HPPD_DICDI
ID HPPD_DICDI Reviewed; 367 AA.
AC Q76NV5; Q1ZXJ9; Q54ZM7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=4-hydroxyphenylpyruvate dioxygenase;
DE EC=1.13.11.27;
DE AltName: Full=4-hydroxyphenylpyruvic acid oxidase;
DE Short=4HPPD;
DE Short=HPD;
DE Short=HPPDase;
GN Name=hpd; ORFNames=DDB_G0277511;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16512674; DOI=10.1021/pr050350q;
RA Reinders Y., Schulz I., Graef R., Sickmann A.;
RT "Identification of novel centrosomal proteins in Dictyostelium discoideum
RT by comparative proteomic approaches.";
RL J. Proteome Res. 5:589-598(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
CC -!- FUNCTION: Key enzyme in the degradation of tyrosine. {ECO:0000250}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q76NV5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q76NV5-2; Sequence=VSP_032743;
CC -!- SIMILARITY: Belongs to the 4HPPD family. {ECO:0000305}.
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DR EMBL; AAFI02000020; EAL68718.1; -; Genomic_DNA.
DR EMBL; AAFI02000020; EAS66903.1; -; Genomic_DNA.
DR RefSeq; XP_001134587.1; XM_001134587.1.
DR RefSeq; XP_642615.1; XM_637523.1.
DR AlphaFoldDB; Q76NV5; -.
DR SMR; Q76NV5; -.
DR STRING; 44689.DDB0231603; -.
DR PaxDb; Q76NV5; -.
DR EnsemblProtists; EAL68718; EAL68718; DDB_G0277511.
DR EnsemblProtists; EAS66903; EAS66903; DDB_G0277511.
DR GeneID; 8621032; -.
DR KEGG; ddi:DDB_G0277511; -.
DR dictyBase; DDB_G0277511; hpd.
DR eggNOG; KOG0638; Eukaryota.
DR HOGENOM; CLU_034004_3_1_1; -.
DR InParanoid; Q76NV5; -.
DR OMA; DPFPVKG; -.
DR PhylomeDB; Q76NV5; -.
DR Reactome; R-DDI-8963684; Tyrosine catabolism.
DR UniPathway; UPA00139; UER00362.
DR PRO; PR:Q76NV5; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; ISS:UniProtKB.
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; ISS:UniProtKB.
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; 2.
DR PIRSF; PIRSF009283; HPP_dOase; 1.
DR SUPFAM; SSF54593; SSF54593; 1.
DR TIGRFAMs; TIGR01263; 4HPPD; 1.
DR PROSITE; PS51819; VOC; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Phenylalanine catabolism; Reference proteome; Repeat; Tyrosine catabolism.
FT CHAIN 1..367
FT /note="4-hydroxyphenylpyruvate dioxygenase"
FT /id="PRO_0000327996"
FT DOMAIN 3..135
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 166..324
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MEM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_032743"
SQ SEQUENCE 367 AA; 41738 MW; EC5A1D87AB196355 CRC64;
MEGFDHVTFW VGNALQAATY YIARFGFQNL AYSGLETGNR QFATHVIHQN NIIMAFTSPL
TGDNKDYADH MMRHGDGVKD IAFNVKDVQH IYDEAVKAGA QSVKEPHQIK DEHGIVTLAT
IMSPYGETTH TFVDRSQYKG AFLPGFTYKV ASDPLSNITE PVGLNLIDHV VSNHADKMME
PVVQWYEKVL QFHRFWSVDD KTIHTEYSSL RSVVVADKSE KVKLPINEPA NGIRKSQIQE
YVDFYNGAGV QHIALKTDNI IDAISKLRSR GVSFLTVPKT YYTSLREKLQ HSSLEIKEDL
DTLEKLHILI DYDDKGYLLQ IFTNNVEDKP TVFFEIIQRN NHDGFGAGNF KSLFEAIERQ
QETRGNL
