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   04-NOV-2008, entry version 28.
DE   RecName: Full=Homogentisate 1,2-dioxygenase;
DE            EC=1.13.11.5;
DE   AltName: Full=Homogentisicase;
DE   AltName: Full=Homogentisate oxygenase;
DE   AltName: Full=Homogentisic acid oxidase;
GN   Name=hmgA; OrderedLocusNames=BPSL2739;
OS   Burkholderia pseudomallei (Pseudomonas pseudomallei).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=28450;
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.,
RA   Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R.,
RA   Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I.,
RA   Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D.,
RA   Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K.,
RA   Keith K.E., Maddison M., Moule S., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA   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,
RT   Burkholderia pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC   -!- CATALYTIC ACTIVITY: Homogentisate + O(2) = 4-maleylacetoacetate.
CC   -!- COFACTOR: Iron (By similarity).
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetic acid and fumarate from L-phenylalanine: step 4/6.
CC   -!- SIMILARITY: Belongs to the homogentisate dioxygenase family.
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DR   EMBL; BX571965; CAH36747.1; -; Genomic_DNA.
DR   RefSeq; YP_109335.1; -.
DR   GeneID; 3092129; -.
DR   GenomeReviews; BX571965_GR; BPSL2739.
DR   KEGG; bps:BPSL2739; -.
DR   HOGENOM; Q63RD3; -.
DR   BioCyc; BPSE272560:BPSL2739-MON; -.
DR   GO; GO:0004411; F:homogentisate 1,2-dioxygenase activity; IEA:HAMAP.
DR   GO; GO:0005506; F:iron ion binding; IEA:HAMAP.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006572; P:tyrosine catabolic process; IEA:HAMAP.
DR   HAMAP; MF_00334; -; 1.
DR   InterPro; IPR005708; Homogentis_dOase.
DR   PANTHER; PTHR11056; Homogentis_dOase; 1.
DR   Pfam; PF04209; HgmA; 1.
DR   TIGRFAMs; TIGR01015; hmgA; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Phenylalanine catabolism; Tyrosine catabolism.
FT   CHAIN         1    450       Homogentisate 1,2-dioxygenase.
FT                                /FTId=PRO_0000225786.
FT   METAL       347    347       Iron (By similarity).
FT   METAL       353    353       Iron (By similarity).
FT   METAL       383    383       Iron (By similarity).
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
//