ID A0A2A9CPD4_9BACI Unreviewed; 372 AA.
AC A0A2A9CPD4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=4-hydroxyphenylpyruvate dioxygenase {ECO:0000313|EMBL:PFG15472.1};
GN ORFNames=ATG70_3733 {ECO:0000313|EMBL:PFG15472.1};
OS Bacillus sp. es.036.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1761764 {ECO:0000313|EMBL:PFG15472.1, ECO:0000313|Proteomes:UP000222003};
RN [1] {ECO:0000313|EMBL:PFG15472.1, ECO:0000313|Proteomes:UP000222003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=es.036 {ECO:0000313|Proteomes:UP000222003};
RA Fredrickson J.;
RT "Microbial Interactions in Extremophilic Mat Communities.";
RL Submitted (OCT-2017) 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:PFG15472.1}.
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DR EMBL; PDIZ01000001; PFG15472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9CPD4; -.
DR Proteomes; UP000222003; 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; 2.
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:PFG15472.1};
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:PFG15472.1};
KW Pyruvate {ECO:0000313|EMBL:PFG15472.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 21..151
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 178..329
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT BINDING 181
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT BINDING 261
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT BINDING 340
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
SQ SEQUENCE 372 AA; 42157 MW; 07AAC54C06ACF170 CRC64;
MQEQMLNQNQ QETADFFPVR DVDYLEIYVG NAKQASHYFC KAFGFKPVAY SGLETGDREK
VSYVLQQNNI RLVLSGALSN DHPITEFVKL HGDGVKDIAL TVENVDSAYK EAAERGAIEL
SPPKEYKDEN GVVKMAVIGT YGDTIHTLVE RKNYSGLFLP GYKKFEGTIP SKETGLLGID
HCVGNVESME EWVSYYENVM GFKQMIHFDD EDISTEYSAL MSKVMHNGGR IKFPINEPAN
GKRKSQIQEY LDYYNGPGVQ HIAVLTNDIV DTVAKLRDGG VEFLETPDDY YDVLTERVGE
IDEEISKLRE LKILVDRDDE GYLLQIFTKP VVDRPTLFIE IIQRKGAKGF GEGNFKALFQ
AIEREQERRG NL
//