ID A0A1F4K160_9BURK Unreviewed; 360 AA.
AC A0A1F4K160;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=4-hydroxyphenylpyruvate dioxygenase {ECO:0000313|EMBL:OGB28380.1};
GN ORFNames=A3F78_21430 {ECO:0000313|EMBL:OGB28380.1};
OS Burkholderiales bacterium RIFCSPLOWO2_12_FULL_61_40.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=1797566 {ECO:0000313|EMBL:OGB28380.1, ECO:0000313|Proteomes:UP000178940};
RN [1] {ECO:0000313|EMBL:OGB28380.1, ECO:0000313|Proteomes:UP000178940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|PIRSR:PIRSR009283-1};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000256|PIRSR:PIRSR009283-1};
CC -!- SIMILARITY: Belongs to the 4HPPD family.
CC {ECO:0000256|ARBA:ARBA00005877}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGB28380.1}.
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DR EMBL; MESI01000127; OGB28380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4K160; -.
DR STRING; 1797566.A3F78_21430; -.
DR Proteomes; UP000178940; Unassembled WGS sequence.
DR GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009072; P:aromatic amino acid metabolic process; IEA:InterPro.
DR CDD; cd07250; HPPD_C_like; 1.
DR CDD; cd08342; HPPD_N_like; 1.
DR Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 2.
DR InterPro; IPR005956; 4OHPhenylPyrv_dOase.
DR InterPro; IPR041735; 4OHPhenylPyrv_dOase_C.
DR InterPro; IPR041736; 4OHPhenylPyrv_dOase_N.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR037523; VOC.
DR NCBIfam; TIGR01263; 4HPPD; 1.
DR PANTHER; PTHR11959; 4-HYDROXYPHENYLPYRUVATE DIOXYGENASE; 1.
DR PANTHER; PTHR11959:SF1; 4-HYDROXYPHENYLPYRUVATE DIOXYGENASE; 1.
DR Pfam; PF00903; Glyoxalase; 1.
DR Pfam; PF14696; Glyoxalase_5; 1.
DR PIRSF; PIRSF009283; HPP_dOase; 1.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR PROSITE; PS51819; VOC; 2.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000313|EMBL:OGB28380.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR009283-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR009283-1};
KW Oxidoreductase {ECO:0000313|EMBL:OGB28380.1};
KW Pyruvate {ECO:0000313|EMBL:OGB28380.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 13..130
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 159..301
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT BINDING 162
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT BINDING 241
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT BINDING 323
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
SQ SEQUENCE 360 AA; 40203 MW; 86C5E9A216F3AFBC CRC64;
MTDLFDNPMG LMGFEFVEFA SPTPNVLEPI FEQMGFTLVA HHRSKDVDLY RQGDINFIIN
REPRSAAGYF AAEHGPSACG MAFRVKSSHQ AYERALAQGA QPMDMPTGPM ELRLPAIKGI
GGASLYLIDR FEDGQSIYDI DFEFIDGVDR HPKGHGLKII DHLTHNVYRG RMAYWAQFYE
RIFNFREIRF FDIKGEYTGL TSKAMTAPDG KIRIPLNEEA AGSGGQIEEF LMQFNGEGIQ
HIALLSDDLI ATLDSLKKAG IPLMTAPPAT YYEMLSERLP GHGEDAQALQ SRGILLDGSS
AGGERRLLLQ IFSQTLLGPV FFEFIQRKGD DGFGEGNFKA LFESMERDQL RRGVIQGDKV
//
