ID A0A1V6PBL9_PENDC Unreviewed; 403 AA.
AC A0A1V6PBL9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE RecName: Full=4-hydroxyphenylpyruvate dioxygenase {ECO:0000256|ARBA:ARBA00013222, ECO:0000256|PIRNR:PIRNR009283};
GN ORFNames=PENDEC_c012G02925 {ECO:0000313|EMBL:OQD74167.1};
OS Penicillium decumbens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=69771 {ECO:0000313|EMBL:OQD74167.1, ECO:0000313|Proteomes:UP000191522};
RN [1] {ECO:0000313|Proteomes:UP000191522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11843 {ECO:0000313|Proteomes:UP000191522};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQD74167.1}.
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DR EMBL; MDYL01000012; OQD74167.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6PBL9; -.
DR STRING; 69771.A0A1V6PBL9; -.
DR OMA; DPFPVKG; -.
DR OrthoDB; 34818at2759; -.
DR UniPathway; UPA00139; UER00362.
DR Proteomes; UP000191522; 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; 2,3-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 Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR009283-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR009283-1};
KW Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232};
KW Reference proteome {ECO:0000313|Proteomes:UP000191522};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878}.
FT DOMAIN 25..169
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 201..359
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT BINDING 204
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT BINDING 287
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT BINDING 370
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
SQ SEQUENCE 403 AA; 45681 MW; C45DBCF3ABCBCE59 CRC64;
MAPSAISNSP PPSSNGASSL ASYRGYDHVH WYVGNAKQAA SYYITRMGFR RVAYRGLETG
SRSICSHVIR NGEITFILTS PLRSQDHIDR FTPEEQAELR EIHHHLEKHG DAVKDVSFEV
DDVDAIFNAA VKNGAKAVSE PKILKDKDGH VKVATIQTYG ETTHTLIERS QYHGAFLPGY
RLESDAEDPI SKFLPAVHLT HIDHCVGNQD WNEMDEICEY YEKALGFHRF WSVDDSQICT
EFSALKSIVM ASPNEVVKMP INEPAKGKKQ SQIEEYVDFY NGAGVQHIAL QTDDIIRDIT
NLKARGVEFI KVPETYYTDM KARLKQSSLV LKEDFETIKS LDILIDFDEG GYLLQLFTKH
MMDRPTVFIE IIQRHNFDGF GAGNFKSLFE AIEREQELRG NLV
//
