ID A0A2S5BHM4_9BASI Unreviewed; 631 AA.
AC A0A2S5BHM4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=BMF94_0449 {ECO:0000313|EMBL:POY76254.1};
OS Rhodotorula taiwanensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=741276 {ECO:0000313|EMBL:POY76254.1, ECO:0000313|Proteomes:UP000237144};
RN [1] {ECO:0000313|EMBL:POY76254.1, ECO:0000313|Proteomes:UP000237144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD1149 {ECO:0000313|EMBL:POY76254.1,
RC ECO:0000313|Proteomes:UP000237144};
RX PubMed=29375494;
RA Tkavc R., Matrosova V.Y., Grichenko O.E., Gostincar C., Volpe R.P.,
RA Klimenkova P., Gaidamakova E.K., Zhou C.E., Stewart B.J., Lyman M.G.,
RA Malfatti S.A., Rubinfeld B., Courtot M., Singh J., Dalgard C.L.,
RA Hamilton T., Frey K.G., Gunde-Cimerman N., Dugan L., Daly M.J.;
RT "Prospects for Fungal Bioremediation of Acidic Radioactive Waste Sites:
RT Characterization and Genome Sequence of Rhodotorula taiwanensis MD1149.";
RL Front. Microbiol. 8:2528-2528(2018).
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:POY76254.1}.
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DR EMBL; PJQD01000005; POY76254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5BHM4; -.
DR STRING; 741276.A0A2S5BHM4; -.
DR OrthoDB; 100633at2759; -.
DR Proteomes; UP000237144; 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:UP000237144};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 135..257
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..566
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..631
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 69344 MW; EAE4EC41950FF651 CRC64;
MTAAEEPTAK RQKLNEEKKQ QLPFHPSLLQ PDIVDRLRQL HDHSQPYKHA VIDKLFDPDF
LKRARKEITE QLSFREKETD IYKINQTGDL TNLSGLPAAE LALLPTLLEL RDALYGPDFR
AFLQKVTGCG PLSGSKTDMS CAEYSEGCYL LNHDDVIGTR RISFILYLVL DEPAWQPEWG
GALELYPVLE ADEKNPDRPN VPVAKPSTCI PPAFNQMVFF EVQPGHSFHS VEEVVVHGDG
QKGGVGARVS LSGWFHKPVE GEEGYEGSEG FQAKSSLQQL YATSLSAPTR YEEQLPLPLP
TLPSSADLDY LRPLLNPAYL TSKVIDLLRA QFVEQSHLVL ADFLAPSIAN ELEGLIRERD
AEMEKDRRGV TVNGQTTNNI PPHTAGEDER NGWAVVGPPH LQRYLALSPS SSASTPAADR
LSTLLREIHA LFTSSAFAAL LASLTSLLPT AYTTAVRRFR PGLDYSLARG ESASEPDAQA
KLDVGLGLTP KCEKESDREV WEGGEAGGWD VWLANEEGGD EATYGGGGGR GSAKEAAENG
TADAPETQAQ EEAEGEEEEE EEDGPLLALE PEWNRLHLVL RDPGVLSFVK YLSARAPASR
WDVVGEWEVQ GIEEEKAEDD DGDNQEEAAQ A
//
