ID HGD_XANCP Reviewed; 455 AA. AC Q8PDA2; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2002, sequence version 1. DT 05-MAY-2009, entry version 39. 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=XCC0438; OS Xanthomonas campestris pv. campestris. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=340; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33913 / NCPPB 528 / LMG 568; RX MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., RA Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing RT host specificities."; RL Nature 417:459-463(2002). 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; AE012141; AAM39756.1; -; Genomic_DNA. DR RefSeq; NP_635832.1; -. DR GeneID; 1000916; -. DR GenomeReviews; AE008922_GR; XCC0438. DR KEGG; xcc:XCC0438; -. DR HOGENOM; Q8PDA2; -. DR OMA; Q8PDA2; HRNCMSE. DR BioCyc; XCAM190485:XCC0438-MON; -. DR BRENDA; 1.13.11.5; 281360. 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 1 455 Homogentisate 1,2-dioxygenase. FT /FTId=PRO_0000220258. FT METAL 351 351 Iron (By similarity). FT METAL 357 357 Iron (By similarity). FT METAL 387 387 Iron (By similarity). SQ SEQUENCE 455 AA; 50406 MW; 2225A12DAD492A23 CRC64; MIQLDPTLLL SWRAGQHPDA PMHNDQRYMT GFGNEFASEA VADTLPVGQN SPQRVAHGLY AEQLSGTAFT APRGENRRSW LYRMRPAAVH GTFSLIEQSQ FHNDFGHGPV PPDQLRWSPL PLPQTPTDFI DGLYTMAGNG SPEAMNGVAV HLYAANASMQ DRFFYNADGE LLLVPQLGRL RVHTELGMLE LEPQQIGVIP RGVRFRVELR DGTARGYVCE NFGGLLHLPD LGPIGSNGLA NPRDFETPCA AFEQREGRFE LVAKFQGHLW RADIGHSPLD VVAWHGNYAP YRYDLRRFNT IGSISFDHPD PSIFTVLTSP SDTHGTANMD FAIFPPRWLV AQHTFRPPWF HRNVASEFMG LVHGVYDAKA DGFAPGGASL HNCMSGHGPD AATFDKASQA DLSRPDVITE TMAFMFETRA VLRPTAQALH APHRQGDYQQ CWAGLRKAFQ APPAS //