ID A0A370KDH4_9GAMM Unreviewed; 357 AA.
AC A0A370KDH4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=4-hydroxyphenylpyruvate dioxygenase {ECO:0000313|EMBL:RDJ00713.1};
DE EC=1.13.11.27 {ECO:0000313|EMBL:RDJ00713.1};
GN Name=hppD {ECO:0000313|EMBL:RDJ00713.1};
GN ORFNames=DVT68_06790 {ECO:0000313|EMBL:RDJ00713.1};
OS Dyella solisilvae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1920168 {ECO:0000313|EMBL:RDJ00713.1, ECO:0000313|Proteomes:UP000254711};
RN [1] {ECO:0000313|EMBL:RDJ00713.1, ECO:0000313|Proteomes:UP000254711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHG54 {ECO:0000313|EMBL:RDJ00713.1,
RC ECO:0000313|Proteomes:UP000254711};
RA Gao Z., Qiu L.;
RT "Dyella solisilvae sp. nov., isolated from the pine and broad-leaved mixed
RT forest soil.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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:RDJ00713.1}.
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DR EMBL; QQSY01000001; RDJ00713.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370KDH4; -.
DR OrthoDB; 9780241at2; -.
DR Proteomes; UP000254711; Unassembled WGS sequence.
DR GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; IEA:UniProtKB-EC.
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; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000313|EMBL:RDJ00713.1};
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:RDJ00713.1};
KW Pyruvate {ECO:0000313|EMBL:RDJ00713.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 164..316
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT BINDING 245
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT BINDING 325
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
SQ SEQUENCE 357 AA; 39836 MW; EB1D984FCB6AB105 CRC64;
MQVTTFENPM GINGFEFVEF AAPAGRGPEL HALFKRMGFS PVLKHKSRAI TVYRQGDVNL
LVNEDPDSFA AEFAKAHGPC AAGFAIRFRK PSGDVRAMVM ANGGEEVGAK GEATKAVNAP
VVKGIGDCML YLVDQYGDNG SIYGDDYAPI PGADQHPKGF GLTFIDHLTH NLYFGNMQKW
SDYYERLFNF REIRYFDIKG AKTGLVSKAM TAPDGIVRIP LNESSDPKSQ INEYLDAYHG
EGIQHIAMFT DNIYDTVEAM RAKGVEFLDT PDTYFDVIDL RIPNHGEDVP RLAKNKILID
ADPETKQRKL LQIFTQNNIG PIFFEIIQRK GNEGFGEGNF QALFESIERD QMKRGVL
//
