ID A0A2G5B8D5_COERN Unreviewed; 501 AA.
AC A0A2G5B8D5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=COEREDRAFT_82227 {ECO:0000313|EMBL:PIA15265.1};
OS Coemansia reversa (strain ATCC 12441 / NRRL 1564).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Coemansia.
OX NCBI_TaxID=763665 {ECO:0000313|EMBL:PIA15265.1, ECO:0000313|Proteomes:UP000242474};
RN [1] {ECO:0000313|EMBL:PIA15265.1, ECO:0000313|Proteomes:UP000242474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1564 {ECO:0000313|EMBL:PIA15265.1,
RC ECO:0000313|Proteomes:UP000242474};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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; KZ303509; PIA15265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5B8D5; -.
DR STRING; 763665.A0A2G5B8D5; -.
DR OrthoDB; 100633at2759; -.
DR Proteomes; UP000242474; 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; 2.60.120.620; q2cbj1_9rhob like domain; 2.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR InterPro; IPR006620; Pro_4_hyd_alph.
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:UP000242474};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 155..264
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 501 AA; 57937 MW; BB872754FEADACBD CRC64;
MMSESKVEAE YRAEKRARKD DRGVLEGATS LQLNSGYLEE EFINEFNRAF TLKDHKQTHH
IINLSKNKGQ GEVITYPFHT GRLRNILPAE FLHKLKTELT ELDWHERSND LYWFHQTDDL
ALNGGKCIKQ LRDYLSGEEF VGFMEQITGV QLTRGYLDIA AQRYKQGNHL LCHDDDVQRG
KLTRKIAYII YLVDEDWKEK DGGALGLFTT DENGYPAKVV SRIIPEFNSI GFFLTGHESF
HTVEEVTVVD ANRERWSVTG WFYGPVDVLE SETSAPPLPS SVLPKLLPLV DSDNEDAAVW
RRWINSEYLK PNVQTKIQET FLEQSSVELC DFLLPEVYYN FTAKLTSKVW REQNYPAHVS
KYYEASVTEE LLLFLRSGSF GRFLTQLTSL DYSRVSQQIR KFDKGDYTLI NDQALEPNGL
DVIMFLDNLE EPDNVWNTSW GGTIHYIADK DELLRIVPQS NSLALVLRDE GTLRFVKYVN
FMAQRPRKEI SMTFIEDDTS Q
//
