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UniProtKB/Swiss-Prot entry O15229


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KMO_HUMAN
Primary accession number O15229
Secondary accession numbers A2A2V0 Q5SY07 Q5SY08 Q5SY09
Integrated into Swiss-Prot on April 4, 2006
Sequence was last modified on February 20, 2007 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 57)
Name and origin of the protein
Protein name Kynurenine 3-monooxygenase
Synonyms EC 1.14.13.9
Kynurenine 3-hydroxylase
Gene name
Name: KMO
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT CYS-452.
TISSUE=Liver;
DOI=10.1016/S0014-5793(97)00627-3; PubMed=9237672 [NCBI, ExPASy, EBI, Israel, Japan]
Alberati-Giani D., Cesura A.M., Broger C., Warren W.D., Rover S., Malherbe P.;
"Cloning and functional expression of human kynurenine 3-monooxygenase.";
FEBS Lett. 410:407-412(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANT CYS-452.
TISSUE=Liver;
PubMed=10672018 [NCBI, ExPASy, EBI, Israel, Japan]
Breton J., Avanzi N., Magagnin S., Covini N., Magistrelli G., Cozzi L., Isacchi A.;
"Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase.";
Eur. J. Biochem. 267:1092-1099(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
REVIEW.
DOI=10.1038/nrd870; PubMed=12402501 [NCBI, ExPASy, EBI, Israel, Japan]
Stone T.W., Darlington L.G.;
"Endogenous kynurenines as targets for drug discovery and development.";
Nat. Rev. Drug Discov. 1:609-620(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y13153; CAA73613.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF056032; AAC62615.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133390; CAM28228.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591898; CAM28228.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591898; CAI13905.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133390; CAI13905.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591898; CAI13906.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133390; CAI13906.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591898; CAI13907.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133390; CAI13907.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_003670.2; -.
UniGene Hs.409081
3D structure databases
ModBase O15229.
PTM databases
PhosphoSite O15229; -.
Enzyme and pathway databases
Reactome REACT_11127; Metabolism of vitamins and cofactors.
REACT_13; Metabolism of amino acids.
Organism-specific databases
GeneCards GC01P239781; -.
H-InvDB HIX0001738; -.
HGNC HGNC:6381; KMO.
GenAtlas KMO.
MIM 603538; gene. [NCBI / EBI]
PharmGKB PA30172; -.
GeneCards O15229.
Gene expression databases
ArrayExpress O15229; -.
CleanEx HS_KMO; -.
GermOnline ENSG00000117009; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005741; Cellular component: mitochondrial outer membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0009055; Molecular function: electron carrier activity (traceable author statement from UniProtKB).
GO:0004502; Molecular function: kynurenine 3-monooxygenase activity (traceable author statement from ProtInc).
GO:0019674; Biological process: NAD metabolic process (inferred from experiment from Reactome).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR006076; FAD-dep_OxRdtase.
IPR003042; Rng_hydrolase.
Graphical view of domain structure.
Pfam PF01266; DAO; 1.
Pfam graphical view of domain structure.
PRINTS PR00420; RNGMNOXGNASE.
Proteomics databases
PRIDE O15229; -.
Genome annotation databases
Ensembl ENSG00000117009; Homo sapiens. [Contig view]
GeneID 8564; -.
KEGG hsa:8564; -.
NMPDR fig|9606.3.peg.3320; -.
Phylogenomic databases
HOGENOM O15229; -.
HOVERGEN O15229; -.
Other
NextBio 32109; -.
SOURCE KMO; Homo sapiens.
ProtoNet O15229.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; FAD; Membrane; Mitochondrion; Mitochondrion outer membrane; Monooxygenase; NADP; Oxidoreductase; Phosphoprotein; Polymorphism; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   486  486     Kynurenine 3-monooxygenase. PRO_0000229742
TRANSMEM   384   404  21     Potential. 
TRANSMEM   425   445  21     Potential. 
MOD_RES   399   399        Phosphothreonine (By similarity). 
VAR_SEQ   367   400        Missing (in isoform 3). VSP_051972
VAR_SEQ   367   379        Missing (in isoform 2). VSP_051973
VARIANT   452   452  1     R -> C (in dbSNP:rs1053230 [NCBI]). VAR_030845 
Sequence information
Length: 486 AA [This is the length of the unprocessed precursor] Molecular weight: 55810 Da [This is the MW of the unprocessed precursor] CRC64: 164870D52E62A08A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDSSVIQRKK VAVIGGGLVG SLQACFLAKR NFQIDVYEAR EDTRVATFTR GRSINLALSH 

        70         80         90        100        110        120 
RGRQALKAVG LEDQIVSQGI PMRARMIHSL SGKKSAIPYG TKSQYILSVS RENLNKDLLT 

       130        140        150        160        170        180 
AAEKYPNVKM HFNHRLLKCN PEEGMITVLG SDKVPKDVTC DLIVGCDGAY STVRSHLMKK 

       190        200        210        220        230        240 
PRFDYSQQYI PHGYMELTIP PKNGDYAMEP NYLHIWPRNT FMMIALPNMN KSFTCTLFMP 

       250        260        270        280        290        300 
FEEFEKLLTS NDVVDFFQKY FPDAIPLIGE KLLVQDFFLL PAQPMISVKC SSFHFKSHCV 

       310        320        330        340        350        360 
LLGDAAHAIV PFFGQGMNAG FEDCLVFDEL MDKFSNDLSL CLPVFSRLRI PDDHAISDLS 

       370        380        390        400        410        420 
MYNYIEMRAH VNSSWFIFQK NMERFLHAIM PSTFIPLYTM VTFSRIRYHE AVQRWHWQKK 

       430        440        450        460        470        480 
VINKGLFFLG SLIAISSTYL LIHYMSPRSF LRLRRPWNWI AHFRNTTCFP AKAVDSLEQI 


SNLISR 

O15229 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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