HGD_BURCM
ID HGD_BURCM Reviewed; 444 AA.
AC Q0BHW3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Bamb_0701;
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000440; ABI86260.1; -; Genomic_DNA.
DR RefSeq; WP_011656087.1; NZ_CP009798.1.
DR AlphaFoldDB; Q0BHW3; -.
DR SMR; Q0BHW3; -.
DR STRING; 339670.Bamb_0701; -.
DR EnsemblBacteria; ABI86260; ABI86260; Bamb_0701.
DR GeneID; 44691385; -.
DR KEGG; bam:Bamb_0701; -.
DR PATRIC; fig|339670.21.peg.894; -.
DR eggNOG; COG3508; Bacteria.
DR OMA; FMFETRW; -.
DR UniPathway; UPA00139; UER00339.
DR Proteomes; UP000000662; Chromosome 1.
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 3: Inferred from homology;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism;
KW Tyrosine catabolism.
FT CHAIN 1..444
FT /note="Homogentisate 1,2-dioxygenase"
FT /id="PRO_1000019523"
FT ACT_SITE 298
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT BINDING 341
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT BINDING 347
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT BINDING 356
FT /ligand="homogentisate"
FT /ligand_id="ChEBI:CHEBI:16169"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT BINDING 377
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT BINDING 377
FT /ligand="homogentisate"
FT /ligand_id="ChEBI:CHEBI:16169"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
SQ SEQUENCE 444 AA; 49032 MW; FA49EAFE21E728E2 CRC64;
MTLDLSKPAT AGYLSGFANE FATEALPGAL PHGRNSPQRA PYGLYAEQLS GTAFTAPRGH
NRRSWLYRIR PAAVHRPFEP FTGPQRLVSE FGDSADVPPT PPNQLRWDPL PMPVEPTDFV
EGLVTMAGNG SAAAMNGCAI HLYAANRSMQ DRFFYSADGE LLIVPQQGRL FIATEFGRLD
VEPFEIAVIP RGVRFSVALP DGDARGYICE NFGALLRLPD LGPIGSNGLA NPRDFLTPQA
AYEDREGAFE LVAKLNGRLW RADIGHSPFD VVAWHGNYAP YKYDLRLFNT IGSISFDHPD
PSIFLVLQSQ SDTPGVDAID FVIFPPRWLA AEDTFRPPWF HRNVASEFMG LVHGAYDAKA
EGFVPGGASL HNCMSGHGPD ADTFEKASAS DTTKPHKVDA TMAFMFETRT LIRPTRYALD
TAQLQPDYFE CWQGIRKHFN PEQP
