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Q7Q6A7 (KMO_ANOGA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Gene names
Name:kh
ORF Names:AGAP005948
OrganismAnopheles gambiae (African malaria mosquito)
Taxonomic identifier7165 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Subcellular location

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

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Kynurenine 3-monooxygenase
PRO_0000361913

Regions

Transmembrane401 – 42424Helical; Potential
Transmembrane437 – 46125Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
Q7Q6A7 [UniParc].

Last modified December 7, 2004. Version 2.
Checksum: 5A5F80A34C8FAB97

FASTA48655,010
        10         20         30         40         50         60 
MATASDSKYK RTNTNGMQHQ PLDVAIVGGG LVGSLLALHL GKKGHEVNLY EYREDIRTAE 

        70         80         90        100        110        120 
LVIGRSINLA LSARGRRALA EVGLEDALLN HGIPMSGRML HDVNGKCKIV PYDANTNQCI 

       130        140        150        160        170        180 
YSVGRKHLNE VLLNAAEKYP NIHLHFNHKL VSANLDEGNL SMVDPVTKDV KSARADLIVG 

       190        200        210        220        230        240 
CDGAYSAVRK EIVKRPRYDF SQTYIEHGYL ELCIPPTAGG EFAMPHNYLH IWPRGQFMMI 

       250        260        270        280        290        300 
ALPNQDRTWT VTLFMPFTQF HSITDQGLLL DFFRQHFPDA IELIGRERLV KDFFKTKAQP 

       310        320        330        340        350        360 
LVMIKCRPYH IGAKALIIGD AAHAMVPFYG QGMNAGFEDC SVLTELFNQY GTDLARILPE 

       370        380        390        400        410        420 
FSEKRWEDAH AICDLAMYNY IEMRDLVTKR SYLLRKKLDE LLFWMMPNTW VPLYNSVSFS 

       430        440        450        460        470        480 
HMRYSKCIAN RAWQDKILTR VLYGASIASV AAIGGLCYRH VTMGHLERLS TRILSTFQLL 


KPKASV 

« Hide

References

[1]"The genome sequence of the malaria mosquito Anopheles gambiae."
Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F. expand/collapse author list , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L.
Science 298:129-149(2002) [PubMed: 12364791] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PEST.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAAB01008960 Genomic DNA. Translation: EAA11712.2.
RefSeqXP_315983.2. XM_315983.4.

3D structure databases

ProteinModelPortalQ7Q6A7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7Q6A7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaAGAP005948-RA; AGAP005948-PA; AGAP005948.
GeneID1276617.
KEGGaga:AgaP_AGAP005948.
VectorBaseAGAP005948. Anopheles gambiae.

Organism-specific databases

CTD1276617.

Phylogenomic databases

eggNOGinNOG08413.
GeneTreeEMGT00050000009966.
HOGENOMHBG430104.
OMAYFPDAIP.
OrthoDBEOG4K6DKV.
PhylomeDBQ7Q6A7.

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...

Entry information

Entry nameKMO_ANOGA
AccessionPrimary (citable) accession number: Q7Q6A7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: December 7, 2004
Last modified: December 14, 2011
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families