ID A0A1Y2W095_9PEZI Unreviewed; 671 AA.
AC A0A1Y2W095;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=M426DRAFT_74800 {ECO:0000313|EMBL:OTB02108.1};
OS Hypoxylon sp. CI-4A.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB02108.1, ECO:0000313|Proteomes:UP000242955};
RN [1] {ECO:0000313|EMBL:OTB02108.1, ECO:0000313|Proteomes:UP000242955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CI-4A {ECO:0000313|EMBL:OTB02108.1,
RC ECO:0000313|Proteomes:UP000242955};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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; KZ111573; OTB02108.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2W095; -.
DR STRING; 1001833.A0A1Y2W095; -.
DR InParanoid; A0A1Y2W095; -.
DR OrthoDB; 100633at2759; -.
DR Proteomes; UP000242955; 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:UP000242955};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 143..268
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 74810 MW; EF423F6802B71C94 CRC64;
MKRKAQSQAS DQKPSKKKPK TSLSNEDARK RFRKGLFDKD VLNNYTQGYA TSAPYKHSVI
HELIDDTLLR SVREEIKNNV SFTPKETDIY KIHQSGDLAN LDGLDDEALA KLPSLLALRD
AMYSQAFRDY VATITGCGPL SGRKTDMAIN VYTPGCYLLC HDDVIGSRKV SYILYLTDPD
IPWKAEWGGA LRLFPVRTIK GKDGQVARTP APDVSKIIPP AWNQLSFFAV QPGESFHDVE
EVYHAESKAQ LEKEGGRVRM AISGWFHIPQ VGEDGYVEGA EEKLAKNSGL MQLQGNPEQY
DKPQLKPTTV KQPKSTSPDD FDEADLEFLL KYMAPTYLTP DTLEQISEQF DELSTITLPN
LLGKKFSEKL RDYVAAQEAA TLPEDSAEIE KGPWRVAKPP HKHRYLYLQA DGAKNGKSKK
DESPIKELLE EFLPSPQFRR WLQIATSCVV ESHDFIARRF RHGKDYTLAT GHEGKPRLEL
TLGITPTTGW GGEEEDKDED TDDDAAESAP EKNGDKTNGK GKAKAKAEAP SKKNNKHKKQ
DEEEEEEEPV EVGGHEVYMA GDADDEEDAA VYKSSGDDDN ILFFEGAAWN KMSLVLRDSG
ALKFVKYVSR KAPGDRWDIS GTFEVEEADD SDDSDGEDVN GKENGTAVGV LDDTEEEEWN
GFSSSVDSDS D
//
