ID   HGD_LEGPH               Reviewed;         416 AA.
AC   Q9S4T0; Q5ZW03;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 124.
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=lpg1285;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10438758; DOI=10.1128/jb.181.16.4879-4889.1999;
RA   Hales L.M., Shuman H.A.;
RT   "The Legionella pneumophila rpoS gene is required for growth within
RT   Acanthamoeba castellanii.";
RL   J. Bacteriol. 181:4879-4889(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD51397.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF117715; AAD51397.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE017354; AAU27368.1; -; Genomic_DNA.
DR   RefSeq; WP_010947016.1; NC_002942.5.
DR   RefSeq; YP_095315.1; NC_002942.5.
DR   AlphaFoldDB; Q9S4T0; -.
DR   SMR; Q9S4T0; -.
DR   STRING; 272624.lpg1285; -.
DR   PaxDb; 272624-lpg1285; -.
DR   GeneID; 66490419; -.
DR   KEGG; lpn:lpg1285; -.
DR   PATRIC; fig|272624.6.peg.1353; -.
DR   eggNOG; COG3508; Bacteria.
DR   HOGENOM; CLU_027174_0_0_6; -.
DR   OrthoDB; 9811253at2; -.
DR   UniPathway; UPA00139; UER00339.
DR   Proteomes; UP000000609; 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..416
FT                   /note="Homogentisate 1,2-dioxygenase"
FT                   /id="PRO_0000220248"
FT   ACT_SITE        275
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         318
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         324
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         333
FT                   /ligand="homogentisate"
FT                   /ligand_id="ChEBI:CHEBI:16169"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         354
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         354
FT                   /ligand="homogentisate"
FT                   /ligand_id="ChEBI:CHEBI:16169"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
SQ   SEQUENCE   416 AA;  47475 MW;  9E06F5AB9FFF3C9B CRC64;
     MYLQGFGNYH HSEAVKGALP PNQNSPQHCS LGLYAEQLSG TAFTRPRHNN LRSWLYRILP
     TVTQGTYYPY EFNIMQPFVD ELSPNAMRWS PLYNSSQIKC DFVEGLFHIA GSPLVNTYTY
     YCNHSMSDKY FANNDGELLF VPYAGEIHLH TEFGKLMLSS GSIAVIPRGV KFKVEVISKE
     AKGYLCENSG NPLTLPQLGP IGANGLANPR HFQYPVAAFE NSGSEHTIIC KNQKKLWFTV
     CNHSPLNVVA WHGNYAPYCY DLSLFNTINT VSFDHPDPSI FTVLTSESEI PGVSNLDFVI
     FPPRWMVAEH TFRPPYFHRN YMNELMGLVY GEYDAKKEGF IPGGISIHNC MTPHGPDYES
     YEIAASQDLK PNYINSLAFM FETKDYWQVT EQAYRHPSRQ MDYLNCWQGF KIEFSQ
//