ID F3FHT2_PSESX Unreviewed; 358 AA.
AC F3FHT2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=4-hydroxyphenylpyruvate dioxygenase {ECO:0000313|EMBL:EGH29768.1};
GN ORFNames=PSYJA_12665 {ECO:0000313|EMBL:EGH29768.1};
OS Pseudomonas syringae pv. japonica str. M301072.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=629262 {ECO:0000313|EMBL:EGH29768.1, ECO:0000313|Proteomes:UP000004471};
RN [1] {ECO:0000313|EMBL:EGH29768.1, ECO:0000313|Proteomes:UP000004471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M301072PT {ECO:0000313|Proteomes:UP000004471};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
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:EGH29768.1}.
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DR EMBL; AEAH01000593; EGH29768.1; -; Genomic_DNA.
DR AlphaFoldDB; F3FHT2; -.
DR PATRIC; fig|629262.5.peg.2083; -.
DR HOGENOM; CLU_034004_1_0_6; -.
DR Proteomes; UP000004471; 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:EGH29768.1};
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:EGH29768.1};
KW Pyruvate {ECO:0000313|EMBL:EGH29768.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 13..130
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 159..292
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 358 AA; 40107 MW; A0C31FA038137C23 CRC64;
MADLYENPMG LMGFEFIEFA SPTPNSLEPV FQMMGFTKVA THRSKDVSLF RQGAINLILN
NEPHSLASYF AAEHGPSVCG MAFRVKDAQK AYNRALELGA QPLEIATGPM ELRLPAIKGI
GGAPLYLIDR FGEGTSIYDI DFNFIEGVDR HPVGAGLKFI DHLTHNVYRG RMAYWAGFYE
KLFNFRELRY FDIKGEYTGL TSKAMTAPDG MIRIPLNEES SRGAGQIEEF LMQFNGEGIQ
HVAFFTDDLI KTWDALKATG MRFMTAPPDT YYEMLQGRLP DHGEPEAELK SRGILLDGSS
EGGERRLLLQ IFSATLMGPV FFEFIQRKGD DGFGEGNFKA LFESIERDQI QRGVLTPD
//
