ID L2GMK9_VITCO Unreviewed; 357 AA.
AC L2GMK9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=VICG_00920 {ECO:0000313|EMBL:ELA42071.1};
OS Vittaforma corneae (strain ATCC 50505) (Microsporidian parasite) (Nosema
OS corneum).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae;
OC Vittaforma.
OX NCBI_TaxID=993615 {ECO:0000313|EMBL:ELA42071.1, ECO:0000313|Proteomes:UP000011082};
RN [1] {ECO:0000313|Proteomes:UP000011082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50505 {ECO:0000313|Proteomes:UP000011082};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Didier E., Bowers L., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Vittaforma corneae strain ATCC 50505.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|RuleBase:RU003682}.
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DR EMBL; JH370135; ELA42071.1; -; Genomic_DNA.
DR RefSeq; XP_007604367.1; XM_007604305.1.
DR AlphaFoldDB; L2GMK9; -.
DR STRING; 993615.L2GMK9; -.
DR GeneID; 19881632; -.
DR VEuPathDB; MicrosporidiaDB:VICG_00920; -.
DR HOGENOM; CLU_816288_0_0_1; -.
DR InParanoid; L2GMK9; -.
DR OMA; RIVIFEV; -.
DR OrthoDB; 100633at2759; -.
DR Proteomes; UP000011082; 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:UP000011082};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 75..167
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 357 AA; 41642 MW; 5162D8B1F9FD38BF CRC64;
MNVTKPFKYE VVDSFLLESE LNKIKDIYST LSFKEVHTDL YNFLQSNELN YDDRFQFFKN
KLDNVFKDKV AEKDVFYTLF ASYYRKGDFL LCHDDMVDER LYAFTFYLDD FDSGQLVLYE
NDCETVHKKI GVCSNRLVIF EVEENSFHEV DQCRSSGRKA ISGWINSKTK KCQSKSFARS
HKVHENVEFF DLNIDIPVNS FVSLEFEDIE VKELSRSLKG PFIDRRVFEI ALEKLYTPQL
EGYALISAEC LLFTEGCYIL CNDRINAVMG DILDVYIFKH ISDKHNKPSS TIGKADAHSV
DGFITYVDQN SNMVFEIDAI GNHMVFGKRN GHCICIHRTL RQVYLKHFYL SKTKLGF
//
