Reviewed, UniProtKB/Swiss-Prot Q2P316 (KMO_XANOM)

Names and origin

Protein names

Recommended name:
    Kynurenine 3-monooxygenase
    EC=1.14.13.9
Alternative name(s):
    Kynurenine 3-hydroxylase

Gene names

Name:	kmo
Ordered Locus Names:	XOO2306

Organism

Xanthomonas oryzae pv. oryzae (strain MAFF 311018) [Complete proteome] [HAMAP]

Taxonomic identifier

342109 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

Protein attributes

Sequence length	455 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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 process	Pyridine nucleotide biosynthesis
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pyridine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	kynurenine 3-monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 455	455	Kynurenine 3-monooxygenase		PRO_0000361951

Sequences

	Sequence		Length	Mass (Da)
	Q2P316-1 [UniParc]. Last modified February 7, 2006. Version 1. Checksum: CC8AE451A359FC4B	FASTA	455	50,983
	10 20 30 40 50 60 MSPVSPRSLT LIGAGLAGCL LAILLSRRGW QITVYERRGD PRIKGYECGR SINLALAERG 70 80 90 100 110 120 RHALRQAGAE ELVMAKAVMM 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

References

[1]

"Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of large numbers of effector genes and insertion sequences to its race diversity." Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H. Jpn. Agric. Res. Q. 39:275-287(2005) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AP008229 Genomic DNA. Translation: BAE69061.1.
RefSeq	YP_451335.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q2P316.
Genome annotation databases
GeneID	3856664.
GenomeReviews	Gene locus XOO2306 in contig AP008229_GR.
KEGG	xom:XOO_2306.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2P316.
OMA	DTIRTEA.
Enzyme and pathway databases
BioCyc	XORY342109:XOO2306-MON.
Family and domain databases
InterPro	IPR002938. mOase_FAD_bd. IPR003042. Rng_hydrolase-like. [Graphical view]
Pfam	PF01494. FAD_binding_3. 1 hit. [Graphical view]
PRINTS	PR00420. RNGMNOXGNASE.
ProtoNet	Search...

Entry information

Entry name

KMO_XANOM

Accession

Primary (citable) accession number: Q2P316

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	February 7, 2006
Last modified:	November 3, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)