ID I2H3G6_TETBL Unreviewed; 591 AA.
AC I2H3G6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN Name=TBLA0D04210 {ECO:0000313|EMBL:CCH60918.1};
GN ORFNames=TBLA_0D04210 {ECO:0000313|EMBL:CCH60918.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH60918.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH60918.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE806319; CCH60918.1; -; Genomic_DNA.
DR RefSeq; XP_004180437.1; XM_004180389.1.
DR AlphaFoldDB; I2H3G6; -.
DR STRING; 1071380.I2H3G6; -.
DR GeneID; 14495954; -.
DR KEGG; tbl:TBLA_0D04210; -.
DR eggNOG; KOG3844; Eukaryota.
DR HOGENOM; CLU_017005_0_0_1; -.
DR InParanoid; I2H3G6; -.
DR OMA; SCYARTD; -.
DR OrthoDB; 100633at2759; -.
DR Proteomes; UP000002866; Chromosome 4.
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:UP000002866};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 134..243
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 69194 MW; 249A4E1D7C025043 CRC64;
MKRSSENSND SSKIQVTEDG KAKSLFNSKL WDPEFRDQMK DTITNNKPYE WGTITDLVDD
ELLRAVRKEI ETEISFSTKE TDIYRLNQSG DLANLSNLDD ENLKRLPNLY KLRSILYSNE
FRKFMAYITQ SGKLSESKRD LNIAIYNKNC HLLPHDDVVG SRRISYILYL PEPDRKWKDH
YGGGLRLYDS KKENVPYNDP FAKLVPQFNQ IAFFKIQPGL SFHDVEEVVV DKNRLSLQGW
FHIPQEGEDG YIENEEKEWI QNYITKLTEE DASDELKQYE FPKDDRSLIS SSLIKEFEKS
FKDFEFTKLT DNDIKLLKDF ISEEYLTNEK IAEIQEEFIA NSTINLSSFL NDEKSELLKN
LIKHEELQNE CPNLTKDVKN PWKVASPIHK WKFMYIDGKP ELKDDNQEDN EGSNFKLLRE
TIDQERLKLE NELIKVVEFL KSKTFKKFIL LLTKMIPITE QILIRRFRSG NDFTMANRIE
LNKYLENIEG YIASILEATL CLTPSTNWED GTNGGYEVFM AEVDDNAVNI DIKDTTVYDN
KHDSVLINNN ASWNTFSLAL IDDSLLEFVK YVSFNAKGSR WDIKMKWDVK E
//
