ID A1D2U7_NEOFI Unreviewed; 355 AA.
AC A1D2U7;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Oxidoreductase, putative {ECO:0000313|EMBL:EAW22740.1};
GN ORFNames=NFIA_014300 {ECO:0000313|EMBL:EAW22740.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW22740.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
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DR EMBL; DS027688; EAW22740.1; -; Genomic_DNA.
DR RefSeq; XP_001264637.1; XM_001264636.1.
DR AlphaFoldDB; A1D2U7; -.
DR EnsemblFungi; EAW22740; EAW22740; NFIA_014300.
DR GeneID; 4590830; -.
DR KEGG; nfi:NFIA_014300; -.
DR VEuPathDB; FungiDB:NFIA_014300; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_6_1_1; -.
DR OMA; AWFGHPN; -.
DR OrthoDB; 1332763at2759; -.
DR Proteomes; UP000006702; 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:0044249; P:cellular biosynthetic process; IEA:UniProt.
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:SF272; SEXUAL DIFFERENTIATION PROCESS PROTEIN ISP7; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PRINTS; PR00682; IPNSYNTHASE.
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:UP000006702}.
FT DOMAIN 176..288
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 85..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 355 AA; 39215 MW; DF8A889B9FD658A2 CRC64;
MVNHDTVDLP VIDFAALSEK DAAGHRTAVS IDERRRLFTA LRDTGFAYLK HPGVNQVTVD
ELFAHSRRFF AKPLEEKMQI LGKLDKGRGP SQGYSNPQKL AHNPQTSDLK EFFGMYRDDD
TEKPNQWLSD ADSKAMRTDL VRFFDSCHGV ILELLSALAE EVGLAAETLH PFISEKNHFI
ACLHYPATEP ESFRTRVRAA AHTDYGCMTL LFNDSGEGLQ VLRNNGQYEY VPRKDGCAVL
NVGDLLSRFF NGVLPSTMHR VVEPPATRSG SSADQVPDRY SIAFFGHFNL DLLVKPLDAL
VSATNPARFE PVVAGEHVKA RVKQLHVAGH SLTDNVKNAE SRAAVTQPAV ASASA
//
