ID HGD_BRADU Reviewed; 448 AA. AC Q89XH1; DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 108. 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=bll0343; OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / OS NBRC 14792 / USDA 110). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Bradyrhizobium. OX NCBI_TaxID=224911; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110; RX PubMed=12597275; DOI=10.1093/dnares/9.6.189; RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.; RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium RT Bradyrhizobium japonicum USDA110."; RL DNA Res. 9:189-197(2002). 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=BAC45608.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000040; BAC45608.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_766983.1; NC_004463.1. DR RefSeq; WP_038967448.1; NZ_CP011360.1. DR AlphaFoldDB; Q89XH1; -. DR SMR; Q89XH1; -. DR STRING; 224911.AAV28_40965; -. DR EnsemblBacteria; BAC45608; BAC45608; BAC45608. DR GeneID; 64020202; -. DR KEGG; bja:bll0343; -. DR PATRIC; fig|224911.44.peg.8868; -. DR eggNOG; COG3508; Bacteria. DR HOGENOM; CLU_027174_0_0_5; -. DR InParanoid; Q89XH1; -. DR OrthoDB; 9811253at2; -. DR UniPathway; UPA00139; UER00339. DR Proteomes; UP000002526; Chromosome. DR GO; GO:0004411; F:homogentisate 1,2-dioxygenase activity; IBA:GO_Central. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central. 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; 2. 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_0000220246" 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; 49780 MW; F6DD465E68735D3C CRC64; MNINTSPDQI IRSSAQVTPG YMSGFGNSFE TEALPGALPI GRNSPQRCAY GLYAEQLSGS PFTAPRGTNE RSWLYRIRPS VKHSGRFEKA DAGLWRSAPC HEYDLPIAQM RWDPTPVPKE EVTFVQGVQT MTTAGDVNTQ AGMAAHVYLI TKSMVDQHFY NADGELMFVL QQGNLRLVTE FGRIDAEPGE IVVIPRGVKF RVEIPNGPAR GYLCENYGGA FTLPERGPIG ANCLANARDF LTPVANYEDK DTPTELFVKW GGSLFKTTLP HSPIDVVAWH GNYAPYKYDL RTFSPVGAIG FDHPDPSIFT VLTSPSETAG TANIDFVIFP ERWMVADNTF RPPWYHMNIM SEFMGLIYGV YDAKPQGFVP GGMSLHNCML PHGPDRDAFE HASNGELKPV KLTGTMAFMF ETRYPQRVTA HAANASTLQD DYADCWKGLE KRFDPNRP //