ID A0A2T0FGX6_9ASCO Unreviewed; 537 AA.
AC A0A2T0FGX6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Prolyl 3,4-dihydroxylase ofd1 {ECO:0000313|EMBL:PRT54253.1};
GN ORFNames=B9G98_01873 {ECO:0000313|EMBL:PRT54253.1};
OS Wickerhamiella sorbophila.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trichomonascaceae; Wickerhamiella.
OX NCBI_TaxID=45607 {ECO:0000313|EMBL:PRT54253.1, ECO:0000313|Proteomes:UP000238350};
RN [1] {ECO:0000313|EMBL:PRT54253.1, ECO:0000313|Proteomes:UP000238350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS02 {ECO:0000313|EMBL:PRT54253.1,
RC ECO:0000313|Proteomes:UP000238350};
RA Ahn J.O.;
RT "Genome sequencing of [Candida] sorbophila.";
RL Submitted (APR-2017) 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:PRT54253.1}.
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DR EMBL; NDIQ01000021; PRT54253.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0FGX6; -.
DR STRING; 45607.A0A2T0FGX6; -.
DR OrthoDB; 100633at2759; -.
DR Proteomes; UP000238350; 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 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:UP000238350};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 137..243
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 60658 MW; 6C912F5432BC70FA CRC64;
MSEPEVKKQR TDNGVSEAKV LPEEALRPGI LDPKFQDELR DSIRNSDPYK HGVIHGLLND
KLLRQAREEI LEHLHFTQKE TDIYKVNQTG DLANLSGLDT DELSKLKAVA KVREGLYSKE
FREMMSYVTD CGPLSGKQQD LSINLYNKGC HLLNHDDVIG TRRISYILYL VPPDTPWDPK
WGGSLRLFPI EQPGVPAADF SKEIPPEWNQ LSFFKVQPGY SFHDVEEVYV DQPRLSISGW
FHIPHPDEPG YDANILAEDD GSKATLAQLS GRGDSHHFEP YTDDEKAELS EADKEYLGEF
INQDVLDRVP SLLETFTSAS VLTIANFLKP DVFDKIAQAT EVDDLAKIPK TEKDISAPWQ
LAKPSHIRHY MFIANDEQVP ATEDLAAHVE LQKIRDFIVS PQFGRFVNAI TSLEPKSRYA
EARRFRPGHD FTLATGLPQD ALLEATLHLT SAKWSDDVGG YEMLMATEDN DDDPAVYRAA
AESMVLHSSA PVANELVIYL REKEVLQFVK YVSRNAPSSR WDVAAEFEVD FGDEEDK
//
