ID HGD_STRAW Reviewed; 438 AA. AC Q828S5; DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 14-MAY-2014, entry version 68. DE RecName: Full=Homogentisate 1,2-dioxygenase; DE Short=HGDO; DE EC=1.13.11.5; DE AltName: Full=Homogentisate oxygenase; DE AltName: Full=Homogentisic acid oxidase; DE AltName: Full=Homogentisicase; GN Name=hmgA; OrderedLocusNames=SAV_6587; OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / OS NCIMB 12804 / NRRL 8165 / MA-4680). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=227882; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / RC MA-4680; RX PubMed=11572948; DOI=10.1073/pnas.211433198; RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., RA Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., RA Kikuchi H., Shiba T., Sakaki Y., Hattori M.; RT "Genome sequence of an industrial microorganism Streptomyces RT avermitilis: deducing the ability of producing secondary RT metabolites."; RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / RC MA-4680; RX PubMed=12692562; DOI=10.1038/nbt820; RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., RA Sakaki Y., Hattori M., Omura S.; RT "Complete genome sequence and comparative analysis of the industrial RT microorganism Streptomyces avermitilis."; RL Nat. Biotechnol. 21:526-531(2003). CC -!- FUNCTION: Involved in the catabolism of homogentisate (2,5- CC dihydroxyphenylacetate or 2,5-OH-PhAc), a central intermediate in CC the degradation of phenylalanine and tyrosine. Catalyzes the CC oxidative ring cleavage of the aromatic ring of homogentisate to CC yield maleylacetoacetate (By similarity). CC -!- CATALYTIC ACTIVITY: Homogentisate + O(2) = 4-maleylacetoacetate. CC -!- COFACTOR: Iron (By similarity). CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation; CC acetoacetate and fumarate from L-phenylalanine: step 4/6. CC -!- SUBUNIT: Hexamer; dimer of trimers (By similarity). CC -!- SIMILARITY: Belongs to the homogentisate dioxygenase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000030; BAC74298.1; -; Genomic_DNA. DR RefSeq; NP_827763.1; NC_003155.4. DR ProteinModelPortal; Q828S5; -. DR STRING; 227882.SAV_6587; -. DR EnsemblBacteria; BAC74298; BAC74298; SAV_6587. DR GeneID; 1211514; -. DR KEGG; sma:SAV_6587; -. DR PATRIC; 23727276; VBIStrAve112782_6987. DR eggNOG; COG3508; -. DR HOGENOM; HOG000139824; -. DR KO; K00451; -. DR OMA; YEATISK; -. DR OrthoDB; EOG6D5FZK; -. DR BioCyc; SAVE227882:GJU1-6672-MONOMER; -. DR UniPathway; UPA00139; UER00339. DR GO; GO:0004411; F:homogentisate 1,2-dioxygenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 2.60.120.10; -; 2. 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. 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 Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase; KW Phenylalanine catabolism; Tyrosine catabolism. FT CHAIN 1 438 Homogentisate 1,2-dioxygenase. FT /FTId=PRO_0000220255. FT ACT_SITE 294 294 Proton acceptor (By similarity). FT METAL 337 337 Iron (By similarity). FT METAL 343 343 Iron (By similarity). FT METAL 373 373 Iron (By similarity). FT BINDING 352 352 homogentisate (By similarity). FT BINDING 373 373 homogentisate (By similarity). SQ SEQUENCE 438 AA; 47823 MW; 8E751EBA9B6F53BC CRC64; MSGDARKTAE GLAHLTGFGN EHASEAVPGA LPEGRNSPQR APLGLYAEQL SGSAFTEPRA HNRRSWLYRI RPSAAHPPFT RADNGAIRTA PFTETAPDPN RLRWNPLPEP PAGTDFVGGL WTLGGNGDAT QRTGMAVHLY HANSSMDRVF SDADGELLIV PERGGLLLRT EFGLLHAEPG QVALVPRGVR FRVDLLDESA RGYVCENYGA PFQLPDLGPI GANGLAAARD FKAPVAAYED VEGPVEVVNK FCGNLWTATY DHSPLDVVAW HGNHVPYTYD LRRFNVLGTI SYDHPDPSIF TVLTSPSDTP GLAGVDFVVF APRWLVGEDT FRPPYFHRNV MSEYMGLIEG AYDAKAAGFV PGGGSLHNMM SAHGPDRETF DRASAAELRP QKIDDGLAFM FETRWPVTAT AQAARAEHLQ PAYDDVWQGL QRHFRPSD //