Skip Header

Contribute Send feedback
Read comments (?) or add your own

B2FL98 (KMO_STRMK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Smlt3161
OrganismStenotrophomonas maltophilia (strain K279a) [Complete proteome] [HAMAP]
Taxonomic identifier522373 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Stenotrophomonas › Stenotrophomonas maltophilia group

Protein attributes

Sequence length455 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 – 455455Kynurenine 3-monooxygenase
PRO_0000361945

Sequences

Sequence LengthMass (Da)Tools
B2FL98 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 692D6D46C223FDDB

FASTA45551,074
        10         20         30         40         50         60 
MIAHASRSLS IIGAGLAGSL LAILLSRQGW RITLYERRGD PRVADYESGR SINLALAERG 

        70         80         90        100        110        120 
RNALRQAGVE DEVMARAVMM RGRMVHPREG EPQLQRYGRD DSEVIWSIHR SDLNTTLLEL 

       130        140        150        160        170        180 
AEQAGATVHF HRRLHTVDFD AGYARFIDDR DDSPHDIRFD TLIGADGAGS ALRAAMNRRA 

       190        200        210        220        230        240 
PLGEDIAFLD HSYKELEIPP ADDGSFRIER NALHIWPRGH YMCIALPNHE GTFTVTLFLP 

       250        260        270        280        290        300 
NQGDPSFATI NTGAQAEALF AREFADTLPL IPNLRADWEQ HPPGLLGTLT LDRWHQQGRA 

       310        320        330        340        350        360 
VLIGDAAHAM VPFHGQGMNC AFEDCVALAR HLMEADDLEG AFAAFEAERK PNARAIQQMA 

       370        380        390        400        410        420 
LENYLEMRDR VADPAFLLQR ELEQELQRRW PTRFVPHYTM VTFLHTPYAE ALRRTELQRD 

       430        440        450 
MLVAATTGHD SLDNIDWAAL EAQIHAQLPV LEGAH

« Hide

References

[1]"The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A. expand/collapse author list , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
Genome Biol. 9:R74.1-R74.13(2008) [PubMed: 18419807] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K279a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM743169 Genomic DNA. Translation: CAQ46605.1.
RefSeqYP_001972896.1. NC_010943.1.

3D structure databases

ProteinModelPortalB2FL98.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2FL98.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6394111.
GenomeReviewsGene locus Smlt3161 in contig AM743169_GR.
KEGGsml:Smlt3161.
PATRIC23701789. VBISteMal45202_2957.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG430104.
OMAYFPDAIP.
ProtClustDBCLSK903475.

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_STRMK
AccessionPrimary (citable) accession number: B2FL98
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: June 10, 2008
Last modified: January 25, 2012
This is version 29 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents