ID   G3AEC7_SPAPN            Unreviewed;       609 AA.
AC   G3AEC7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Fe II, 2-oxoglutarate-dependent dioxygenase {ECO:0000313|EMBL:EGW35715.1};
GN   ORFNames=SPAPADRAFT_130916 {ECO:0000313|EMBL:EGW35715.1};
OS   Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN   [1] {ECO:0000313|EMBL:EGW35715.1, ECO:0000313|Proteomes:UP000000709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(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}.
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DR   EMBL; GL996499; EGW35715.1; -; Genomic_DNA.
DR   RefSeq; XP_007373127.1; XM_007373065.1.
DR   AlphaFoldDB; G3AEC7; -.
DR   STRING; 619300.G3AEC7; -.
DR   GeneID; 18869539; -.
DR   KEGG; spaa:SPAPADRAFT_130916; -.
DR   eggNOG; KOG3844; Eukaryota.
DR   HOGENOM; CLU_017005_0_0_1; -.
DR   InParanoid; G3AEC7; -.
DR   OMA; GWYHIPQ; -.
DR   OrthoDB; 100633at2759; -.
DR   Proteomes; UP000000709; 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, ECO:0000313|EMBL:EGW35715.1};
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:UP000000709};
KW   Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT   DOMAIN          137..247
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   609 AA;  69744 MW;  9D5008ED5F82C929 CRC64;
     MTKRKVDSVE NTDSKKQSIE FTKEDIVSFF NSQIWDSKFQ DDLKQSIEAS QPYRWGTVTQ
     LIDDTLLRQV RKEVLSEIAF TQKETDIYKV YQSGDLANLS GLDWNDLSRL PSLFKLRAGI
     YSQEFRDVIS KVTGCGKLSG VKTDISINTY TKGCHLLTHD DVIGSRRVSF ILYLPDPDRT
     WKESYGGGLR LYPAVIPNVP HTDYSQKLIP QFNQIAFFTV QPGLSFHDVE EVREDKQRLS
     IQGWFHIPQE GEDGFIPGEQ EETEARSTLQ QLQSKELQEY DFPKSERDRV VPSELNIYQS
     PFKSLSEAET EYLRKFINPL YLTDDVITKL NKSFIDESII EIQNVLVDEY ANVLRDQIRD
     LELNSVTPQK STDIEAPWKC AVPPHKQRFM YIDGKSPIGE MTESNINYVT KVGPQELPNF
     ALIEAKNDVD VKLIELASLF KSVAFKKWLK LLTDLVVTAD QVLVRRFRPG HDFILATTID
     KSETADEENV LLEATLNLTP SAVNPKNWES GEFGGYELCM LLAGDESDGE FEEDDDPAVY
     KANDPNDDSI LFTSQCKWNV LTLYLRDPSV LKFIKYVSIN AKGSRWDISG QWNVKTENDD
     EEEEQEDSK
//