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Database: UniProt
Entry: F0UCI0_AJEC8
LinkDB: F0UCI0_AJEC8
Original site: F0UCI0_AJEC8 
ID   F0UCI0_AJEC8            Unreviewed;       428 AA.
AC   F0UCI0;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=4-hydroxyphenylpyruvate dioxygenase {ECO:0000256|ARBA:ARBA00013222, ECO:0000256|PIRNR:PIRNR009283};
GN   Name=HPD1 {ECO:0000313|EMBL:QSS49439.1};
GN   ORFNames=HCEG_02471 {ECO:0000313|EMBL:EGC43256.1}, I7I53_09785
GN   {ECO:0000313|EMBL:QSS49439.1};
OS   Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS   capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN   [1] {ECO:0000313|Proteomes:UP000008142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EGC43256.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H88 {ECO:0000313|EMBL:EGC43256.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QSS49439.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H88 {ECO:0000313|EMBL:QSS49439.1};
RA   Voorhies M., Cohen S., Shea T.P., Petrus S., Munoz J.F., Poplawski S.,
RA   Goldman W.E., Michael T., Cuomo C.A., Sil A., Beyhan S.;
RT   "Chromosome-level genome assembly of a human fungal pathogen reveals
RT   clustering of transcriptionally co-regulated genes.";
RL   Submitted (JAN-2021) 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   -!- 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}.
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DR   EMBL; DS990637; EGC43256.1; -; Genomic_DNA.
DR   EMBL; CP069102; QSS49439.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0UCI0; -.
DR   STRING; 544711.F0UCI0; -.
DR   VEuPathDB; FungiDB:I7I53_09785; -.
DR   HOGENOM; CLU_034004_3_1_1; -.
DR   OMA; DMCSEYS; -.
DR   UniPathway; UPA00139; UER00362.
DR   Proteomes; UP000008142; Unassembled WGS sequence.
DR   Proteomes; UP000663419; Chromosome 1.
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; 1.
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:EGC43256.1};
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:EGC43256.1};
KW   Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232};
KW   Pyruvate {ECO:0000313|EMBL:EGC43256.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008142};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878}.
FT   DOMAIN          30..183
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   DOMAIN          214..385
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   BINDING         217
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT   BINDING         300
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT   BINDING         396
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
SQ   SEQUENCE   428 AA;  47294 MW;  FF834128C659DE77 CRC64;
     MGSSLCFDST AATSENGEIM PSVLGPEYYG FDHITWYVGN AKQAASYLIT RLGFNPVAYR
     GPETGSRALV SYVIANSGAT FVMTSPVCGK LATDEISKFQ ISVREQALLD EIHNHLEKHG
     DGVKDVAFRV NADVKAKWER AVANGAVSVV NPTIISGDEP GSGQIEMATI KSFGDTTHTL
     INRDHYKGCF LPGYVRVEQG DSINELLPPI DFIEIDHCVG NQPWNGLDMA VKFYEDCLNF
     HRYWSVDDKS LCSGYSSMRS IVVASPNEVI KMPLNEPAVG KKKSQIEEFV DYYNGSGVQH
     IAFRTNDIIT AITNLRKRGV EFLSVPAAYY DVIRARLAAM NAGNTGVHGD KKGNLVIKES
     IDTLQALNIL IDFDEQGYLL QIFTKHVLDR PTVFFEVIQR NNFDGFGAGN FKSLFEAFER
     EQAARGNL
//
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