ID A0A1V6RX35_9EURO Unreviewed; 658 AA.
AC A0A1V6RX35;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=PENVUL_c018G06364 {ECO:0000313|EMBL:OQE06327.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE06327.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + [ribosomal protein uS12]-L-proline + O2 =
CC [ribosomal protein uS12]-(3S)-3-hydroxy-L-proline + CO2 + succinate;
CC Xref=Rhea:RHEA:54156, Rhea:RHEA-COMP:13816, Rhea:RHEA-COMP:13818,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:85428;
CC Evidence={ECO:0000256|ARBA:ARBA00001792};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SIMILARITY: Belongs to the TPA1 family.
CC {ECO:0000256|ARBA:ARBA00007443}.
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:OQE06327.1}.
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DR EMBL; MDYP01000018; OQE06327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6RX35; -.
DR STRING; 29845.A0A1V6RX35; -.
DR OrthoDB; 100633at2759; -.
DR Proteomes; UP000191518; Unassembled WGS sequence.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0031543; F:peptidyl-proline dioxygenase activity; IEA:UniProt.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.60.130.20; Oxoglutarate/iron-dependent oxygenase, C-terminal degradation domain; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR043044; TPA1/Ofd1_C.
DR InterPro; IPR039558; TPA1/OFD1_N.
DR PANTHER; PTHR12117; HISTONE ACETYLTRANSFERASE COMPLEX; 1.
DR PANTHER; PTHR12117:SF0; PROLYL 3-HYDROXYLASE OGFOD1; 1.
DR Pfam; PF13661; 2OG-FeII_Oxy_4; 1.
DR Pfam; PF10637; Ofd1_CTDD; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000191518};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 144..267
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..516
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..563
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 658 AA; 74051 MW; 2DB94C835CF146D7 CRC64;
MKRKTDSRAS LDGNAMRQSK KRALSSEEAA ARFRDGLFDA AEQQKYTDQY AKSSPYLHGV
IHPLIEPTLL RSVRNEIETQ VSFTEKETDI YKIFQSGDLA NLDGLDDSSL SKLPSVLKLR
DAIYSARFRE YLSSVTGSGK LSGQKTDMAI NVYTEGCHLL CHDDVIGSRR VSYILYLTDP
DTPWQAEWGG ALRLFPTTTK KDAKGKDVKI PSPDYSLSIP PAFNQLSFFT VQPGESFHDV
EEVYHPRDDE DKTKKRVRMA ISGWFHIPQK GEDGYEEGLE EKLAERSSLA QLQGRGDIYD
LPQSQPVSWE EPEVEGKGKG KVEEQTEGEF TESDLAFLLR YIAPSYLTPD IAEEMSDAFS
AESSLSLEQF LSDKFGSRVS AYIEEQERQP LPASADEIQV QRGWTVARPP HKHRYLYQHA
SGEKDTDNPI QELLNVLFPS QAFRKWLSLV TGVDHLTSHN LLARRFRRGC DYTLASSYEG
EEPRLEFSLC ITPSTGWEKQ EEEEDEDEDE DEDEEANGSS AKASKPKEQL NDDTVEGPAL
GGYEIYMAGD EDEDDDDEED AENADQVLGR KKTKADPAVY RSAGEDEDDG ILFSTQAGWN
RLSIVLRDSG TLKFVKYVSA AAKGDRWDIT GEIGVEFEEG DEDEYDGDEG EDEDEDEE
//
