HGD_BRADU
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 03-AUG-2022, entry version 101.
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}; OrderedLocusNames=bll0343;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; 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;
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 -!- 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};
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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; 224911.27348591; -.
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 OMA; FMFETRW; -.
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 Gene3D; 2.60.120.10; -; 2.
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 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
