ID A0A0L1J7W9_ASPNO Unreviewed; 640 AA.
AC A0A0L1J7W9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KNG87483.1};
GN ORFNames=ANOM_004150 {ECO:0000313|EMBL:KNG87483.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG87483.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG87483.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG87483.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:KNG87483.1}.
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DR EMBL; JNOM01000080; KNG87483.1; -; Genomic_DNA.
DR RefSeq; XP_015408406.1; XM_015549407.1.
DR AlphaFoldDB; A0A0L1J7W9; -.
DR STRING; 1509407.A0A0L1J7W9; -.
DR GeneID; 26805954; -.
DR OrthoDB; 100633at2759; -.
DR Proteomes; UP000037505; 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:UP000037505};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 144..267
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..521
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..640
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 72458 MW; F0165FF8279D75CA CRC64;
MKRKTEGRES LGGSDQPDSK RRALTSEEAA ARFRDGLFEP SEQQKYTEQY AESAPYKHGV
IHPLIEPSLL RAVRNEIQEH LDFTEKETDI YKIFQSGDLA NLDGLDDASL SRLPSLLKLR
DAMYSARFRE YLSSVTGSGK LSGRKTDMAI NIYNEGCHLL CHDDVIGSRR VSYILYLTDP
DTPWQAEWGG ALRLYPTTTK KDAEGEDVKI PSPDFSLSIP PAFNQLSFFT VQPGESFHDV
EEVYHYKEGE DRSKKRVRMA ISGWFHIPQK GEDGYEEGLE EKLAERSSLA QLQGRGDIYD
LPQPKTVVCE NESQEVEGKG KGKVEEQPSS EFTEADLNFL IQYIAPSYLT PDIAEEMSET
FTNESSLNLE QFLSEKFSAR VREYIEEQEK KTLPQSSDEI QAQTGWTVAR PPHKQRYMFL
QHSTAAQDEK SPLQELLNDV FPSPAFRKWL AAITGAERLT SYDFMARRFR RGQDYTLASG
YDGEEPRLEF TLSLTPTPGW EKEGDEEEDD EEDDDDEDGE NDESEKKPKA EPKEKEPKSD
AEEPAVGGYE LYMAGDDEEE GDAAIYRSAA ADEDDGILFS TSAGWNRLSI VLRDSGTLKF
VKYVSAAAKG DRWDITGEMG VEFNDDDEDD EDDEMEADEE
//
