NDOR1_ASHGO
ID NDOR1_ASHGO Reviewed; 620 AA.
AC Q75B78;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=NADPH-dependent diflavin oxidoreductase 1 {ECO:0000255|HAMAP-Rule:MF_03178};
DE EC=1.18.1.- {ECO:0000255|HAMAP-Rule:MF_03178};
DE AltName: Full=NADPH-dependent FMN and FAD-containing oxidoreductase {ECO:0000255|HAMAP-Rule:MF_03178};
GN Name=TAH18 {ECO:0000255|HAMAP-Rule:MF_03178}; OrderedLocusNames=ADL306C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: NADPH-dependent reductase which is a central component of the
CC cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery.
CC Transfers electrons from NADPH via its FAD and FMN prosthetic groups to
CC the [2Fe-2S] cluster of DRE2, another key component of the CIA
CC machinery. In turn, this reduced cluster provides electrons for
CC assembly of cytosolic iron-sulfur cluster proteins. Positively controls
CC H(2)O(2)-induced cell death. {ECO:0000255|HAMAP-Rule:MF_03178}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 oxidized [2Fe-2S]-[protein] = H(+) + NADP(+) + 2
CC reduced [2Fe-2S]-[protein]; Xref=Rhea:RHEA:67716, Rhea:RHEA-
CC COMP:17327, Rhea:RHEA-COMP:17328, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000255|HAMAP-Rule:MF_03178};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67717;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03178};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03178};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03178};
CC -!- SUBUNIT: Interacts with DRE2; as part of the cytosolic iron-sulfur (Fe-
CC S) protein assembly (CIA) machinery. {ECO:0000255|HAMAP-Rule:MF_03178}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03178}.
CC Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03178}. Note=Relocalizes to
CC mitochondria after H(2)O(2) exposure. {ECO:0000255|HAMAP-
CC Rule:MF_03178}.
CC -!- SIMILARITY: Belongs to the NADPH-dependent diflavin oxidoreductase
CC NDOR1 family. {ECO:0000255|HAMAP-Rule:MF_03178}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC family. {ECO:0000255|HAMAP-Rule:MF_03178}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP-
CC Rule:MF_03178}.
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DR EMBL; AE016817; AAS51614.1; -; Genomic_DNA.
DR RefSeq; NP_983790.1; NM_209143.2.
DR AlphaFoldDB; Q75B78; -.
DR SMR; Q75B78; -.
DR STRING; 33169.AAS51614; -.
DR EnsemblFungi; AAS51614; AAS51614; AGOS_ADL306C.
DR GeneID; 4619925; -.
DR KEGG; ago:AGOS_ADL306C; -.
DR eggNOG; KOG1159; Eukaryota.
DR HOGENOM; CLU_001570_17_6_1; -.
DR InParanoid; Q75B78; -.
DR OMA; QLFEMMP; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0097361; C:CIA complex; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; IEA:EnsemblFungi.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:1905118; P:positive regulation of ribonucleoside-diphosphate reductase activity; IEA:EnsemblFungi.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR HAMAP; MF_03178; NDOR1; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR028879; NDOR1.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; FMN; Mitochondrion; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..620
FT /note="NADPH-dependent diflavin oxidoreductase 1"
FT /id="PRO_0000167612"
FT DOMAIN 6..168
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT DOMAIN 222..475
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 12..17
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 59..62
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 106..115
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 380
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 410..413
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 442..445
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 535..536
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 620
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
SQ SEQUENCE 620 AA; 70540 MW; 2BDC608A61A83D57 CRC64;
MAATRIAILY GSETGTAQDF ANILSHQLRR FHYKHTVCSI GEYSAQNILA CQYLFVICST
TGQGALPQNA RQSPQGKVEG TLWSVLKRSS LPPTLLDHLQ VAFLGLGDSS YSKFNFAIRK
LHNRIVGQLG AREIFPRLEA DAIGLAGSNA GNGNGIELVY SEFEKRVLSF LNDQFPFMTV
NGEQVPREPI ATDIYLKPEY YLEASGNDKG TASVPCTFEG DSSVKYGTVV TNKRITATDH
FQDVRQLVFS SQDGENYYPG DTVSIYPYNT DADVQAFIDT QQHWASIADV PLQIKTPTSA
RGICDGGLVS PLTLRNLLKY HCDIVSIPMR SFFMKTWTFA VDHERLPDGK DQLQQQRDKL
REFAESEDMQ DIYDYCNRPR RSILEVVQDF MSLRLPWEYI LDYLPHIKPR FFSISSQPCN
KDIELTIAIV RYKTILRRIR RGLCTNYISD LSEGSIIRYK VQYNDLLPAG KQDRPVIMIS
PGVGLAPMKC LIYAQLFNPM LLFFGNRYKD KDFLYADTLQ KWADENRIKL FVCFSRSPDD
SPGLKYVQDA VWENAREVAR LITEENAVVY VCGSSGKMPV QVRLTLCEVL KKWGNFPDDK
ASEEYLKDME NSDRYLQETW
