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UniProtKB/Swiss-Prot entry Q9VKJ0


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

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Entry information
Entry name HGD_DROME
Primary accession number Q9VKJ0
Secondary accession number Q86P40
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on July 25, 2003 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 57)
Name and origin of the protein
Protein name Homogentisate 1,2-dioxygenase
Synonyms EC 1.13.11.5
Homogentisic acid oxidase
Homogentisate oxygenase
Homogentisicase
Gene name
Name: hgo
ORFNames: CG4779
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Schmidt S.R.;
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Embryo;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(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
AF131124; AAF36489.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014134; AAF53078.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT003496; AAO39500.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_523544.2; -.
UniGene Dm.2807
3D structure databases
HSSP Q93099; 1EYB. [HSSP ENTRY / PDB]
ModBase Q9VKJ0.
Protein-protein interaction databases
DIP DIP:23788N; -.
IntAct Q9VKJ0; -.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-008534-MON; -.
Organism-specific databases
FlyBase FBgn0040211; hgo.
Gene expression databases
ArrayExpress Q9VKJ0; -.
GermOnline CG4779; Drosophila melanogaster.
Ontologies
GO
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR005708; Homogentis_dOase.
Graphical view of domain structure.
PANTHER PTHR11056; Homogentis_dOase; 1.
Pfam PF04209; HgmA; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01015; hmgA; 1.
BLOCKS Q9VKJ0.
Genome annotation databases
Ensembl CG4779; Drosophila melanogaster. [Contig view]
GeneID 34552; -.
KEGG dme:Dmel_CG4779; -.
NMPDR fig|7227.3.peg.1976; -.
Phylogenomic databases
HOGENOM Q9VKJ0; -.
Other
ProtoNet Q9VKJ0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism; Tyrosine catabolism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   439  439     Homogentisate 1,2-dioxygenase. PRO_0000220242
METAL   335   335        Iron (By similarity). 
METAL   341   341        Iron (By similarity). 
METAL   371   371        Iron (By similarity). 
CONFLICT   96   106        Missing (in Ref. 1; AAF36489). 
Sequence information
Length: 439 AA [This is the length of the unprocessed precursor] Molecular weight: 49398 Da [This is the MW of the unprocessed precursor] CRC64: 08418138B9600FE1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSEYKYLSGF GSHFSSEDER YPNSLPVGQN SPQVCPYKLY AEQLSGSAFT APRTENMRTW 

        70         80         90        100        110        120 
LYRKLPSAAH LPFQPFKGAE YFSQNWDEQP PNPNQLRWKP FDLPPKDGKN VNFVEGLHTV 

       130        140        150        160        170        180 
CGAGDPRSRH GLAIHIYSCN GSMDNSAFYN SDGDFLIVPQ QGVLDITTEF GRMSVAPNEI 

       190        200        210        220        230        240 
CVIPQGIRFA VNVDSPSRGY ILEVYDDHFV LPDLGPIGAN GLANPRDFET PVAWFDDRDV 

       250        260        270        280        290        300 
KDFQVISKFQ GRLFVAKQNH TVFDVVAWHG NYVPFKYDLS KFMVINSVSF DHCDPSIFTV 

       310        320        330        340        350        360 
LTCPSLRAGT AIADFVIFPP RWSVQEHTFR PPYYHRNCMS EFMGLILGKY EAKEDGFAAG 

       370        380        390        400        410        420 
GATLHSMMTP HGPDVKCFEG ASNAKLVPER VAEGTQAFMF ESSLSLAVTK WGEETCQKLD 

       430 
AAYYECWQAL KNNFQITKN 

Q9VKJ0 in FASTA format

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