HGD_RHIME
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 03-AUG-2022, entry version 111.
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, ECO:0000303|PubMed:10220173};
GN OrderedLocusNames=R02939; ORFNames=SMc03208;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; 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;
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: 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}.
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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 STRING; 266834.SMc03208; -.
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 OMA; FMFETRW; -.
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 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 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
