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
//