ID HGD_BORA1 Reviewed; 432 AA. AC Q2KYC8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 05-MAY-2009, entry version 21. 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=BAV0528; OS Bordetella avium (strain 197N). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=360910; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16885469; DOI=10.1128/JB.01927-05; RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., RA King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., RA Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., RA Squares S., Woodward J., Parkhill J., Temple L.M.; RT "Comparison of the genome sequence of the poultry pathogen Bordetella RT avium with those of B. bronchiseptica, B. pertussis, and B. RT parapertussis reveals extensive diversity in surface structures RT associated with host interaction."; RL J. Bacteriol. 188:6002-6015(2006). 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM167904; CAJ48133.1; -; Genomic_DNA. DR RefSeq; YP_785061.1; -. DR GeneID; 6266951; -. DR GenomeReviews; AM167904_GR; BAV0528. DR KEGG; bav:BAV0528; -. DR NMPDR; fig|521.1.peg.1029; -. DR HOGENOM; Q2KYC8; -. DR OMA; Q2KYC8; HRNCMSE. 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 1 432 Homogentisate 1,2-dioxygenase. FT /FTId=PRO_1000019520. FT METAL 329 329 Iron (By similarity). FT METAL 335 335 Iron (By similarity). FT METAL 365 365 Iron (By similarity). SQ SEQUENCE 432 AA; 47808 MW; 2CEC82ACE2DE950E CRC64; MPLNYQSGFG NACATEALPG ALPQGRNSPQ QCPYGLYAEQ LSGTAFTAPR SENRRSWLYR IRPGVVHRPF EPYAGAPHWL ADFGTGPVTP NQLRWSPLPL PATPTDFIDG VHTWGGNGGP DEQSGVGIHL YAANQSMKGR FFYNADAEML LVPQLGRLRL ATEMGLLDLE PLEIAVLPRG VRFRVELLDA EARGYLLENF GTALRPPELG PIGSNGLANA RDFQTPVAWY EDVEGDFELI AKFTGGFWRA PLTHSPLDVV AWHGTHAPYK YDLRHFNTIG SISYDHPDPS IFTVLTSPSD TPGTANLDFA IFPPRILAME NTFRPPWFHR NIASEFMGLI QGVYDAKAEG FAPGGASLHN CMSGHGPDAD TFEKASVADT SKAHYIRDTM AFMFETRRVI RPTRQALASA QLQGDYYQCW QDLKKHFNPE KA //