ID   A0A367F448_9ACTN        Unreviewed;       453 AA.
AC   A0A367F448;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   08-MAY-2019, entry version 4.
DE   RecName: Full=Homogentisate 1,2-dioxygenase {ECO:0000256|HAMAP-Rule:MF_00334, ECO:0000256|SAAS:SAAS00345391};
DE            Short=HGDO {ECO:0000256|HAMAP-Rule:MF_00334};
DE            EC=1.13.11.5 {ECO:0000256|HAMAP-Rule:MF_00334, ECO:0000256|SAAS:SAAS00345372};
DE   AltName: Full=Homogentisate oxygenase {ECO:0000256|HAMAP-Rule:MF_00334};
DE   AltName: Full=Homogentisic acid oxidase {ECO:0000256|HAMAP-Rule:MF_00334};
DE   AltName: Full=Homogentisicase {ECO:0000256|HAMAP-Rule:MF_00334};
GN   Name=hmgA {ECO:0000256|HAMAP-Rule:MF_00334};
GN   ORFNames=DQ392_01125 {ECO:0000313|EMBL:RCG25148.1};
OS   Streptomyces sp. LHW50302.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=2250578 {ECO:0000313|EMBL:RCG25148.1, ECO:0000313|Proteomes:UP000253507};
RN   [1] {ECO:0000313|EMBL:RCG25148.1, ECO:0000313|Proteomes:UP000253507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHW50302 {ECO:0000313|EMBL:RCG25148.1,
RC   ECO:0000313|Proteomes:UP000253507};
RA   Li L.;
RT   "Streptomyces reniochalinae sp. nov. and Streptomyces diacarnus sp.
RT   nov. from marine sponges.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00334,
CC         ECO:0000256|SAAS:SAAS01118316};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00334,
CC         ECO:0000256|SAAS:SAAS00172633};
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 4/6.
CC       {ECO:0000256|HAMAP-Rule:MF_00334, ECO:0000256|SAAS:SAAS00015628}.
CC   -!- SUBUNIT: Hexamer; dimer of trimers. {ECO:0000256|HAMAP-
CC       Rule:MF_00334, ECO:0000256|SAAS:SAAS00345363}.
CC   -!- SIMILARITY: Belongs to the homogentisate dioxygenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00334, ECO:0000256|SAAS:SAAS00570051}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00334}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:RCG25148.1}.
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DR   EMBL; QOIM01000018; RCG25148.1; -; Genomic_DNA.
DR   UniPathway; UPA00139; UER00339.
DR   Proteomes; UP000253507; Unassembled WGS sequence.
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   Complete proteome {ECO:0000313|Proteomes:UP000253507};
KW   Dioxygenase {ECO:0000256|HAMAP-Rule:MF_00334,
KW   ECO:0000256|SAAS:SAAS00459208, ECO:0000313|EMBL:RCG25148.1};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00334, ECO:0000256|SAAS:SAAS00459182};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00334,
KW   ECO:0000256|SAAS:SAAS00459204};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00334,
KW   ECO:0000256|SAAS:SAAS00459188, ECO:0000313|EMBL:RCG25148.1};
KW   Phenylalanine catabolism {ECO:0000256|HAMAP-Rule:MF_00334,
KW   ECO:0000256|SAAS:SAAS00423649};
KW   Tyrosine catabolism {ECO:0000256|HAMAP-Rule:MF_00334,
KW   ECO:0000256|SAAS:SAAS00084222}.
FT   ACT_SITE    310    310       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00334}.
FT   BINDING     389    389       homogentisate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00334}.
SQ   SEQUENCE   453 AA;  49588 MW;  6EB74AE7BA6BAB74 CRC64;
     MGQGTTSTTS TAAVRSRERA REEAAALTYL TGFGNEHSSE AVAGALPTGR NSPQRAPLGL
     YAEQLSGTAF TEPRAHNRRS WLYRIRPSAA HPRFVRGDNG GLRGTPFDET VPDPNRLRWG
     PVPDPAPGTD FLHGLWTLGG NGDARERSGM AVHLYAANTS MSDRVFSDAD GELLLVPERG
     GLLLRTEFGL LHAAPGHVAL IPRGVRFRVE LLEETARGYV CENHGRPFVL PDLGPIGANG
     LANPRDFQAP TAAYEEREGP VEVVTKFCGN LWHAVLDHSP LDVVAWHGNH VPYVYDLHRF
     NVLGSISYDH PDPSLFTVLT SPSDTPGLAG VDFVVFAPRW LVGEDTFRPP YFHRNVMSEY
     MGLIEGAYDA KAEGFVPGGG SLHNMMSAHG PDRETFERAS AAELAPQKID DGLAFMFETR
     WPLSLTRQAS EAGHLQRDYD AVWQGLERHF PAP
//