ID   HGD_CUPPJ               Reviewed;         439 AA.
AC   Q46UA4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Homogentisate 1,2-dioxygenase {ECO:0000255|HAMAP-Rule:MF_00334};
DE            Short=HGDO {ECO:0000255|HAMAP-Rule:MF_00334};
DE            EC=1.13.11.5 {ECO:0000255|HAMAP-Rule:MF_00334};
DE   AltName: Full=Homogentisate oxygenase {ECO:0000255|HAMAP-Rule:MF_00334};
DE   AltName: Full=Homogentisic acid oxidase {ECO:0000255|HAMAP-Rule:MF_00334};
DE   AltName: Full=Homogentisicase {ECO:0000255|HAMAP-Rule:MF_00334};
GN   Name=hmgA {ECO:0000255|HAMAP-Rule:MF_00334}; OrderedLocusNames=Reut_B3923;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
CC   -!- FUNCTION: Involved in the catabolism of homogentisate (2,5-
CC       dihydroxyphenylacetate or 2,5-OH-PhAc), a central intermediate in the
CC       degradation of phenylalanine and tyrosine. Catalyzes the oxidative ring
CC       cleavage of the aromatic ring of homogentisate to yield
CC       maleylacetoacetate. {ECO:0000255|HAMAP-Rule:MF_00334}.
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:0000255|HAMAP-Rule:MF_00334};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00334};
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 4/6.
CC       {ECO:0000255|HAMAP-Rule:MF_00334}.
CC   -!- SUBUNIT: Hexamer; dimer of trimers. {ECO:0000255|HAMAP-Rule:MF_00334}.
CC   -!- SIMILARITY: Belongs to the homogentisate dioxygenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00334}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAZ63280.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000091; AAZ63280.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041680146.1; NC_007348.1.
DR   AlphaFoldDB; Q46UA4; -.
DR   SMR; Q46UA4; -.
DR   STRING; 264198.Reut_B3923; -.
DR   PRIDE; Q46UA4; -.
DR   EnsemblBacteria; AAZ63280; AAZ63280; Reut_B3923.
DR   KEGG; reu:Reut_B3923; -.
DR   eggNOG; COG3508; Bacteria.
DR   HOGENOM; CLU_027174_0_0_4; -.
DR   OMA; FMFETRW; -.
DR   OrthoDB; 193687at2; -.
DR   UniPathway; UPA00139; UER00339.
DR   GO; GO:0004411; F:homogentisate 1,2-dioxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.120.10; -; 1.
DR   HAMAP; MF_00334; Homogentis_dioxygen; 1.
DR   InterPro; IPR005708; Homogentis_dOase.
DR   InterPro; IPR022950; Homogentis_dOase_bac.
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   3: Inferred from homology;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism;
KW   Tyrosine catabolism.
FT   CHAIN           1..439
FT                   /note="Homogentisate 1,2-dioxygenase"
FT                   /id="PRO_0000225794"
FT   ACT_SITE        293
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         336
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         342
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         351
FT                   /ligand="homogentisate"
FT                   /ligand_id="ChEBI:CHEBI:16169"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         372
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         372
FT                   /ligand="homogentisate"
FT                   /ligand_id="ChEBI:CHEBI:16169"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
SQ   SEQUENCE   439 AA;  48732 MW;  293FAF36EFC3752D CRC64;
     MNLTHTQLAE HGYMSGFANE FATEALPGAL PVGQNSPQRA PYGLYAEQLS GTAFTAPRAH
     NRRSWLYRIR PGAVHKPFTL VEQSRFLSRF DEVPPSPNQM RWSPPAMPTT PTDFIDGIVT
     MAGNGGPDAM TGCGIHLYLA NQSMQDRFFY NADGEMLIVP QQGRVRFVTE MGRLDVEPQE
     IVVIPRGVRF RVELPDGEAR GYICENYGAL FKLPDLGVIG SNGLANPRDF MTPVAAYEDR
     EGDFELVAKF QGNLWRADIG HSPLDVVAWH GNFAPYKYDL RRFNTIGSIS FDHPDPSIFL
     VLQSPSDTPG VDTIDFVIFG PRWLAMENSF RPPWFHRNIA SEFMGLITGV YDAKADGFAP
     GGASLHNCMS GHGPDADTFA KATSADTSTP HHITDTMAFM FETPGVIRPT PYAARSASLQ
     QDYYTCWQGL KKHFNPNVR