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B2SIT6 (KMO_XANOP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 24. 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:PXO_00760
OrganismXanthomonas oryzae pv. oryzae (strain PXO99A) [Complete proteome] [HAMAP]
Taxonomic identifier360094 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

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.

Sequence caution

The sequence ACD58731.1 differs from that shown. Reason: Erroneous initiation.

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_0000361952

Sequences

Sequence LengthMass (Da)Tools
B2SIT6 [UniParc].

Last modified February 10, 2009. Version 2.
Checksum: 5FA4778CE64A75ED

FASTA45551,014
        10         20         30         40         50         60 
MNPVSPRSLT MIGAGLAGCL LAILLSRRGW QITVYERRGD PRIKGYECGR SINLALAERG 

        70         80         90        100        110        120 
RHALRQAGAE EVVMAKAVMM RGRMVHPLVG EPQLQRYGRD DSEVIWSIHR AALNVALLDL 

       130        140        150        160        170        180 
AEQAGARVHF YRRLHTVDFD AGYARFIDDR DDQPHEIHFQ SLIGSDGAGS ALRAAMQRKS 

       190        200        210        220        230        240 
PLGERTEFLD HSYKELEIPP LPGGGFRIEG NALHIWPRGR YMFIALPNDG GTFTVTLFLP 

       250        260        270        280        290        300 
NAGEPSFATT RNGDEAFALF ARDFPDALPL IPQLKQHWEE HPPGLLGTLT LDRWHLDGRA 

       310        320        330        340        350        360 
LLIGDAAHAM VPFHGQGMNC AFEDCVALAD QLDAHDDLAS AFAAFEAARR DDAGAIQQMA 

       370        380        390        400        410        420 
LENYLEMRDR VDDPEFLLQR QLEQQLQARW PTRFVPHYTM VTFLRTRYSI ALARSEIQRE 

       430        440        450 
ILVEATRGHS DLSRLDWAAL ETIVHARLEP LDGAH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000967 Genomic DNA. Translation: ACD58731.1. Different initiation.
RefSeqYP_001913263.1. NC_010717.1.

3D structure databases

ProteinModelPortalB2SIT6.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2SIT6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6305628.
GenomeReviewsGene locus PXO_00760 in contig CP000967_GR.
KEGGxop:PXO_00760.
PATRIC24123624. VBIXanOry73153_2175.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG430104.
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_XANOP
AccessionPrimary (citable) accession number: B2SIT6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 24 of the entry and version 2 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