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A1Z746 (KMO_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kynurenine 3-monooxygenase
EC=1.14.13.9
Alternative name(s):
Kynurenine 3-hydroxylase
Protein cinnabar
Gene names
Name:cn
ORF Names:CG1555
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 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.

Subcellular location

Mitochondrion By similarity. Membrane; Multi-pass membrane protein Potential.

Sequence similarities

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

Sequence caution

The sequence AAC47351.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAF59196.3 differs from that shown. Reason: Erroneous initiation.

The sequence AAK07882.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: A1Z746-1)

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.
Isoform 2 (identifier: A1Z746-2)

The sequence of this isoform differs from the canonical sequence as follows:
     399-465: RKWLDTLLFR...GGAIYAQRFL → DLLLKSSKSF...AAHFRLNCCC

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 465465Kynurenine 3-monooxygenase
PRO_0000361914

Regions

Transmembrane405 – 42723Helical; Potential
Transmembrane440 – 46223Helical; Potential

Natural variations

Alternative sequence399 – 46567RKWLD…AQRFL → DLLLKSSKSFSSPKVERHGW FRVFKEGELSMVRERERQRA AHFRLNCCC in isoform 2.
VSP_036238

Experimental info

Sequence conflict211R → M in AAK07882. Ref.2
Sequence conflict651Q → E in AAK07882. Ref.2
Sequence conflict651Q → E in AAL48918. Ref.5
Sequence conflict701Q → H in AAK07882. Ref.2
Sequence conflict1381V → E in AAK07882. Ref.2
Sequence conflict197 – 1982NN → HL in AAL48918. Ref.5
Sequence conflict3801A → P in AAK07882. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 10, 2009. Version 2.
Checksum: B44B6D22537353C0

FASTA46552,882
        10         20         30         40         50         60 
MSPGIVSQEV NGRQEPTEAA RDERHGRRRR VAVIGAGLVG SLAALNFARM GNHVDLYEYR 

        70         80         90        100        110        120 
EDIRQALVVQ GRSINLALSQ RGRKALAAVG LEQEVLATAI PMRGRMLHDV RGNSSVVLYD 

       130        140        150        160        170        180 
PINNQCLYSV GRRQLNEVLL NACDKLPNIR CHFEHKLTSA NLREGSMEFR NPAKEAVAAH 

       190        200        210        220        230        240 
ADLIVGCDGA FSSVRQNNVR LPGFNYSQEY IETGYLELCI PSKSGDFQMP ANYLHIWPRN 

       250        260        270        280        290        300 
TFMMIALPNQ DKSFTVTLSM PFEIFAGIQN QNDLLEFFKL NFRDALPLIG EQQLIKDFFK 

       310        320        330        340        350        360 
TRPQFLVSIK CRPYHYADKA LILGDAAHAM VPYYGQGMNA GMEDVTLLTD ILAKQLPLDE 

       370        380        390        400        410        420 
TLALFTESRW QDAFAICDLA MYNYVEMRDL TKRWTFRLRK WLDTLLFRLF PGWIPLYNSV 

       430        440        450        460 
SFSSMPYRQC IANRKWQDQL LKRIFGATFL AAIVTGGAIY AQRFL

« Hide

Isoform 2 [UniParc].

Checksum: E759C1445F98266E
Show »

FASTA44750,881

References

« Hide 'large scale' references
[1]"Drosophila melanogaster contains both X-linked and autosomal homologues of the gene encoding calcineurin B."
Warren W.D., Phillips A.M., Howells A.J.
Gene 177:149-153(1996) [PubMed: 8921860] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Canton-S.
[2]"Molecular nature of 11 spontaneous de novo mutations in Drosophila melanogaster."
Yang H.P., Tanikawa A.Y., Kondrashov A.S.
Genetics 157:1285-1292(2001) [PubMed: 11238412] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U56245 Genomic DNA. Translation: AAC47351.1. Different initiation.
AF317319 Genomic DNA. Translation: AAK07882.1. Different initiation.
AE013599 Genomic DNA. Translation: AAF59196.3. Different initiation.
AY071296 mRNA. Translation: AAL48918.1.
RefSeqNP_523651.3. NM_078927.2.
UniGeneDm.2860.

3D structure databases

ProteinModelPortalA1Z746.
SMRA1Z746. Positions 26-389.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1Z746.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID35724.
KEGGdme:Dmel_CG1555.
UCSCCG1555-RA. d. melanogaster.

Organism-specific databases

CTD35724.
FlyBaseFBgn0000337. cn.

Phylogenomic databases

eggNOGinNOG08413.
InParanoidA1Z746.
OrthoDBEOG4K6DKV.

Gene expression databases

ArrayExpressA1Z746.
BgeeA1Z746.

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...

Other

NextBio794902.

Entry information

Entry nameKMO_DROME
AccessionPrimary (citable) accession number: A1Z746
Secondary accession number(s): Q27577, Q8SYV3, Q9BMM9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 46 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents