ID   HGD_PSEP1               Reviewed;         433 AA.
AC   A5W8Z1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=Pput_4481;
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000712; ABQ80601.1; -; Genomic_DNA.
DR   RefSeq; WP_003251670.1; NC_009512.1.
DR   AlphaFoldDB; A5W8Z1; -.
DR   SMR; A5W8Z1; -.
DR   STRING; 351746.Pput_4481; -.
DR   EnsemblBacteria; ABQ80601; ABQ80601; Pput_4481.
DR   KEGG; ppf:Pput_4481; -.
DR   eggNOG; COG3508; Bacteria.
DR   HOGENOM; CLU_027174_0_0_6; -.
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..433
FT                   /note="Homogentisate 1,2-dioxygenase"
FT                   /id="PRO_1000019535"
FT   ACT_SITE        288
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         331
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         337
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         346
FT                   /ligand="homogentisate"
FT                   /ligand_id="ChEBI:CHEBI:16169"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         367
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         367
FT                   /ligand="homogentisate"
FT                   /ligand_id="ChEBI:CHEBI:16169"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
SQ   SEQUENCE   433 AA;  47972 MW;  E17B29B7B84A5E5E CRC64;
     MNRDTSPDLH YLSGFGNEFA SEALPGALPV GQNSPQKAPY GLYAELLSGT AFTMARSELR
     RTWLYRIRPS ALHPRFERLA RQPLGGPLGG INPNRLRWSP QPIPAEPTDF IEGWLPMAAN
     AAAEKPAGVS IYIYCANRSM ERVFFNADGE LLLVPEQGRL RIATELGVME VEPLEIAVIP
     RGMKFRVELL DGQARGYIAE NHGAPLRLPD LGPIGSNGLA NPRDFLTPVA HYEEAEGPVQ
     LVQKFLGEHW ACELQHSPLD VVAWHGSNVP YKYDLRRFNT IGTVSFDHPD PSIFTVLTSP
     TSVHGMANMD FVIFPPRWMV AENTFRPPWF HRNLMNEFMG LINGAYDAKA EGFLPGGASL
     HGVMSAHGPD AETCEKAIAA DLAPHKIDNT MAFMFETSQV LRPSLQALEC PQLQADYDSC
     WATLPSTFNP NRR