ID   HGD_PSEF5               Reviewed;         434 AA.
AC   Q4KI35;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, 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};
GN   OrderedLocusNames=PFL_0967;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY90254.1; -; Genomic_DNA.
DR   RefSeq; WP_011059321.1; NC_004129.6.
DR   AlphaFoldDB; Q4KI35; -.
DR   SMR; Q4KI35; -.
DR   STRING; 220664.PFL_0967; -.
DR   KEGG; pfl:PFL_0967; -.
DR   PATRIC; fig|220664.5.peg.992; -.
DR   eggNOG; COG3508; Bacteria.
DR   HOGENOM; CLU_027174_0_0_6; -.
DR   UniPathway; UPA00139; UER00339.
DR   Proteomes; UP000008540; 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   Tyrosine catabolism.
FT   CHAIN           1..434
FT                   /note="Homogentisate 1,2-dioxygenase"
FT                   /id="PRO_0000225791"
FT   ACT_SITE        289
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         332
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         338
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         347
FT                   /ligand="homogentisate"
FT                   /ligand_id="ChEBI:CHEBI:16169"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         368
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT   BINDING         368
FT                   /ligand="homogentisate"
FT                   /ligand_id="ChEBI:CHEBI:16169"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
SQ   SEQUENCE   434 AA;  47945 MW;  4C32086AE5EEE7A8 CRC64;
     MNLDSSASAL SYQSGFGNEF ASEALPGALP VGQNSPQKAP YGLYAELFSG TAFTMTRSEA
     RRTWMYRIQP SAKHPAFAKL ARQLAGGPLG EVTPNRLRWS PLQIPSEPTD FIDGLVAMVA
     NSAAQKPAGI SVYHYRANRS MERVFFNADG ELLLVPELGR LRIVTELGML DLEPLEIAVL
     PRGLKFRIEL LDPQARGYVA ENHGAPLRLP DLGPIGSNGL ANPRDFLAPV AHYEDLRQPT
     TLVQKYLGEL WGCELDHSPL NVVAWHGNNV PYKYDLRRFN TIGTVSFDHP DPSIFTVLTS
     PTSVPGLANL DFVIFPPRWM VAENTFRPPW FHRNLMNEFM GLIQGAYDAK AEGFLPGGAS
     LHSCMSAHGP DGETCTKAIN AQLQPAKIDN TMAFMFETSQ VLRPSQFALE CPELQNDYDA
     CWASLPVTFN PNRR
//