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Database: UniProt
Entry: A0A2N6NWM7_BEABA
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ID   A0A2N6NWM7_BEABA        Unreviewed;       408 AA.
AC   A0A2N6NWM7;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=4-hydroxyphenylpyruvate dioxygenase {ECO:0000256|ARBA:ARBA00013222, ECO:0000256|PIRNR:PIRNR009283};
GN   Name=B23G1.170 {ECO:0000313|EMBL:PMB71657.1};
GN   ORFNames=BM221_001753 {ECO:0000313|EMBL:PMB71657.1};
OS   Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS   shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB71657.1, ECO:0000313|Proteomes:UP000235728};
RN   [1] {ECO:0000313|EMBL:PMB71657.1, ECO:0000313|Proteomes:UP000235728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEF-007 {ECO:0000313|EMBL:PMB71657.1,
RC   ECO:0000313|Proteomes:UP000235728};
RX   PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA   Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT   "Characterization of T-DNA insertion mutants with decreased virulence in
RT   the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL   Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
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   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 3/6.
CC       {ECO:0000256|ARBA:ARBA00005162}.
CC   -!- SIMILARITY: Belongs to the 4HPPD family.
CC       {ECO:0000256|ARBA:ARBA00005877, ECO:0000256|PIRNR:PIRNR009283}.
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:PMB71657.1}.
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DR   EMBL; MRVG01000002; PMB71657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N6NWM7; -.
DR   OMA; DPFPVKG; -.
DR   UniPathway; UPA00139; UER00362.
DR   Proteomes; UP000235728; 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:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
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:PMB71657.1};
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:PMB71657.1};
KW   Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232};
KW   Pyruvate {ECO:0000313|EMBL:PMB71657.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235728};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878}.
FT   DOMAIN          24..175
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   DOMAIN          205..365
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   BINDING         208
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT   BINDING         291
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT   BINDING         376
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
SQ   SEQUENCE   408 AA;  44926 MW;  901DD8C6386F94B6 CRC64;
     MAPSAIATTS RPADAAAPVG NFTGYDHVTW WVGNAKQAAS YYTTLFGFHV EAYRGLETGS
     RFFASYVVSN NAVRFVFTSP LRSAAHLPAD DEAASISADE RQLLVDMYAH LERHGDAVKD
     VAFEVDNVAA VYDGAVRGGA VAVQPPRTVT DDEHGAVTTA VIRTYGDTTH TLVNRAGYTG
     TFMPGFRAGK PSTSIVSAPA VPLARIDHCV GNQDWDEMNA ACNFYETALS FHRFWSVDDN
     QISTEFSALS SVVMASPNNL VKMPINEPAP GKKKSQIEEY VVFNSGPGVQ HIALLTGDII
     GAVTALRARG VDFINVPQTY YDTMRHRLKT EKRAWELRED LDTIQRLNIL IDYDEGGYLL
     QLFTKPLMDR PTVFIEIIQR NHFEGFGAGN FKSLFEAIER EQAERGNL
//
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