ID   HGD_EMENI               Reviewed;         448 AA.
AC   Q00667; C8VKJ8; Q5BC33;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Homogentisate 1,2-dioxygenase;
DE            EC=1.13.11.5 {ECO:0000269|PubMed:7673153};
DE   AltName: Full=Homogentisate oxygenase;
DE   AltName: Full=Homogentisic acid oxidase;
DE   AltName: Full=Homogentisicase;
GN   Name=hmgA; ORFNames=AN1897;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND INDUCTION.
RC   STRAIN=biA1;
RX   PubMed=7673153; DOI=10.1074/jbc.270.36.21199;
RA   Fernandez-Canon J.M., Penalva M.A.;
RT   "Molecular characterization of a gene encoding a homogentisate dioxygenase
RT   from Aspergillus nidulans and identification of its human and plant
RT   homologues.";
RL   J. Biol. Chem. 270:21199-21205(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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:0000269|PubMed:7673153};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 4/6.
CC   -!- INDUCTION: During growth with phenylacetate and phenylalanine.
CC       {ECO:0000269|PubMed:7673153}.
CC   -!- SIMILARITY: Belongs to the homogentisate dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; U30797; AAC49071.1; -; Genomic_DNA.
DR   EMBL; AJ001836; CAA05042.1; -; Genomic_DNA.
DR   EMBL; AACD01000029; EAA65062.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF85779.1; -; Genomic_DNA.
DR   PIR; A57435; A57435.
DR   RefSeq; XP_659501.1; XM_654409.1.
DR   AlphaFoldDB; Q00667; -.
DR   SMR; Q00667; -.
DR   STRING; 227321.Q00667; -.
DR   EnsemblFungi; CBF85779; CBF85779; ANIA_01897.
DR   GeneID; 2874820; -.
DR   KEGG; ani:AN1897.2; -.
DR   VEuPathDB; FungiDB:AN1897; -.
DR   eggNOG; KOG1417; Eukaryota.
DR   HOGENOM; CLU_027174_0_0_1; -.
DR   InParanoid; Q00667; -.
DR   OMA; MLPHGPD; -.
DR   OrthoDB; 525at2759; -.
DR   BioCyc; MetaCyc:MONOMER-12040; -.
DR   BRENDA; 1.13.11.5; 517.
DR   UniPathway; UPA00139; UER00339.
DR   Proteomes; UP000000560; Chromosome VII.
DR   GO; GO:0004411; F:homogentisate 1,2-dioxygenase activity; IDA:AspGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IMP:AspGD.
DR   GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07000; cupin_HGO_N; 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   1: Evidence at protein level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism;
KW   Reference proteome; Tyrosine catabolism.
FT   CHAIN           1..448
FT                   /note="Homogentisate 1,2-dioxygenase"
FT                   /id="PRO_0000220245"
FT   BINDING         340
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         346
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         377
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   448 AA;  50168 MW;  4AE6414823A04C0D CRC64;
     MPVTEFSFKD PYTYQNGFDS YHESEAIEGA LPVGHNSPQK APYGLYAEKL SGTAFTAPRH
     ENKQTWVYRI LPAAAHENFV EEDASSYHTL SDAKKLQHIP NQLRWDPFDL DETVDWVHGL
     HLVAGSGDPT VKQGLGILLY AAGKDMGKEA FYSADGDFLI VAQHGVLDIQ TELGRLLVRP
     NEICVIPRGV RYRVTLPDGP VRGYICELYQ GHYQLPELGP IGSNGLANAR DFQAPVAAFD
     DEEGPTEYRL YSKFNNHLFS ARQDHTPFDI VAWHGNYYPY KYDLGRFNTM GSVSFDHPDP
     SIYTVLTGPS DHVGTAIADF VIFPPRWLVA EKTFRPPWYH RNTMSEFMGL ITGNYDAKTG
     GGFQPAGASL HNIMSAHGPD MHAFEGASNA DLKPTKIGDG SMAFMFESSL MVGVSEWGLK
     TCQKVQEEYN EHSWQPLKRH FKDPRKAQ
//