ID   B4MWE2_DROWI            Unreviewed;       437 AA.
AC   B4MWE2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 85.
DE   RecName: Full=Homogentisate 1,2-dioxygenase {ECO:0000256|ARBA:ARBA00018757};
DE            EC=1.13.11.5 {ECO:0000256|ARBA:ARBA00013127};
DE   AltName: Full=Homogentisate oxygenase {ECO:0000256|ARBA:ARBA00030235};
DE   AltName: Full=Homogentisic acid oxidase {ECO:0000256|ARBA:ARBA00030437};
DE   AltName: Full=Homogentisicase {ECO:0000256|ARBA:ARBA00033225};
GN   Name=Dwil\GK14896 {ECO:0000313|EMBL:EDW76012.1};
GN   Synonyms=dwil_GLEANR_15182 {ECO:0000313|EMBL:EDW76012.1}, GK14896
GN   {ECO:0000313|EMBL:EDW76012.1};
GN   ORFNames=Dwil_GK14896 {ECO:0000313|EMBL:EDW76012.1};
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260 {ECO:0000313|EMBL:EDW76012.1, ECO:0000313|Proteomes:UP000007798};
RN   [1] {ECO:0000313|EMBL:EDW76012.1, ECO:0000313|Proteomes:UP000007798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 Genomes Consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
RN   [2] {ECO:0000313|EMBL:EDW76012.1, ECO:0000313|Proteomes:UP000007798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798};
RX   PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA   Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT   "Assembly reconciliation.";
RL   Bioinformatics 24:42-45(2008).
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         Evidence={ECO:0000256|ARBA:ARBA00000076};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962,
CC         ECO:0000256|PIRSR:PIRSR605708-2};
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 4/6.
CC       {ECO:0000256|ARBA:ARBA00004704}.
CC   -!- SIMILARITY: Belongs to the homogentisate dioxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007757}.
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; CH963857; EDW76012.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4MWE2; -.
DR   SMR; B4MWE2; -.
DR   FunCoup; B4MWE2; 57.
DR   STRING; 7260.B4MWE2; -.
DR   GeneID; 6641961; -.
DR   KEGG; dwi:6641961; -.
DR   eggNOG; KOG1417; Eukaryota.
DR   HOGENOM; CLU_027174_0_0_1; -.
DR   InParanoid; B4MWE2; -.
DR   OMA; MLPHGPD; -.
DR   OrthoDB; 1689029at2759; -.
DR   PhylomeDB; B4MWE2; -.
DR   UniPathway; UPA00139; UER00339.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0004411; F:homogentisate 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07000; cupin_HGO_N; 1.
DR   FunFam; 2.60.120.10:FF:000026; Homogentisate 1,2-dioxygenase; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR046451; HgmA_C.
DR   InterPro; IPR046452; HgmA_N.
DR   InterPro; IPR005708; Homogentis_dOase.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   NCBIfam; TIGR01015; hmgA; 1.
DR   PANTHER; PTHR11056; HOMOGENTISATE 1,2-DIOXYGENASE; 1.
DR   PANTHER; PTHR11056:SF0; HOMOGENTISATE 1,2-DIOXYGENASE; 1.
DR   Pfam; PF04209; HgmA_C; 1.
DR   Pfam; PF20510; HgmA_N; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR605708-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR605708-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007798};
KW   Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878}.
FT   DOMAIN          5..279
FT                   /note="Homogentisate 1,2-dioxygenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20510"
FT   DOMAIN          281..434
FT                   /note="Homogentisate 1,2-dioxygenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04209"
FT   ACT_SITE        292
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605708-1"
FT   BINDING         335
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605708-2"
FT   BINDING         341
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605708-2"
FT   BINDING         350
FT                   /ligand="homogentisate"
FT                   /ligand_id="ChEBI:CHEBI:16169"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605708-2"
FT   BINDING         371
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605708-2"
FT   BINDING         371
FT                   /ligand="homogentisate"
FT                   /ligand_id="ChEBI:CHEBI:16169"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605708-2"
SQ   SEQUENCE   437 AA;  49269 MW;  A06D0992F465542A CRC64;
     MSEYKYLSGF GSHFSSEDER CPNSLPIGQN SPQICPYKLY AEQLSGSAFT APRTENQRTW
     LYRRLPSAVH QPFKPFVGAK YFTQNWNEQP PNPNQLRWKP FDLPTERKKP VDFVQGLHTV
     CGAGDPRVRH GLAIHVYLCN VSMENSAFYN SDGDFLIVPQ QGVLDITTEL GKMTVAPNEI
     CVIPQGIRFA VGVDSVSRGY ILEVYDGHFC LPDLGPIGAN GLANPRDFQT PVAWFNDKQV
     EDFNVISKYQ GGLFVAKQNH TVFDVVAWHG NYVPFKYDLN KFMVINSVSF DHCDPSIFTV
     LTCPSLRPGT AIADFVIFPP RWSVQEHTFR PPYYHRNCMS EFMGLILGRY EAKEDGFAAG
     GATLHSMMTP HGPDVKCFDG ASKAKLVPER IAEGTQAFMF ETSLSLAVTK WGEETCQKLD
     AEYYECWQSL KDNFTIQ
//