HGD_BURPS
ID HGD_BURPS Reviewed; 450 AA.
AC Q63RD3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=BPSL2739;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571965; CAH36747.1; -; Genomic_DNA.
DR RefSeq; YP_109335.1; NC_006350.1.
DR AlphaFoldDB; Q63RD3; -.
DR SMR; Q63RD3; -.
DR STRING; 272560.BPSL2739; -.
DR EnsemblBacteria; CAH36747; CAH36747; BPSL2739.
DR KEGG; bps:BPSL2739; -.
DR PATRIC; fig|272560.6.peg.3128; -.
DR eggNOG; COG3508; Bacteria.
DR OMA; FMFETRW; -.
DR UniPathway; UPA00139; UER00339.
DR Proteomes; UP000000605; 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 Reference proteome; Tyrosine catabolism.
FT CHAIN 1..450
FT /note="Homogentisate 1,2-dioxygenase"
FT /id="PRO_0000225786"
FT ACT_SITE 304
FT /note="Proton acceptor"
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 353
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT BINDING 362
FT /ligand="homogentisate"
FT /ligand_id="ChEBI:CHEBI:16169"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT BINDING 383
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
FT BINDING 383
FT /ligand="homogentisate"
FT /ligand_id="ChEBI:CHEBI:16169"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00334"
SQ SEQUENCE 450 AA; 50130 MW; 1BC1019C4C2C398F CRC64;
MERTTIMTLD FSKPGEAGYQ SGFANEFATE ALPGALPHAR NSPQRAPYGL YAEQFSGTAF
TAPRGHNRRS WLYRIRPAAV HRPFELVSGE RRIVAEFGDS DDVPPTPPNQ LRWDPLPMPA
QPTDFVDGWV TMAGNGSAAA MSGCAIHLYA ANRSMRERFF YSADGELLIV PQEGRLFIMT
ELGRLDVEPF EIAVIPRGVR FAVALPDGRA RGYVCENFGA LLRLPDLGPI GSNGLANPRD
FLTPHASYED REGAFELVAK LNGRLWRADI DHSPFDVVAW HGNYAPYKYD LRHFNTIGSI
SYDHPDPSIF LVLQSQSDTP GVDAIDFVIF PPRWLAAEDT FRPPWFHRNV ASEFMGLVHG
VYDAKAEGFV PGGASLHNCM SGHGPDADTF EKASSIDTSK PNKVGDTMAF MFETRTLIRP
TRFALDTAQL QANYFECWQG LKKHFNPEQR
