HPPD_COCP7
ID HPPD_COCP7 Reviewed; 399 AA.
AC P0CW94; C5PGS8; Q00415; Q02288; Q400Q0; Q400Q8; Q9C0M8;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=4-hydroxyphenylpyruvate dioxygenase;
DE Short=4HPPD;
DE Short=HPD;
DE Short=HPPDase;
DE EC=1.13.11.27;
DE AltName: Full=T-cell reactive protein;
GN Name=TCRP; ORFNames=CPC735_051010;
OS Coccidioides posadasii (strain C735) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=222929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C735;
RX PubMed=7642122; DOI=10.1016/0378-1119(95)00250-a;
RA Wyckoff E.E., Pishko E.J., Kirkland T.N., Cole G.T.;
RT "Cloning and expression of a gene encoding a T-cell reactive protein from
RT Coccidioides immitis: homology to 4-hydroxyphenylpyruvate dioxygenase and
RT the mammalian F antigen.";
RL Gene 161:107-111(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C735;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 237-305.
RC STRAIN=C634, and C735;
RX PubMed=1840578; DOI=10.1128/iai.59.11.3952-3961.1991;
RA Kirkland T.N., Zhu S., Kruse D., Hsu L., Seshan K.R., Cole G.T.;
RT "Coccidioides immitis fractions which are antigenic for immune T
RT lymphocytes.";
RL Infect. Immun. 59:3952-3961(1991).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate;
CC Xref=Rhea:RHEA:16189, ChEBI:CHEBI:15379, ChEBI:CHEBI:16169,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:36242; EC=1.13.11.27;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 3/6.
CC -!- SIMILARITY: Belongs to the 4HPPD family. {ECO:0000305}.
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DR EMBL; L38493; AAA82574.1; -; Genomic_DNA.
DR EMBL; ACFW01000049; EER23731.1; -; Genomic_DNA.
DR EMBL; S69110; AAC60567.2; -; mRNA.
DR RefSeq; XP_003065876.1; XM_003065830.1.
DR AlphaFoldDB; P0CW94; -.
DR SMR; P0CW94; -.
DR EnsemblFungi; EER23731; EER23731; CPC735_051010.
DR GeneID; 9691346; -.
DR KEGG; cpw:CPC735_051010; -.
DR VEuPathDB; FungiDB:CPC735_051010; -.
DR HOGENOM; CLU_034004_3_1_1; -.
DR UniPathway; UPA00139; UER00362.
DR Proteomes; UP000009084; 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.
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 PANTHER; PTHR11959; PTHR11959; 1.
DR Pfam; PF00903; Glyoxalase; 1.
DR PIRSF; PIRSF009283; HPP_dOase; 1.
DR SUPFAM; SSF54593; SSF54593; 1.
DR TIGRFAMs; TIGR01263; 4HPPD; 1.
DR PROSITE; PS51819; VOC; 2.
PE 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism;
KW Repeat; Tyrosine catabolism.
FT CHAIN 1..399
FT /note="4-hydroxyphenylpyruvate dioxygenase"
FT /id="PRO_0000088403"
FT DOMAIN 23..166
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 197..355
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 200
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 297
FT /note="N -> T (in Ref. 3; AAC60567)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 45262 MW; 342DEFF33091C3C2 CRC64;
MAPAADSPTL QPAQPSDLNQ YRGYDHVHWY VGNAKQAATY YVTRMGFERV AYRGLETGSK
AVASHVVRNG NITFILTSPL RSVEQASRFP EDEALLKEIH AHLERHGDGV KDVAFEVDCV
ESVFSAAVRN GAEVVSDVRT VEDEDGQIKM ATIRTYGETT HTLIERSGYR GGFMPGYRME
SNADATSKFL PKVVLERIDH CVGNQDWDEM ERVCDYYEKI LGFHRFWSVD DKDICTEFSA
LKSIVMASPN DIVKMPINEP AKGKKQSQIE EYVDFYNGAG VQHIALRTNN IIDAITNLKA
RGTEFIKVPE TYYEDMKIRL KRQGLVLDED FETLKSLDIL IDFDENGYLL QLFTKHLMDR
PTVFIEIIQR NNFSGFGAGN FRALFEAIER EQALRGTLI
