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Q9VKJ0

- HGD_DROME

UniProt

Q9VKJ0 - HGD_DROME

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Protein

Homogentisate 1,2-dioxygenase

Gene
hgo, CG4779
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Homogentisate + O2 = 4-maleylacetoacetate.

Cofactori

Iron By similarity.

Pathwayi

Sites

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

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3508.
GeneTreeiENSGT00390000004601.
InParanoidiQ9VKJ0.
KOiK00451.
OMAiTTETHKL.
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

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MSEYKYLSGF GSHFSSEDER YPNSLPVGQN SPQVCPYKLY AEQLSGSAFT    50
APRTENMRTW LYRKLPSAAH LPFQPFKGAE YFSQNWDEQP PNPNQLRWKP 100
FDLPPKDGKN VNFVEGLHTV CGAGDPRSRH GLAIHIYSCN GSMDNSAFYN 150
SDGDFLIVPQ QGVLDITTEF GRMSVAPNEI CVIPQGIRFA VNVDSPSRGY 200
ILEVYDDHFV LPDLGPIGAN GLANPRDFET PVAWFDDRDV KDFQVISKFQ 250
GRLFVAKQNH TVFDVVAWHG NYVPFKYDLS KFMVINSVSF DHCDPSIFTV 300
LTCPSLRAGT AIADFVIFPP RWSVQEHTFR PPYYHRNCMS EFMGLILGKY 350
EAKEDGFAAG GATLHSMMTP HGPDVKCFEG ASNAKLVPER VAEGTQAFMF 400
ESSLSLAVTK WGEETCQKLD AAYYECWQAL KNNFQITKN 439
Length:439
Mass (Da):49,398
Last modified:July 25, 2003 - v3
Checksum:i08418138B9600FE1
GO

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF131124 Genomic DNA. Translation: AAF36489.1.
AE014134 Genomic DNA. Translation: AAF53078.2.
BT003496 mRNA. Translation: AAO39500.1.
RefSeqiNP_523544.2. NM_078820.2.
UniGeneiDm.2807.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF131124 Genomic DNA. Translation: AAF36489.1 .
AE014134 Genomic DNA. Translation: AAF53078.2 .
BT003496 mRNA. Translation: AAO39500.1 .
RefSeqi NP_523544.2. NM_078820.2.
UniGenei Dm.2807.

3D structure databases

ProteinModelPortali Q9VKJ0.
SMRi Q9VKJ0. Positions 2-412.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 60614. 1 interaction.
DIPi DIP-23788N.
MINTi MINT-927986.

Proteomic databases

PaxDbi Q9VKJ0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0080201 ; FBpp0079790 ; FBgn0040211 .
GeneIDi 34552.
KEGGi dme:Dmel_CG4779.

Organism-specific databases

CTDi 34552.
FlyBasei FBgn0040211. hgo.

Phylogenomic databases

eggNOGi COG3508.
GeneTreei ENSGT00390000004601.
InParanoidi Q9VKJ0.
KOi K00451.
OMAi TTETHKL.
OrthoDBi EOG7PP58Z.
PhylomeDBi Q9VKJ0.

Enzyme and pathway databases

UniPathwayi UPA00139 ; UER00339 .
Reactomei REACT_203229. Phenylalanine and tyrosine catabolism.

Miscellaneous databases

GenomeRNAii 34552.
NextBioi 789029.
PROi Q9VKJ0.

Gene expression databases

Bgeei Q9VKJ0.

Family and domain databases

Gene3Di 2.60.120.10. 2 hits.
InterProi IPR005708. Homogentis_dOase.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view ]
PANTHERi PTHR11056. PTHR11056. 1 hit.
Pfami PF04209. HgmA. 1 hit.
[Graphical view ]
SUPFAMi SSF51182. SSF51182. 1 hit.
TIGRFAMsi TIGR01015. hmgA. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 104 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

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