ID   HGD_RHOPA               Reviewed;         448 AA.
AC   Q6N0T9;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 102.
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};
GN   OrderedLocusNames=RPA4672;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
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; Evidence={ECO:0000255|HAMAP-
CC         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}.
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DR   EMBL; BX572608; CAE30112.1; -; Genomic_DNA.
DR   RefSeq; WP_011160204.1; NZ_CP116810.1.
DR   AlphaFoldDB; Q6N0T9; -.
DR   SMR; Q6N0T9; -.
DR   STRING; 258594.RPA4672; -.
DR   GeneID; 66895830; -.
DR   eggNOG; COG3508; Bacteria.
DR   HOGENOM; CLU_027174_0_0_5; -.
DR   PhylomeDB; Q6N0T9; -.
DR   UniPathway; UPA00139; UER00339.
DR   Proteomes; UP000001426; Chromosome.
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   CDD; cd07000; cupin_HGO_N; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   HAMAP; MF_00334; Homogentis_dioxygen; 1.
DR   InterPro; IPR046451; HgmA_C.
DR   InterPro; IPR046452; HgmA_N.
DR   InterPro; IPR005708; Homogentis_dOase.
DR   InterPro; IPR022950; Homogentis_dOase_bac.
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; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism;
KW   Reference proteome; Tyrosine catabolism.
FT   CHAIN           1..448
FT                   /note="Homogentisate 1,2-dioxygenase"
FT                   /id="PRO_0000225795"
FT   ACT_SITE        303
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         346
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         352
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         361
FT                   /ligand="homogentisate"
FT                   /ligand_id="ChEBI:CHEBI:16169"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         382
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         382
FT                   /ligand="homogentisate"
FT                   /ligand_id="ChEBI:CHEBI:16169"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
SQ   SEQUENCE   448 AA;  49761 MW;  1E3C3C8BB33EE45D CRC64;
     MNINAAPQIL GRSSQDITPG YMSGFGNSFE TEALPGALPV GRNSPQRCAY GLYAEQLSGS
     PFTAPRGANE RSWLYRIRPS VKHSGRFAKT DMGLWRSAPC FEHDLPIAQL RWDPPPMPQE
     ALTFLQGVRT MTTAGDVNTQ AGMATHLYLI TQSMVDQHFY NADGEMMFVP QQGSLRLVTE
     FGIITIEPAE IAVIPRGVKF RVELVDGPAR GYLCENYGGA FTLPERGPIG ANCLANSRDF
     LTPVAAYEDK DTPTELYVKW GGSLYVTKLP HSPIDVVAWH GNYAPYKYDL RTYSPVGAIG
     FDHPDPSIFT VLTSPSETPG TANIDFVIFP ERWMVADNTF RPPWYHMNIM SEFMGLIYGV
     YDAKPQGFVP GGASLHNMML PHGPDREAFD HASNGELKPV KLTGTMAFMF ETRYPQRVTE
     YAASSGLLQD DYADCWNGLE KRFDPNRP
//