ID A0A084GF91_PSEDA Unreviewed; 384 AA.
AC A0A084GF91;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=SAPIO_CDS1406 {ECO:0000313|EMBL:KEZ46003.1};
OS Pseudallescheria apiosperma (Scedosporium apiospermum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Microascaceae; Scedosporium.
OX NCBI_TaxID=563466 {ECO:0000313|EMBL:KEZ46003.1, ECO:0000313|Proteomes:UP000028545};
RN [1] {ECO:0000313|EMBL:KEZ46003.1, ECO:0000313|Proteomes:UP000028545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHEM 14462 {ECO:0000313|EMBL:KEZ46003.1,
RC ECO:0000313|Proteomes:UP000028545};
RX PubMed=25278533; DOI=10.1128/genomea.00988-14;
RA Vandeputte P., Ghamrawi S., Rechenmann M., Iltis A., Giraud S., Fleury M.,
RA Thornton C., Delhaes L., Meyer W., Papon N., Bouchara J.P.;
RT "Draft genome sequence of the pathogenic fungus Scedosporium apiospermum.";
RL Genome Announc. 2:E00988-E00988(2014).
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEZ46003.1}.
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DR EMBL; JOWA01000055; KEZ46003.1; -; Genomic_DNA.
DR RefSeq; XP_016645802.1; XM_016784686.1.
DR AlphaFoldDB; A0A084GF91; -.
DR GeneID; 27720478; -.
DR KEGG; sapo:SAPIO_CDS1406; -.
DR VEuPathDB; FungiDB:SAPIO_CDS1406; -.
DR HOGENOM; CLU_010119_1_1_1; -.
DR OMA; ARETGFF; -.
DR OrthoDB; 1380829at2759; -.
DR Proteomes; UP000028545; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR47990:SF34; 2-OXOGLUTARATE-DEPENDENT DIOXYGENASE 33; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 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:UP000028545}.
FT DOMAIN 174..280
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 384 AA; 42894 MW; 8C7AB4CDF816C6CE CRC64;
MSFQSIPILD LSLARNPETK PEFLKELRHA LMEVGFLYLK NIGIPDDLWQ SVIRLGKEFF
DIPEEEKLRI EMKNAPSFLG YSRLSAEITA GAIDHREQID LSTEHPTPAP GSPLHYNLLA
PNQWPAEEAL PGFRAAFTDY MNRMGKISIE FTSLIAEAIE LPADAFSKYF DENQQHKLKI
VKYPDLQELG LEGEGQGVGP HKDSMLSSYL LQVTNHRGLQ VQNLDGQWID CPPIDKTLVV
AIGQGLEALT GGVCASTTHR VLSPPAGQGA RLSIPFFQGV RGDTDFIDLE TVGVGEVPEH
VREQRRRIIA EHGGRLDDVE FTFRKGGVAK TLGEATLRNR VKSHPDVAER WYPDLLRDVR
EEQERIKRGK EQAIPVAPAT VVAH
//
