HPPD2_ASPFU
ID HPPD2_ASPFU Reviewed; 406 AA.
AC Q4WPV8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable 4-hydroxyphenylpyruvate dioxygenase 2;
DE Short=4HPPD 2;
DE Short=HPD 2;
DE Short=HPPDase 2;
DE EC=1.13.11.27;
GN ORFNames=AFUA_4G10620;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AAHF01000005; EAL89726.1; -; Genomic_DNA.
DR RefSeq; XP_751764.1; XM_746671.1.
DR AlphaFoldDB; Q4WPV8; -.
DR SMR; Q4WPV8; -.
DR STRING; 746128.CADAFUBP00006590; -.
DR PRIDE; Q4WPV8; -.
DR EnsemblFungi; EAL89726; EAL89726; AFUA_4G10620.
DR GeneID; 3509500; -.
DR KEGG; afm:AFUA_4G10620; -.
DR VEuPathDB; FungiDB:Afu4g10620; -.
DR eggNOG; KOG0638; Eukaryota.
DR HOGENOM; CLU_034004_3_1_1; -.
DR InParanoid; Q4WPV8; -.
DR OMA; FRPIAYR; -.
DR OrthoDB; 1087836at2759; -.
DR UniPathway; UPA00139; UER00362.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 3: Inferred from homology;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism;
KW Reference proteome; Repeat; Tyrosine catabolism.
FT CHAIN 1..406
FT /note="Probable 4-hydroxyphenylpyruvate dioxygenase 2"
FT /id="PRO_0000088402"
FT DOMAIN 22..174
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 205..363
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 208
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 406 AA; 45776 MW; BF038D6775106A55 CRC64;
MTVSKKVEEN IFASKLGPEY VGFDHITWYV GNAKQAASYY VTRMGFKQIA YRGPETGSRS
VVSHVISNGQ AIFVLTSPIR SMAGTGAYDD DPDVTKADRR LLEEIHNHLI KHGDGVKDVA
FRIEGDIEAV WKRAVDHGAA PVAAPTTLKD DRHGSITLAT IGTYEDTVHS LINRHDYSGP
FLPGYEVVTD DDPINRLLPS IDFIEIDHCV GNQPWNGVDP IVKYYEDCLN FHRYWTVDDL
NMCGEYSAMR SIVVASPNEV IKMPMNEPAQ GKKKSQIEEF VNYYNGAGVQ HIAFRTHDIV
TAVTRLRERG VSFLEVPSAY YSDLRQRLSH TGLTLEEDIA VLEKLHILVD FDEKGYLLQI
FSKHVLDRPT VFIEVIQRNN FDGFGAGNFK SLFEAFEREQ ARRGNL
