: ABQ56323.1.
RefSeqYP_001251669.1. NC_009494.2.

3D structure databases

ProteinModelPortalA5IG23.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5IG23.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5180232.
GenomeReviewsGene locus LPC_2401 in contig CP000675_GR.
KEGGlpc:LPC_2401.
PATRIC22311371. VBILegPne45588_2498.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0654.
HOGENOMHBG430104.
OMAYFPDAIP.
ProtClustDBCLSK903475.

Enzyme and pathway databases

BioCycLPNE400673:LPC_2401-MONOMER.

Family and domain databases

InterProIPR002938. mOase_FAD-bd.
IPR003042. Rng_hydrolase-like.
[Graphical view]
KOK00486.
PfamPF01494. FAD_binding_3. 1 hit.
[Graphical view]
PRINTSPR00420. RNGMNOXGNASE.
ProtoNetSearch...

Entry information

Entry nameKMO_LEGPC
AccessionPrimary (citable) accession number: A5IG23
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: June 26, 2007
Last modified: December 14, 2011
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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