ID   HGD_PSEPU               Reviewed;         433 AA.
AC   Q6EMI9;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 66.
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};
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   INDUCTION.
RC   STRAIN=U;
RX   PubMed=15262943; DOI=10.1128/jb.186.15.5062-5077.2004;
RA   Arias-Barrau E., Olivera E.R., Luengo J.M., Fernandez C., Galan B.,
RA   Garcia J.L., Diaz E., Minambres B.;
RT   "The homogentisate pathway: a central catabolic pathway involved in the
RT   degradation of L-phenylalanine, L-tyrosine, and 3-hydroxyphenylacetate in
RT   Pseudomonas putida.";
RL   J. Bacteriol. 186:5062-5077(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 2,5-dihydroxyphenylacetate to yield
CC       maleylacetoacetate. {ECO:0000269|PubMed:15262943}.
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   -!- INDUCTION: Induced by homogentisate and repressed by HmgR.
CC       {ECO:0000269|PubMed:15262943}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow in
CC       medium containing phenylalanine or tyrosine as the sole carbon sources,
CC       and accumulate homogentisate. {ECO:0000269|PubMed:15262943}.
CC   -!- SIMILARITY: Belongs to the homogentisate dioxygenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00334}.
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DR   EMBL; AY168855; AAO12527.1; -; Genomic_DNA.
DR   RefSeq; WP_049275436.1; NZ_QLLF01000019.1.
DR   AlphaFoldDB; Q6EMI9; -.
DR   SMR; Q6EMI9; -.
DR   STRING; 1240350.AMZE01000018_gene1082; -.
DR   eggNOG; COG3508; Bacteria.
DR   UniPathway; UPA00139; UER00339.
DR   GO; GO:0004411; F:homogentisate 1,2-dioxygenase activity; IMP:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IMP:UniProtKB.
DR   GO; GO:0006572; P:tyrosine catabolic process; IMP:UniProtKB.
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   2: Evidence at transcript level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism;
KW   Tyrosine catabolism.
FT   CHAIN           1..433
FT                   /note="Homogentisate 1,2-dioxygenase"
FT                   /id="PRO_0000428934"
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;  48024 MW;  F0C7F7D7CC197299 CRC64;
     MTRDTSPDLH YLSGFGNEFA SEALPGALPV GQNSPQRAPY GLYAELLSGT AFTMARSELR
     RTWLYRIRPS ALHPRFERLA RQPLTAPLGA INPNRLRWSP QPIPAEPTDF IEGWLPMVAN
     APAQKPAGVS IYIYCANRSM ERVFFNADGE LLLVPEQGRL RIATELGVME VGPLEIAVIP
     RGMKFRVELL DGQARGYIAE NHGAPLRIPE LGPIGSNGLA NPRDFLTPVA HYEEAEGPVQ
     LVQKFLGEHW ACELQHSPLD VVAWHGSNVP YKYDLRRFNT IGTVSFDHPD PSIFTVLTSP
     TSVHGLANMD FVIFPPRWMV AENTFRPPWF HRNLMNEFMG LISGAYDAKA EGFLPGGASL
     HGVMSAHGPD AETCEKAIAA DLAPHKIDNT MAFMFETSQV LRPSQQALEC PQLQADYDSC
     WATLPSTFNP NRR