HGD_DROME
ID HGD_DROME Reviewed; 439 AA.
AC Q9VKJ0; Q86P40;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Homogentisate 1,2-dioxygenase;
DE EC=1.13.11.5;
DE AltName: Full=Homogentisate oxygenase;
DE AltName: Full=Homogentisic acid oxidase;
DE AltName: Full=Homogentisicase;
GN Name=hgo; ORFNames=CG4779;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Schmidt S.R.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=homogentisate + O2 = 4-maleylacetoacetate + H(+);
CC Xref=Rhea:RHEA:15449, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16169, ChEBI:CHEBI:17105; EC=1.13.11.5;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 4/6.
CC -!- SIMILARITY: Belongs to the homogentisate dioxygenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF131124; AAF36489.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53078.2; -; Genomic_DNA.
DR EMBL; BT003496; AAO39500.1; -; mRNA.
DR RefSeq; NP_523544.2; NM_078820.3.
DR AlphaFoldDB; Q9VKJ0; -.
DR SMR; Q9VKJ0; -.
DR BioGRID; 60614; 1.
DR DIP; DIP-23788N; -.
DR STRING; 7227.FBpp0079790; -.
DR PaxDb; Q9VKJ0; -.
DR PRIDE; Q9VKJ0; -.
DR DNASU; 34552; -.
DR EnsemblMetazoa; FBtr0080201; FBpp0079790; FBgn0040211.
DR GeneID; 34552; -.
DR KEGG; dme:Dmel_CG4779; -.
DR CTD; 34552; -.
DR FlyBase; FBgn0040211; hgo.
DR VEuPathDB; VectorBase:FBgn0040211; -.
DR eggNOG; KOG1417; Eukaryota.
DR GeneTree; ENSGT00390000004601; -.
DR HOGENOM; CLU_027174_0_0_1; -.
DR InParanoid; Q9VKJ0; -.
DR OMA; FMFETRW; -.
DR OrthoDB; 795654at2759; -.
DR PhylomeDB; Q9VKJ0; -.
DR Reactome; R-DME-8963684; Tyrosine catabolism.
DR UniPathway; UPA00139; UER00339.
DR BioGRID-ORCS; 34552; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34552; -.
DR PRO; PR:Q9VKJ0; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0040211; Expressed in capitellum (Drosophila) and 11 other tissues.
DR Genevisible; Q9VKJ0; DM.
DR GO; GO:0004411; F:homogentisate 1,2-dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR005708; Homogentis_dOase.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR11056; PTHR11056; 1.
DR Pfam; PF04209; HgmA; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
DR TIGRFAMs; TIGR01015; hmgA; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism;
KW Reference proteome; Tyrosine catabolism.
FT CHAIN 1..439
FT /note="Homogentisate 1,2-dioxygenase"
FT /id="PRO_0000220242"
FT BINDING 335
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 96..106
FT /note="Missing (in Ref. 1; AAF36489)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 49398 MW; 08418138B9600FE1 CRC64;
MSEYKYLSGF GSHFSSEDER YPNSLPVGQN SPQVCPYKLY AEQLSGSAFT APRTENMRTW
LYRKLPSAAH LPFQPFKGAE YFSQNWDEQP PNPNQLRWKP FDLPPKDGKN VNFVEGLHTV
CGAGDPRSRH GLAIHIYSCN GSMDNSAFYN SDGDFLIVPQ QGVLDITTEF GRMSVAPNEI
CVIPQGIRFA VNVDSPSRGY ILEVYDDHFV LPDLGPIGAN GLANPRDFET PVAWFDDRDV
KDFQVISKFQ GRLFVAKQNH TVFDVVAWHG NYVPFKYDLS KFMVINSVSF DHCDPSIFTV
LTCPSLRAGT AIADFVIFPP RWSVQEHTFR PPYYHRNCMS EFMGLILGKY EAKEDGFAAG
GATLHSMMTP HGPDVKCFEG ASNAKLVPER VAEGTQAFMF ESSLSLAVTK WGEETCQKLD
AAYYECWQAL KNNFQITKN
