ID A0A1X0QAN6_9MICR Unreviewed; 285 AA.
AC A0A1X0QAN6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=OGFD1 {ECO:0000313|EMBL:ORD96836.1};
GN Name=OGFD1 {ECO:0000313|EMBL:ORD96836.1};
GN ORFNames=HERIO_1257 {ECO:0000313|EMBL:ORD96836.1};
OS Hepatospora eriocheir.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Hepatosporidae;
OC Hepatospora.
OX NCBI_TaxID=1081669 {ECO:0000313|EMBL:ORD96836.1, ECO:0000313|Proteomes:UP000192356};
RN [1] {ECO:0000313|EMBL:ORD96836.1, ECO:0000313|Proteomes:UP000192356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB1 {ECO:0000313|EMBL:ORD96836.1,
RC ECO:0000313|Proteomes:UP000192356};
RX PubMed=28345194; DOI=10.1111/1462-2920.13734;
RA Wiredu Boakye D., Jaroenlak P., Prachumwat A., Williams T.A., Bateman K.S.,
RA Itsathitphaisarn O., Sritunyalucksana K., Paszkiewicz K.H., Moore K.A.,
RA Stentiford G.D., Williams B.A.;
RT "Decay of the glycolytic pathway and adaptation to intranuclear parasitism
RT within Enterocytozoonidae microsporidia.";
RL Environ. Microbiol. 19:2077-2089(2017).
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|RuleBase:RU003682}.
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:ORD96836.1}.
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; LVKB01000059; ORD96836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0QAN6; -.
DR VEuPathDB; MicrosporidiaDB:A0H76_481; -.
DR VEuPathDB; MicrosporidiaDB:HERIO_1257; -.
DR Proteomes; UP000192356; Unassembled WGS sequence.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
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 PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|RuleBase:RU003682};
KW Metal-binding {ECO:0000256|RuleBase:RU003682};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW Reference proteome {ECO:0000313|Proteomes:UP000192356};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 18..110
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 285 AA; 33660 MW; 378EA3CDE79761BB CRC64;
MDFLKEKISK QFSEYKDTYF NIFGSYYREG DYLYTHDDCV AGREIAFILY LNDCKSGNLV
IYENDCKTVH LKIKPKRNRL AYFKVSDVSF HEVEKVLDVK RQAITGWLNV KGKINESRDL
KNDNMKVPDD LIYIDLPITK ENLTNLNHQE NKYFSMCLGY FELEEESIEK SGPFIKRRVS
KINLKSTPFA PSIESFNLIK YEYIKMEPND YILVNDDIND KTDNILDVFI FMDDYDNLIK
VHDSDISYIS AEQFTLLYGL RNGKVFSINN INKEVKFIHM IYELM
//
