ID A0A1Y0IL48_9BACL Unreviewed; 372 AA.
AC A0A1Y0IL48;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=4-hydroxyphenylpyruvate dioxygenase {ECO:0000313|EMBL:ARU60225.1};
GN ORFNames=CBW65_03490 {ECO:0000313|EMBL:ARU60225.1};
OS Tumebacillus avium.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Tumebacillus.
OX NCBI_TaxID=1903704 {ECO:0000313|EMBL:ARU60225.1, ECO:0000313|Proteomes:UP000195437};
RN [1] {ECO:0000313|Proteomes:UP000195437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR23208 {ECO:0000313|Proteomes:UP000195437};
RA Sung H.;
RL Submitted (MAY-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}.
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DR EMBL; CP021434; ARU60225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0IL48; -.
DR KEGG; tum:CBW65_03490; -.
DR OrthoDB; 9780241at2; -.
DR Proteomes; UP000195437; Chromosome.
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:ARU60225.1};
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:ARU60225.1};
KW Pyruvate {ECO:0000313|EMBL:ARU60225.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 20..150
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 177..329
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT BINDING 180
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; 42294 MW; 93FF57E96EAB8961 CRC64;
MSIQQEQATE TLQDILPVED IDYVEVYSGN AKQSVFYYCK LFGMKVTAYK GLETGSRNLV
SYVVEKGDIR FVISGSFAPD HPIAEFTKKH GDAVKDIALR VENVEETYRL AVERGGIGMI
EPYVEEDEHG FVKKAMIGTF GDTVHTLIER SAYNGVFAPG FQPVESEEPE IDTAITRLDH
LAINVEQMDT WTDYYEKVFG FKLIKEFRQE DVSSDSSSLM TKALRNGNHR IKFPIVEPAP
GKKKSQVQEF IDYNLGAGVQ HVALETDNIL MAVENLQKNG IRFLYTPDAY YELLPKRVGD
IDEPIDELNR LNILVDRDDE GYLLQIFSQP MQDRPTMFFE IIQRKGSNGF GNGNIRALFE
AVEREQEKRG NL
//
