KMO

Functionⁱ

Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn) (PubMed:29429898, PubMed:23575632, PubMed:26752518, PubMed:28604669, PubMed:29208702). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract (Probable).1 Publication5 Publications

Miscellaneous

Increased in neuroinflammatory conditions. Inhibitors are investigated as potential neuroprotective drugs since they lead to an increased level of kynurenic acid, a neuroprotective NMDA receptor agonist.1 Publication

Catalytic activityⁱ

L-kynurenine + NADPH + O₂ = 3-hydroxy-L-kynurenine + NADP⁺ + H₂O.UniRule annotation3 Publications

Cofactorⁱ

FADUniRule annotation2 Publications

Kineticsⁱ

Kcat is 0.24 sec(-1) for L-kynurenine.1 Publication

V_max=
8.5 µmol/min/mg enzyme
2 Publications
Manual assertion based on experiment inⁱ
- Ref.1
  "Cloning and functional expression of human kynurenine 3-monooxygenase."
  Alberati-Giani D., Cesura A.M., Broger C., Warren W.D., Rover S., Malherbe P.
  FEBS Lett. 410:407-412(1997) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT CYS-452.
- Ref.2
  "Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase."
  Breton J., Avanzi N., Magagnin S., Covini N., Magistrelli G., Cozzi L., Isacchi A.
  Eur. J. Biochem. 267:1092-1099(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, VARIANT CYS-452.

pH dependenceⁱ

Pathwayⁱ: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:

Kynurenine 3-monooxygenase (KMO), Kynurenine 3-monooxygenase (KMO), Kynurenine 3-monooxygenase (KMO), Kynurenine 3-monooxygenase (KMO)
Kynureninase (KYNU), Kynureninase (KYNU), Kynureninase (KYNU)
3-hydroxyanthranilate 3,4-dioxygenase (HAAO)

This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	19	FAD; via amide nitrogenCombined sources1 Publication	1
Binding siteⁱ	57	FAD; via amide nitrogen and carbonyl oxygenCombined sources1 Publication	1
Binding siteⁱ	85	L-kynurenineBy similarity	1
Binding siteⁱ	99	L-kynurenineBy similarity	1
Binding siteⁱ	111	FADCombined sources1 Publication	1
Binding siteⁱ	136	FAD; via amide nitrogen and carbonyl oxygenCombined sources1 Publication	1
Binding siteⁱ	172	FADCombined sources1 Publication	1
Binding siteⁱ	304	FAD; via amide nitrogenCombined sources1 Publication	1
Binding siteⁱ	363	L-kynurenineBy similarity	1
Binding siteⁱ	398	L-kynurenineBy similarity	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	37 – 40	FADCombined sources1 Publication		4
Nucleotide bindingⁱ	317 – 318	FADCombined sources1 Publication		2

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-UniRule
aging Source: Ensembl
anthranilate metabolic process Source: UniProtKB-UniRule
cellular response to interleukin-1 Source: Ensembl
cellular response to lipopolysaccharide Source: Ensembl
kynurenic acid biosynthetic process Source: Ensembl
kynurenine metabolic process
Source: UniProtKB
Inferred from direct assayⁱ
L-kynurenine metabolic process Source: Ensembl
NAD metabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 23575632
- 29429898
positive regulation of glutamate secretion, neurotransmission Source: Ensembl
positive regulation of neuron death Source: Ensembl
quinolinate biosynthetic process Source: UniProtKB-UniRule
response to salt stress
Source: UniProtKB
Inferred from direct assayⁱ
- 10672018
tryptophan catabolic process Source: Reactome

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Monooxygenase, Oxidoreductase
Biological process	Pyridine nucleotide biosynthesis
Ligand	FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS04082-MONOMER
Reactomeⁱ	R-HSA-71240 Tryptophan catabolism
SABIO-RKⁱ	O15229
UniPathwayⁱ	UPA00253;UER00328

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Kynurenine 3-monooxygenaseUniRule annotation (EC:1.14.13.9UniRule annotation) Alternative name(s): Kynurenine 3-hydroxylaseUniRule annotation
Gene namesⁱ	Name:KMOUniRule annotationImported
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 1

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000117009.11
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:6381 KMO
MIMⁱ	603538 gene
neXtProtⁱ	NX_O15229

Topology

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transmembraneⁱ	385 – 404	HelicalUniRule annotationAdd BLAST		20
Transmembraneⁱ	425 – 445	HelicalUniRule annotationAdd BLAST		21

Keywords - Cellular componentⁱ

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	85	R → A or K: Abolishes kynurenine 3-monooxygenase activity. 1 Publication	1
Mutagenesisⁱ	99	Y → A: Abolishes kynurenine 3-monooxygenase activity. 1 Publication	1
Mutagenesisⁱ	99	Y → F: Strongly decreases kynurenine 3-monooxygenase activity. 1 Publication	1
Mutagenesisⁱ	312 – 313	FF → AA: Abolishes NADPH oxidase activity. 1 Publication	2
Mutagenesisⁱ	312	F → A: Decreases to 30% NADPH oxidase activity. 1 Publication	1
Mutagenesisⁱ	313	F → A: Decreases to 50% NADPH oxidase activity. 1 Publication	1
Mutagenesisⁱ	363	N → A: Strongly decreases kynurenine 3-monooxygenase activity. 1 Publication	1
Mutagenesisⁱ	363	N → D: Abolishes kynurenine 3-monooxygenase activity. 1 Publication	1
Mutagenesisⁱ	366	E → A or Q: Strongly decreases kynurenine 3-monooxygenase activity. 1 Publication	1
Mutagenesisⁱ	367	M → A: Strongly decreases kynurenine 3-monooxygenase activity. 1 Publication	1
Mutagenesisⁱ	367	M → L: Strongly decreases kynurenine 3-monooxygenase activity. 1 Publication	1
Mutagenesisⁱ	398	Y → A or F: Abolishes kynurenine 3-monooxygenase activity. 1 Publication	1
Mutagenesisⁱ	465	N → A: Not glycosylted. Reduces to 80% kynurenine 3-monooxygenase activity. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	8564
Open Targets More...OpenTargetsⁱ	ENSG00000117009
PharmGKBⁱ	PA30172

Chemistry databases

ChEMBLⁱ	CHEMBL2145
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2886

Polymorphism and mutation databases

BioMutaⁱ	KMO

BioMutaⁱ

KMO

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000229742	1 – 486	Kynurenine 3-monooxygenaseCuratedAdd BLAST		486

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Glycosylationⁱ	465	N-linked (GlcNAc...) asparagine1 Publication		1

Keywords - PTMⁱ

Glycoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O15229
PaxDbⁱ	O15229
PeptideAtlas More...PeptideAtlasⁱ	O15229
PRIDEⁱ	O15229
ProteomicsDBⁱ	48519 48520 [O15229-2] 48521 [O15229-3]

PTM databases

iPTMnetⁱ	O15229
PhosphoSitePlusⁱ	O15229

Expressionⁱ

Tissue specificityⁱ

Highest levels in placenta and liver. Detectable in kidney.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000117009 Expressed in 128 organ(s), highest expression level in placenta
CleanExⁱ	HS_KMO
ExpressionAtlasⁱ	O15229 baseline and differential
Genevisibleⁱ	O15229 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA031115 HPA056942

HPAⁱ

HPA031115
HPA056942

Interactionⁱ

Protein-protein interaction databases

BioGridⁱ	114133, 3 interactors
STRINGⁱ	9606.ENSP00000355517

Chemistry databases

BindingDBⁱ

O15229

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	10 – 14	Combined sources	5
Helixⁱ	18 – 28	Combined sources	11
Turnⁱ	29 – 31	Combined sources	3
Beta strandⁱ	33 – 37	Combined sources	5
Turnⁱ	43 – 45	Combined sources	3
Beta strandⁱ	55 – 58	Combined sources	4
Helixⁱ	60 – 68	Combined sources	9
Helixⁱ	72 – 76	Combined sources	5
Beta strandⁱ	80 – 82	Combined sources	3
Beta strandⁱ	84 – 88	Combined sources	5
Beta strandⁱ	94 – 98	Combined sources	5
Helixⁱ	102 – 104	Combined sources	3
Beta strandⁱ	106 – 110	Combined sources	5
Helixⁱ	111 – 123	Combined sources	13
Beta strandⁱ	128 – 131	Combined sources	4
Beta strandⁱ	138 – 140	Combined sources	3
Turnⁱ	141 – 144	Combined sources	4
Beta strandⁱ	145 – 148	Combined sources	4
Beta strandⁱ	156 – 159	Combined sources	4
Beta strandⁱ	161 – 165	Combined sources	5
Helixⁱ	172 – 177	Combined sources	6
Beta strandⁱ	189 – 199	Combined sources	11
Beta strandⁱ	202 – 205	Combined sources	4
Beta strandⁱ	212 – 217	Combined sources	6
Beta strandⁱ	222 – 227	Combined sources	6
Beta strandⁱ	233 – 240	Combined sources	8
Helixⁱ	241 – 244	Combined sources	4
Helixⁱ	250 – 260	Combined sources	11
Helixⁱ	264 – 268	Combined sources	5
Helixⁱ	270 – 277	Combined sources	8
Beta strandⁱ	283 – 286	Combined sources	4
Beta strandⁱ	288 – 290	Combined sources	3
Beta strandⁱ	293 – 295	Combined sources	3
Turnⁱ	296 – 298	Combined sources	3
Beta strandⁱ	299 – 301	Combined sources	3
Helixⁱ	303 – 305	Combined sources	3
Turnⁱ	311 – 313	Combined sources	3
Helixⁱ	316 – 333	Combined sources	18
Turnⁱ	334 – 336	Combined sources	3
Helixⁱ	338 – 349	Combined sources	12
Beta strandⁱ	363 – 365	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	O15229
SMRⁱ	O15229
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domainⁱ

Transmembrane domains are required for enzymatic activity.2 Publications

Sequence similaritiesⁱ

Belongs to the aromatic-ring hydroxylase family. KMO subfamily.UniRule annotation

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG2614 Eukaryota COG0654 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000000747
HOVERGENⁱ	HBG057213
InParanoidⁱ	O15229
KEGG Orthology (KO) More...KOⁱ	K00486
OMAⁱ	MHGRMIH
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0769
PhylomeDBⁱ	O15229
TreeFamⁱ	TF312990

Family and domain databases

Gene3Dⁱ	3.50.50.60, 1 hit
HAMAPⁱ	MF_01971 Kynurenine_monooxygenase, 1 hit
InterProⁱ	View protein in InterPro IPR002938 FAD-bd IPR036188 FAD/NAD-bd_sf IPR027545 Kynurenine_monooxygenase
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01494 FAD_binding_3, 1 hit
SUPFAMⁱ	SSF51905 SSF51905, 1 hit

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 1 potential isoform that is computationally mapped.Show all Align All

Isoform 12 Publications (identifier: O15229-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDSSVIQRKK VAVIGGGLVG SLQACFLAKR NFQIDVYEAR EDTRVATFTR 
        60         70         80         90        100
GRSINLALSH RGRQALKAVG LEDQIVSQGI PMRARMIHSL SGKKSAIPYG 
       110        120        130        140        150
TKSQYILSVS RENLNKDLLT AAEKYPNVKM HFNHRLLKCN PEEGMITVLG 
       160        170        180        190        200
SDKVPKDVTC DLIVGCDGAY STVRSHLMKK PRFDYSQQYI PHGYMELTIP 
       210        220        230        240        250
PKNGDYAMEP NYLHIWPRNT FMMIALPNMN KSFTCTLFMP FEEFEKLLTS 
       260        270        280        290        300
NDVVDFFQKY FPDAIPLIGE KLLVQDFFLL PAQPMISVKC SSFHFKSHCV 
       310        320        330        340        350
LLGDAAHAIV PFFGQGMNAG FEDCLVFDEL MDKFSNDLSL CLPVFSRLRI 
       360        370        380        390        400
PDDHAISDLS MYNYIEMRAH VNSSWFIFQK NMERFLHAIM PSTFIPLYTM 
       410        420        430        440        450
VTFSRIRYHE AVQRWHWQKK VINKGLFFLG SLIAISSTYL LIHYMSPRSF 
       460        470        480 
LRLRRPWNWI AHFRNTTCFP AKAVDSLEQI SNLISR

Length:486

Mass (Da):55,810

Last modified:February 20, 2007 - v2

Checksum:ⁱ164870D52E62A08A

GO

Isoform 21 Publication (identifier: O15229-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
367-379: Missing.

« Hide

        10         20         30         40         50
MDSSVIQRKK VAVIGGGLVG SLQACFLAKR NFQIDVYEAR EDTRVATFTR 
        60         70         80         90        100
GRSINLALSH RGRQALKAVG LEDQIVSQGI PMRARMIHSL SGKKSAIPYG 
       110        120        130        140        150
TKSQYILSVS RENLNKDLLT AAEKYPNVKM HFNHRLLKCN PEEGMITVLG 
       160        170        180        190        200
SDKVPKDVTC DLIVGCDGAY STVRSHLMKK PRFDYSQQYI PHGYMELTIP 
       210        220        230        240        250
PKNGDYAMEP NYLHIWPRNT FMMIALPNMN KSFTCTLFMP FEEFEKLLTS 
       260        270        280        290        300
NDVVDFFQKY FPDAIPLIGE KLLVQDFFLL PAQPMISVKC SSFHFKSHCV 
       310        320        330        340        350
LLGDAAHAIV PFFGQGMNAG FEDCLVFDEL MDKFSNDLSL CLPVFSRLRI 
       360        370        380        390        400
PDDHAISDLS MYNYIEKNME RFLHAIMPST FIPLYTMVTF SRIRYHEAVQ 
       410        420        430        440        450
RWHWQKKVIN KGLFFLGSLI AISSTYLLIH YMSPRSFLRL RRPWNWIAHF 
       460        470 
RNTTCFPAKA VDSLEQISNL ISR

Note: Gene model based on cDNA data. No experimental confirmation available.

Show »

Length:473

Mass (Da):54,205

Checksum:ⁱ9D898B2A91A76782

GO

Isoform 31 Publication (identifier: O15229-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
367-400: Missing.

« Hide

        10         20         30         40         50
MDSSVIQRKK VAVIGGGLVG SLQACFLAKR NFQIDVYEAR EDTRVATFTR 
        60         70         80         90        100
GRSINLALSH RGRQALKAVG LEDQIVSQGI PMRARMIHSL SGKKSAIPYG 
       110        120        130        140        150
TKSQYILSVS RENLNKDLLT AAEKYPNVKM HFNHRLLKCN PEEGMITVLG 
       160        170        180        190        200
SDKVPKDVTC DLIVGCDGAY STVRSHLMKK PRFDYSQQYI PHGYMELTIP 
       210        220        230        240        250
PKNGDYAMEP NYLHIWPRNT FMMIALPNMN KSFTCTLFMP FEEFEKLLTS 
       260        270        280        290        300
NDVVDFFQKY FPDAIPLIGE KLLVQDFFLL PAQPMISVKC SSFHFKSHCV 
       310        320        330        340        350
LLGDAAHAIV PFFGQGMNAG FEDCLVFDEL MDKFSNDLSL CLPVFSRLRI 
       360        370        380        390        400
PDDHAISDLS MYNYIEVTFS RIRYHEAVQR WHWQKKVINK GLFFLGSLIA 
       410        420        430        440        450
ISSTYLLIHY MSPRSFLRLR RPWNWIAHFR NTTCFPAKAV DSLEQISNLI 

SR

Note: Gene model based on mouse cDNA data. No experimental confirmation available.

Show »

Length:452

Mass (Da):51,682

Checksum:ⁱ59D707C5D8F21C03

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	H0Y320	H0Y320_HUMAN		Kynurenine 3-monooxygenase Kynurenine 3-monooxygenase	KMO	182	Annotation score:

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_030845	452	R → C2 PublicationsCorresponds to variant dbSNP:rs1053230Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_051972	367 – 400	Missing in isoform 3. 1 PublicationAdd BLAST		34
Alternative sequenceⁱVSP_051973	367 – 379	Missing in isoform 2. 1 PublicationAdd BLAST		13

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	Y13153 mRNA Translation: CAA73613.1 AF056032 mRNA Translation: AAC62615.1 AL133390 Genomic DNA No translation available. FO393423 Genomic DNA No translation available.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS1618.1 [O15229-1]
NCBI Reference Sequences More...RefSeqⁱ	NP_003670.2, NM_003679.4 [O15229-1]
UniGeneⁱ	Hs.731056 Hs.744065

Genome annotation databases

Ensemblⁱ	ENST00000366557; ENSP00000355515; ENSG00000117009 [O15229-3] ENST00000366558; ENSP00000355516; ENSG00000117009 [O15229-2] ENST00000366559; ENSP00000355517; ENSG00000117009 [O15229-1]
GeneIDⁱ	8564
KEGGⁱ	hsa:8564
UCSC genome browser More...UCSCⁱ	uc001hyy.4 human [O15229-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
O15229	Kynurenine 3-monooxygenase		HUMAN		526	UniRef100_O15229
UPI000387CA3B		HUMAN		405

Protein	Similar proteins		Species	Score	Length	Source
O15229	Kynurenine 3-monooxygenase		HUMAN		526	UniRef90_O15229
Kynurenine 3-monooxygenase		PANTR		501
Kynurenine 3-monooxygenase		PANPA		492
Kynurenine 3-monooxygenase		GORGO		486
Kynurenine 3-monooxygenase		PONAB		486
+39
O15229-3	Kynurenine 3-monooxygenase		MACMU		455	UniRef90_O15229-3
Kynurenine 3-monooxygenase		PANTR		452
KMO isoform 7		PONAB		452
Kynurenine 3-monooxygenase		PANPA		452
Uncharacterized protein		NOMLE		452
+4

Protein	Similar proteins		Species	Score	Length	Source
O15229	Kynurenine 3-monooxygenase		XENTR		473	UniRef50_O15229
Kynurenine 3-monooxygenase		MOUSE		479
Kynurenine 3-monooxygenase		RAT		478
Kynurenine 3-monooxygenase		PIG		471
Kynurenine 3-monooxygenase		DANRE		474
+505

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	Y13153 mRNA Translation: CAA73613.1 AF056032 mRNA Translation: AAC62615.1 AL133390 Genomic DNA No translation available. FO393423 Genomic DNA No translation available.
CCDSⁱ	CCDS1618.1 [O15229-1]
RefSeqⁱ	NP_003670.2, NM_003679.4 [O15229-1]
UniGeneⁱ	Hs.731056 Hs.744065

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	5X68	X-ray	2.10	A/B	1-374	[»]
ProteinModelPortalⁱ	O15229
SMRⁱ	O15229
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	114133, 3 interactors
STRINGⁱ	9606.ENSP00000355517

Chemistry databases

BindingDBⁱ	O15229
ChEMBLⁱ	CHEMBL2145
GuidetoPHARMACOLOGYⁱ	2886

PTM databases

iPTMnetⁱ	O15229
PhosphoSitePlusⁱ	O15229

Polymorphism and mutation databases

BioMutaⁱ	KMO

BioMutaⁱ

KMO

Proteomic databases

MaxQBⁱ	O15229
PaxDbⁱ	O15229
PeptideAtlasⁱ	O15229
PRIDEⁱ	O15229
ProteomicsDBⁱ	48519 48520 [O15229-2] 48521 [O15229-3]

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000366557; ENSP00000355515; ENSG00000117009 [O15229-3] ENST00000366558; ENSP00000355516; ENSG00000117009 [O15229-2] ENST00000366559; ENSP00000355517; ENSG00000117009 [O15229-1]
GeneIDⁱ	8564
KEGGⁱ	hsa:8564
UCSCⁱ	uc001hyy.4 human [O15229-1]

Organism-specific databases

CTDⁱ	8564
DisGeNETⁱ	8564
EuPathDBⁱ	HostDB:ENSG00000117009.11
GeneCardsⁱ	KMO
HGNCⁱ	HGNC:6381 KMO
HPAⁱ	HPA031115 HPA056942
MIMⁱ	603538 gene
neXtProtⁱ	NX_O15229
OpenTargetsⁱ	ENSG00000117009
PharmGKBⁱ	PA30172
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2614 Eukaryota COG0654 LUCA
GeneTreeⁱ	ENSGT00390000000747
HOVERGENⁱ	HBG057213
InParanoidⁱ	O15229
KOⁱ	K00486
OMAⁱ	MHGRMIH
OrthoDBⁱ	EOG091G0769
PhylomeDBⁱ	O15229
TreeFamⁱ	TF312990

Enzyme and pathway databases

UniPathwayⁱ	UPA00253;UER00328
BioCycⁱ	MetaCyc:HS04082-MONOMER
Reactomeⁱ	R-HSA-71240 Tryptophan catabolism
SABIO-RKⁱ	O15229

Miscellaneous databases

ChiTaRSⁱ	KMO human
GeneWikiⁱ	KMO_(gene)
GenomeRNAiⁱ	8564
Protein Ontology More...PROⁱ	PR:O15229
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000117009 Expressed in 128 organ(s), highest expression level in placenta
CleanExⁱ	HS_KMO
ExpressionAtlasⁱ	O15229 baseline and differential
Genevisibleⁱ	O15229 HS

Family and domain databases

Gene3Dⁱ	3.50.50.60, 1 hit
HAMAPⁱ	MF_01971 Kynurenine_monooxygenase, 1 hit
InterProⁱ	View protein in InterPro IPR002938 FAD-bd IPR036188 FAD/NAD-bd_sf IPR027545 Kynurenine_monooxygenase
Pfamⁱ	View protein in Pfam PF01494 FAD_binding_3, 1 hit
SUPFAMⁱ	SSF51905 SSF51905, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	KMO_HUMAN
Accessionⁱ	O15229Primary (citable) accession number: O15229 Secondary accession number(s): A2A2U8 , A2A2U9, A2A2V0, Q5SY07, Q5SY08, Q5SY09
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
	Last sequence update:	February 20, 2007
	Last modified:	November 7, 2018
	This is version 153 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

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UniProtKB - O15229 (KMO_HUMAN)

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Kynurenine 3-monooxygenase

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

pH dependencei

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: NAD(+) biosynthesis

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GO - Biological processi

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Organism-specific databases

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Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

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Secondary structure

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<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

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Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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Functionⁱ

Kineticsⁱ

pH dependenceⁱ

Pathwayⁱ: NAD(+) biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ