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Protein

Homogentisate 1,2-dioxygenase

Gene

hgo

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Homogentisate + O2 = 4-maleylacetoacetate.

Cofactori

Fe cationBy similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi335 – 3351IronBy similarity
Metal bindingi341 – 3411IronBy similarity
Metal bindingi371 – 3711IronBy similarity

GO - Molecular functioni

  1. homogentisate 1,2-dioxygenase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. L-phenylalanine catabolic process Source: UniProtKB-UniPathway
  2. tyrosine catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Phenylalanine catabolism, Tyrosine catabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_203229. Phenylalanine and tyrosine catabolism.
UniPathwayiUPA00139; UER00339.

Names & Taxonomyi

Protein namesi
Recommended name:
Homogentisate 1,2-dioxygenase (EC:1.13.11.5)
Alternative name(s):
Homogentisate oxygenase
Homogentisic acid oxidase
Homogentisicase
Gene namesi
Name:hgo
ORF Names:CG4779
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0040211. hgo.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439Homogentisate 1,2-dioxygenasePRO_0000220242Add
BLAST

Proteomic databases

PaxDbiQ9VKJ0.

Expressioni

Gene expression databases

BgeeiQ9VKJ0.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself1EBI-150349,EBI-150349

Protein-protein interaction databases

BioGridi60614. 1 interaction.
DIPiDIP-23788N.
MINTiMINT-927986.

Structurei

3D structure databases

ProteinModelPortaliQ9VKJ0.
SMRiQ9VKJ0. Positions 2-412.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the homogentisate dioxygenase family.Curated

Phylogenomic databases

eggNOGiCOG3508.
GeneTreeiENSGT00390000004601.
InParanoidiQ9VKJ0.
KOiK00451.
OMAiKSHFTPN.
OrthoDBiEOG7PP58Z.
PhylomeDBiQ9VKJ0.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR005708. Homogentis_dOase.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR11056. PTHR11056. 1 hit.
PfamiPF04209. HgmA. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR01015. hmgA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9VKJ0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEYKYLSGF GSHFSSEDER YPNSLPVGQN SPQVCPYKLY AEQLSGSAFT
60 70 80 90 100
APRTENMRTW LYRKLPSAAH LPFQPFKGAE YFSQNWDEQP PNPNQLRWKP
110 120 130 140 150
FDLPPKDGKN VNFVEGLHTV CGAGDPRSRH GLAIHIYSCN GSMDNSAFYN
160 170 180 190 200
SDGDFLIVPQ QGVLDITTEF GRMSVAPNEI CVIPQGIRFA VNVDSPSRGY
210 220 230 240 250
ILEVYDDHFV LPDLGPIGAN GLANPRDFET PVAWFDDRDV KDFQVISKFQ
260 270 280 290 300
GRLFVAKQNH TVFDVVAWHG NYVPFKYDLS KFMVINSVSF DHCDPSIFTV
310 320 330 340 350
LTCPSLRAGT AIADFVIFPP RWSVQEHTFR PPYYHRNCMS EFMGLILGKY
360 370 380 390 400
EAKEDGFAAG GATLHSMMTP HGPDVKCFEG ASNAKLVPER VAEGTQAFMF
410 420 430
ESSLSLAVTK WGEETCQKLD AAYYECWQAL KNNFQITKN
Length:439
Mass (Da):49,398
Last modified:July 25, 2003 - v3
Checksum:i08418138B9600FE1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 10611Missing in AAF36489. 1 PublicationCuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF131124 Genomic DNA. Translation: AAF36489.1.
AE014134 Genomic DNA. Translation: AAF53078.2.
BT003496 mRNA. Translation: AAO39500.1.
RefSeqiNP_523544.2. NM_078820.3.
UniGeneiDm.2807.

Genome annotation databases

EnsemblMetazoaiFBtr0080201; FBpp0079790; FBgn0040211.
GeneIDi34552.
KEGGidme:Dmel_CG4779.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF131124 Genomic DNA. Translation: AAF36489.1.
AE014134 Genomic DNA. Translation: AAF53078.2.
BT003496 mRNA. Translation: AAO39500.1.
RefSeqiNP_523544.2. NM_078820.3.
UniGeneiDm.2807.

3D structure databases

ProteinModelPortaliQ9VKJ0.
SMRiQ9VKJ0. Positions 2-412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60614. 1 interaction.
DIPiDIP-23788N.
MINTiMINT-927986.

Proteomic databases

PaxDbiQ9VKJ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0080201; FBpp0079790; FBgn0040211.
GeneIDi34552.
KEGGidme:Dmel_CG4779.

Organism-specific databases

CTDi34552.
FlyBaseiFBgn0040211. hgo.

Phylogenomic databases

eggNOGiCOG3508.
GeneTreeiENSGT00390000004601.
InParanoidiQ9VKJ0.
KOiK00451.
OMAiKSHFTPN.
OrthoDBiEOG7PP58Z.
PhylomeDBiQ9VKJ0.

Enzyme and pathway databases

UniPathwayiUPA00139; UER00339.
ReactomeiREACT_203229. Phenylalanine and tyrosine catabolism.

Miscellaneous databases

GenomeRNAii34552.
NextBioi789029.
PROiQ9VKJ0.

Gene expression databases

BgeeiQ9VKJ0.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR005708. Homogentis_dOase.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR11056. PTHR11056. 1 hit.
PfamiPF04209. HgmA. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR01015. hmgA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Schmidt S.R.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiHGD_DROME
AccessioniPrimary (citable) accession number: Q9VKJ0
Secondary accession number(s): Q86P40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 25, 2003
Last modified: January 7, 2015
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.