ID K1WN02_MARBU Unreviewed; 660 AA.
AC K1WN02;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=2-oxoglutarate and Fe(II) dioxygenase domain containing protein 1 {ECO:0000313|EMBL:EKD19070.1};
GN ORFNames=MBM_02307 {ECO:0000313|EMBL:EKD19070.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD19070.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD19070.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD19070.1};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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; JH921431; EKD19070.1; -; Genomic_DNA.
DR RefSeq; XP_007290196.1; XM_007290134.1.
DR AlphaFoldDB; K1WN02; -.
DR STRING; 1072389.K1WN02; -.
DR GeneID; 18758242; -.
DR KEGG; mbe:MBM_02307; -.
DR eggNOG; KOG3844; Eukaryota.
DR HOGENOM; CLU_017005_0_0_1; -.
DR InParanoid; K1WN02; -.
DR OMA; GWYHIPQ; -.
DR OrthoDB; 100633at2759; -.
DR Proteomes; UP000006753; 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:EKD19070.1};
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:UP000006753};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 146..270
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 474..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..561
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..660
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 74268 MW; 75C4327917B553E0 CRC64;
MKRKADTQPG SQDGKGILKK RAKIVLSSED VKKSFRKGLF AKDVLRKYGE DYAKSEPYKH
GVITSLIDDD LLRSVRDEIR ENVQFTPKET DIYKIHQSGD LANLDGLEDS ALEKLPSVLR
LRDAMYSSQF RKYVSKITGS GELSGRKTDM AINVYTPGCY LLCHDDVIGS RRISYILYLT
DPDIPWEEKW GGALRLFPTT THEDDGVTTI TPDPDTSKII PPAWNQLSFF AVQPGLSFHD
VEEVYHAKNE KQLAKDGNRI RMAISGWFHI PQIGEEGYVE GEEEKWGKNS SLKQLQGNPD
RYDMPKPQPI TVDLPTESNV EGFDEADLDF LLKYMAPTYL TPDTLEAIAE QFAEESTVTL
DGLLSKKFSS RVREYVEAQE ASPLPSSSTE IDKGPWKVAR PPHKHRYLYL QPFSSSTVDK
ASLEDPIKEL TEVFLSSRQF RQWLKLATKG EIENYDILAR RFRRGLDYAL ATSHEGEPRL
ELSLGLTPTP GWGAEEDEGE GADEHEEKDP APKKKSKSKK NGDSQTNGKD KKKEPEPEPE
PEEPKEEDDV GGYETYMAGD EDDAADAAVY KAATGEEDDN VLFTMPATWN KMSIVLRDSG
VLKFVKYVSK NAKGDRWDIS GSFGVKFSDE EGEEEMVPLP ESDEEEVFNG FPDSDDSDSD
//
