Q11PP7 (KMO_CYTH3) Reviewed, UniProtKB/Swiss-Prot

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:	CHU_3380

Organism

Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469) [Complete proteome] [HAMAP]

Taxonomic identifier

269798 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Cytophagia › Cytophagales › Cytophagaceae › Cytophaga

Protein attributes

Sequence length	449 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Ref.2
Catalytic activity	L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O. Ref.2
Cofactor	FAD By similarity. Ref.2
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3.
Sequence similarities	Belongs to the aromatic-ring hydroxylase family. KMO subfamily.
Biophysicochemical properties	Kinetic parameters: KM=76 µM for L-kynurenine Ref.2 KM=89 µM for NADPH

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	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 – 449	449	Kynurenine 3-monooxygenase		PRO_0000361935

Sequences

	Sequence		Length	Mass (Da)
	Q11PP7 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: 87CAAAAF07A2BE16	FASTA	449	50,783
	10 20 30 40 50 60 MKEQITICGA GLVGSLLAVY LIERGFSVRV FEKRKDPRKN EADAGRSINL AISHRGIHAL 70 80 90 100 110 120 KDAQTGLEKE ALKLAVPMYG RAIHDLHGHV SFQAYGEASQ HINSIGRGAL NKLLITTAEN 130 140 150 160 170 180 LGVHFLFEHT CTDYHAAGEQ WLFSDITGNT VATQSKEIVI GADGAFSIVR SFLSKQQQPQ 190 200 210 220 230 240 PQIETLEYGY KELEIASAHT ETITNNQALH IWPRERFMLI ALPNEDGSYT ATLFLPLKGE 250 260 270 280 290 300 ISFEALQSDQ DIQLFFKKYF PDTENLFPDL TEQFYRHPTS KLFTIHSSNW FNAHTLLIGD 310 320 330 340 350 360 AAHALVPFYG QGMNAGFEDC RILAEIIDGK SKTNWSEIFA EFYNQRKENA DAISDLALQN 370 380 390 400 410 420 FIEMRDHVAD ASFLLRKKIE KHLHQELEDA FIPQYTMVSF TDISYKEAME TGLLHQKILD 430 440 EIMAIPDIEA AWPTEELKNK VITVTKKYI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the cellulolytic gliding bacterium Cytophaga hutchinsonii." Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P., Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R., Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B., McBride M.J. Appl. Environ. Microbiol. 73:3536-3546(2007) [PubMed: 17400776] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33406 / NCIMB 9469.
[2]	"NAD biosynthesis: identification of the tryptophan to quinolinate pathway in bacteria." Kurnasov O., Goral V., Colabroy K., Gerdes S., Anantha S., Osterman A., Begley T.P. Chem. Biol. 10:1195-1204(2003) [PubMed: 14700627] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000383 Genomic DNA. Translation: ABG60616.1.
RefSeq	YP_679959.1. NC_008255.1.
3D structure databases
ProteinModelPortal	Q11PP7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q11PP7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4187169.
GenomeReviews	Gene locus CHU_3380 in contig CP000383_GR.
KEGG	chu:CHU_3380.
NMPDR	fig|269798.12.peg.3223.
PATRIC	21597639. VBICytHut34013_3364.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0654.
HOGENOM	HBG430104.
OMA	YFPDAIP.
ProtClustDB	CLSK903475.
Enzyme and pathway databases
BioCyc	CHUT269798:CHU_3380-MONOMER.
Family and domain databases
InterPro	IPR002938. mOase_FAD-bd. IPR003042. Rng_hydrolase-like. [Graphical view]
KO	K00486.
Pfam	PF01494. FAD_binding_3. 1 hit. [Graphical view]
PRINTS	PR00420. RNGMNOXGNASE.
ProtoNet	Search...

Entry information

Entry name

KMO_CYTH3

Accession

Primary (citable) accession number: Q11PP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	August 22, 2006
Last modified:	January 25, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program