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HPPD1_ASPFU
ID   HPPD1_ASPFU             Reviewed;         403 AA.
AC   Q4WHU1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=4-hydroxyphenylpyruvate dioxygenase {ECO:0000303|PubMed:19028908};
DE            Short=4HPPD {ECO:0000305};
DE            Short=HPD {ECO:0000305};
DE            Short=HPPDase {ECO:0000305};
DE            EC=1.13.11.27 {ECO:0000269|PubMed:22046314};
DE   AltName: Full=L-tyrosine degradation gene cluster protein hppD {ECO:0000303|PubMed:22046314};
DE   AltName: Full=Pyomelanin biosynthesis cluster protein hppD {ECO:0000303|PubMed:22046314};
GN   Name=hppD {ECO:0000303|PubMed:19028908}; ORFNames=AFUA_2G04200;
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).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND PATHWAY.
RX   PubMed=19028908; DOI=10.1128/aem.02077-08;
RA   Schmaler-Ripcke J., Sugareva V., Gebhardt P., Winkler R., Kniemeyer O.,
RA   Heinekamp T., Brakhage A.A.;
RT   "Production of pyomelanin, a second type of melanin, via the tyrosine
RT   degradation pathway in Aspergillus fumigatus.";
RL   Appl. Environ. Microbiol. 75:493-503(2009).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19715768; DOI=10.1016/j.fgb.2009.08.005;
RA   Valiante V., Jain R., Heinekamp T., Brakhage A.A.;
RT   "The MpkA MAP kinase module regulates cell wall integrity signaling and
RT   pyomelanin formation in Aspergillus fumigatus.";
RL   Fungal Genet. Biol. 46:909-918(2009).
RN   [4]
RP   FUNCTION, INDUCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=22046314; DOI=10.1371/journal.pone.0026604;
RA   Keller S., Macheleidt J., Scherlach K., Schmaler-Ripcke J., Jacobsen I.D.,
RA   Heinekamp T., Brakhage A.A.;
RT   "Pyomelanin formation in Aspergillus fumigatus requires HmgX and the
RT   transcriptional activator HmgR but is dispensable for virulence.";
RL   PLoS ONE 6:e26604-e26604(2011).
CC   -!- FUNCTION: 4-hydroxyphenylpyruvate dioxygenase; part of the L-tyrosine
CC       degradation gene cluster that mediates the biosynthesis of the brownish
CC       pigment pyomelanin as an alternative melanin (PubMed:19028908,
CC       PubMed:22046314). The 4-hydroxyphenylpyruvate dioxygenase hppD
CC       catalyzes the conversion of 4-hydroxyphenylpyruvate to homogentisic
CC       acid (HGA) (PubMed:19028908, PubMed:22046314). The protein hmgX is
CC       crucial for this conversion and thus, probably functions as an
CC       accessory factor to mediate specific activity of hppD
CC       (PubMed:22046314). The homogentisate 1,2-dioxygenase hmgA is then
CC       involved in the cleavage of the aromatic ring of HGA and its conversion
CC       to 4-maleylacetoacetate (PubMed:19028908, PubMed:19715768). When hmgA
CC       activity is lowered by the cell wall integrity (CWI) signaling pathway,
CC       HGA accumulates and leads to the production of pyomelanin through
CC       benzoquinone acetic acid after oxidation and polymerization
CC       (PubMed:19715768). On the opposite, in non-stress conditions, both hppD
CC       and hmgA activities are balanced and HGA is degraded into 4-
CC       maleylacetoacetate (PubMed:19715768). 4-maleylacetoacetate is further
CC       converted to 4-fumarylacetoacetate by the maleylacetoacetate isomerase
CC       maiA, which is degraded into fumarate and acetoacetate by the
CC       fumarylacetoacetase fahA (Probable). {ECO:0000269|PubMed:19028908,
CC       ECO:0000269|PubMed:19715768, ECO:0000269|PubMed:22046314,
CC       ECO:0000305|PubMed:19028908}.
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         Evidence={ECO:0000269|PubMed:22046314};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16190;
CC         Evidence={ECO:0000269|PubMed:22046314};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000250|UniProtKB:P93836};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250|UniProtKB:P93836};
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 3/6.
CC       {ECO:0000305|PubMed:19028908}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P93836}.
CC   -!- INDUCTION: Expression is induced by L-tyrosine (PubMed:19028908).
CC       Expression is positively regulated by the cluster-specific
CC       transcription factor hmgR (PubMed:22046314).
CC       {ECO:0000269|PubMed:19028908, ECO:0000269|PubMed:22046314}.
CC   -!- DISRUPTION PHENOTYPE: Impairs growth on L-tyrosine as the sole carbon
CC       source and affects homogentisic acid and pyomelanin formation
CC       (PubMed:19028908, PubMed:19715768). Leads to increased sensitivity to
CC       reactive oxygen intermediates (PubMed:19028908).
CC       {ECO:0000269|PubMed:19028908, ECO:0000269|PubMed:19715768}.
CC   -!- SIMILARITY: Belongs to the 4HPPD family. {ECO:0000305}.
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DR   EMBL; AAHF01000008; EAL87514.1; -; Genomic_DNA.
DR   RefSeq; XP_749552.1; XM_744459.1.
DR   AlphaFoldDB; Q4WHU1; -.
DR   SMR; Q4WHU1; -.
DR   STRING; 746128.CADAFUBP00002076; -.
DR   PRIDE; Q4WHU1; -.
DR   EnsemblFungi; EAL87514; EAL87514; AFUA_2G04200.
DR   GeneID; 3507145; -.
DR   KEGG; afm:AFUA_2G04200; -.
DR   VEuPathDB; FungiDB:Afu2g04200; -.
DR   eggNOG; KOG0638; Eukaryota.
DR   HOGENOM; CLU_034004_3_1_1; -.
DR   InParanoid; Q4WHU1; -.
DR   OMA; DPFPVKG; -.
DR   OrthoDB; 1087836at2759; -.
DR   UniPathway; UPA00139; UER00362.
DR   Proteomes; UP000002530; Chromosome 2.
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:0042438; P:melanin biosynthetic process; IMP:AspGD.
DR   GO; GO:0006572; P:tyrosine catabolic process; IMP:AspGD.
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   1: Evidence at protein level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism;
KW   Reference proteome; Repeat; Tyrosine catabolism.
FT   CHAIN           1..403
FT                   /note="4-hydroxyphenylpyruvate dioxygenase"
FT                   /id="PRO_0000088401"
FT   DOMAIN          25..169
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          201..359
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         204
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P93836"
FT   BINDING         287
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P93836"
FT   BINDING         370
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P93836"
SQ   SEQUENCE   403 AA;  45534 MW;  849FED016DA354AC CRC64;
     MAPSAISTSP PPTDRVSSSL ASYKGYDHVH WYVGNAKQAA SYYITRMGFK RIAYRGLETG
     CRSVCSHVVR NGDITFILTS PLRSLDQVDR FPPEEQELLK EIHAHLEKHG DGVKDVAFEV
     DSVDSVFYAA TNNGAKIVSQ PRTLEDDNGQ VRVATIQTYG ETTHTLVERG SYHGAFLPGY
     RMETGVEDPI SQLLPGVHLN RIDHCVGNQD WDEMDKVCEY YEKALGFHRF WSVDDKQICT
     EYSALKSIVM ASPNEVVKMP INEPAKGKKQ SQIEEYVDFY NGAGVQHIAL LTDDIIRDIT
     NLKARGVEFI KVPDTYYEDI KVRLKKAGLT LHEDFETIRS LDILIDFDEG GYLLQLFTKH
     LMDRPTVFIE IIQRHNFSGF GAGNFKSLFE AIEREQALRG NLV
 
 
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