ID D2UFQ4_XANAP Unreviewed; 370 AA.
AC D2UFQ4;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Probable 4-hydroxyphenylpyruvate dioxygenase protein {ECO:0000313|EMBL:CBA17215.1};
DE EC=1.13.11.27 {ECO:0000313|EMBL:CBA17215.1};
GN OrderedLocusNames=XALc_2738 {ECO:0000313|EMBL:CBA17215.1};
OS Xanthomonas albilineans (strain GPE PC73 / CFBP 7063).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=380358 {ECO:0000313|EMBL:CBA17215.1, ECO:0000313|Proteomes:UP000001890};
RN [1] {ECO:0000313|EMBL:CBA17215.1, ECO:0000313|Proteomes:UP000001890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GPE PC73 / CFBP 7063 {ECO:0000313|Proteomes:UP000001890};
RX PubMed=20017926; DOI=10.1186/1471-2164-10-616;
RA Pieretti I., Royer M., Barbe V., Carrere S., Koebnik R., Cociancich S.,
RA Couloux A., Darrasse A., Gouzy J., Jacques M.A., Lauber E., Manceau C.,
RA Mangenot S., Poussier S., Segurens B., Szurek B., Verdier V., Arlat M.,
RA Rott P.;
RT "The complete genome sequence of Xanthomonas albilineans provides new
RT insights into the reductive genome evolution of the xylem-limited
RT Xanthomonadaceae.";
RL BMC Genomics 10:616-616(2009).
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; FP565176; CBA17215.1; -; Genomic_DNA.
DR AlphaFoldDB; D2UFQ4; -.
DR STRING; 380358.XALC_2738; -.
DR KEGG; xal:XALC_2738; -.
DR PATRIC; fig|29447.3.peg.2699; -.
DR eggNOG; COG3185; Bacteria.
DR OrthoDB; 9780241at2; -.
DR Proteomes; UP000001890; Chromosome.
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:CBA17215.1};
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:CBA17215.1};
KW Pyruvate {ECO:0000313|EMBL:CBA17215.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001890};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
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 258
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT BINDING 338
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
SQ SEQUENCE 370 AA; 41534 MW; A4277B4B7F6ACB0E CRC64;
MRAQPQHPPQ PTNLGMQVTT FDNPMGIDGF EFVEFAAPAG QGERLHEYFR RMGFTAVLRH
RHRAITVYRQ GGVNFLVNEA PDSFAADFSA AHGPCACGFA IRFKRPADVV FAKVLENGGE
AVANKPDTRA VPAPVIQGIG DCMLYLVDQY GDTGSVYAEF EPVPGAELYP VGFGLTFIDH
LTHNLYFGNM QRWSDYYARL FNFREIRYFD IKGAKTGLVS KAMTAPDGVV RIPLNESSDP
KSQINEYLDA YHGEGIQHIA CFTDDIYVTV ERMRAAGVEF LETPDTYFDV IDQRIPDHGE
DVARLARNKI LIDADPETKQ RKLLQIFTQN CIGPIFFEII QRKGNEGFGE GNFQALFESI
ERDQIKRGVL
//
