ID HGD_RHIME Reviewed; 453 AA. AC Q9X4F5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 117. 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 ECO:0000303|PubMed:10220173}; OrderedLocusNames=R02939; GN ORFNames=SMc03208; OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium OS meliloti). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=266834; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN TYROSINE DEGRADATION, RP INDUCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=1021; RX PubMed=10220173; DOI=10.1099/13500872-145-4-935; RA Milcamps A., de Bruijn F.J.; RT "Identification of a novel nutrient-deprivation-induced Sinorhizobium RT meliloti gene (hmgA) involved in the degradation of tyrosine."; RL Microbiology 145:935-947(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11481430; DOI=10.1073/pnas.161294398; RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T., RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., RA Thebault P., Vandenbol M., Weidner S., Galibert F.; RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium RT meliloti strain 1021."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11474104; DOI=10.1126/science.1060966; RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., RA Wong K., Yeh K.-C., Batut J.; RT "The composite genome of the legume symbiont Sinorhizobium meliloti."; RL Science 293:668-672(2001). 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 ECO:0000305|PubMed:10220173}. 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 -!- INDUCTION: By nitrogen and carbon deprivation as well as in the CC presence of tyrosine. Also induced by phenylalanine, but only in CC nitrogen-free medium. {ECO:0000269|PubMed:10220173}. CC -!- DISRUPTION PHENOTYPE: Mutant is unable to use tyrosine as carbon CC source, lacks homogentisate dioxygenase activity, produces a melanin- CC like pigment and is affected in stationary-phase survival. CC {ECO:0000269|PubMed:10220173}. CC -!- SIMILARITY: Belongs to the homogentisate dioxygenase family. CC {ECO:0000255|HAMAP-Rule:MF_00334}. 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; AF109131; AAD29874.1; -; Genomic_DNA. DR EMBL; AL591688; CAC47518.1; -; Genomic_DNA. DR RefSeq; NP_387045.1; NC_003047.1. DR RefSeq; WP_010970302.1; NC_003047.1. DR AlphaFoldDB; Q9X4F5; -. DR SMR; Q9X4F5; -. DR EnsemblBacteria; CAC47518; CAC47518; SMc03208. DR GeneID; 61604399; -. DR KEGG; sme:SMc03208; -. DR PATRIC; fig|266834.11.peg.4461; -. DR eggNOG; COG3508; Bacteria. DR HOGENOM; CLU_027174_0_0_5; -. DR OrthoDB; 9811253at2; -. DR UniPathway; UPA00139; UER00339. DR Proteomes; UP000001976; 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 1: Evidence at protein level; KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism; KW Reference proteome; Tyrosine catabolism. FT CHAIN 1..453 FT /note="Homogentisate 1,2-dioxygenase" FT /id="PRO_0000220254" FT REGION 1..42 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 306 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334" FT BINDING 349 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334" FT BINDING 355 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334" FT BINDING 364 FT /ligand="homogentisate" FT /ligand_id="ChEBI:CHEBI:16169" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334" FT BINDING 385 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334" FT BINDING 385 FT /ligand="homogentisate" FT /ligand_id="ChEBI:CHEBI:16169" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334" SQ SEQUENCE 453 AA; 50756 MW; AC49AEFF0C783200 CRC64; MLEKAEKQRR AGSGQQRAAG YMPGFGNDFE TESLPGALPQ GQNSPQKCNY GLYAEQLSGS PFTAPRGTNE RSWLYRIRPS VRHTGRFRRV DYPHWKTAPH VGEHSLALGQ LRWSPLPAPS EALDFLQGIR TMTTAGDALT QAGMAAHAYA FNADMVDDYF FNADGELLIV PETGAIQVFT ELGRMDVEPS EICLIPRGMM FKVTRLGEEK VWRGYICENY GAKFTLPDRG PIGANCLANP RDFKTPVAAY EDKETPCRVQ VKWCGSFHMV EIGHSPLDVV AWHGNYAPYK YDLKTFSPVG AILFDHPDPS IFTVLTAPSG EEGTANVDFV IFPPRWLVAE HTFRPPWYHR NIMSEFMGLI YGRYDAKEEG FVPGGMSLHN MMLAHGPDFS GFEKASNGEL KPVKLDNTMA FMFETRFPQQ LTTFAAELDT LQDDYMDCWS GLERKFDGTP GIK //