NDOR1_YEAST
ID NDOR1_YEAST Reviewed; 623 AA.
AC Q12181; D6W456;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
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, ECO:0000269|PubMed:20802492};
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=YPR048W;
GN ORFNames=YP9499.06;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=12759774; DOI=10.1007/s00294-003-0407-2;
RA Chanet R., Heude M.;
RT "Characterization of mutations that are synthetic lethal with pol3-13, a
RT mutated allele of DNA polymerase delta in Saccharomyces cerevisiae.";
RL Curr. Genet. 43:337-350(2003).
RN [4]
RP FUNCTION IN APOPTOSIS, INTERACTION WITH DRE2, AND SUBCELLULAR LOCATION.
RX PubMed=19194512; DOI=10.1371/journal.pone.0004376;
RA Vernis L., Facca C., Delagoutte E., Soler N., Chanet R., Guiard B.,
RA Faye G., Baldacci G.;
RT "A newly identified essential complex, Dre2-Tah18, controls mitochondria
RT integrity and cell death after oxidative stress in yeast.";
RL PLoS ONE 4:E4376-E4376(2009).
RN [5]
RP FUNCTION, COFACTOR, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP INTERACTION WITH DRE2.
RX PubMed=20802492; DOI=10.1038/nchembio.432;
RA Netz D.J., Stumpfig M., Dore C., Muhlenhoff U., Pierik A.J., Lill R.;
RT "Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein
RT biogenesis.";
RL Nat. Chem. Biol. 6:758-765(2010).
RN [6]
RP FUNCTION, AND INTERACTION WITH DRE2.
RX PubMed=21902732; DOI=10.1111/j.1365-2958.2011.07788.x;
RA Soler N., Delagoutte E., Miron S., Facca C., Baille D., d'Autreaux B.,
RA Craescu G., Frapart Y.M., Mansuy D., Baldacci G., Huang M.E., Vernis L.;
RT "Interaction between the reductase Tah18 and highly conserved Fe-S
RT containing Dre2 C-terminus is essential for yeast viability.";
RL Mol. Microbiol. 82:54-67(2011).
CC -!- FUNCTION: NADPH-dependent reductase which is a central component of the
CC cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery
CC (PubMed:20802492). Transfers electrons from NADPH via its FAD and FMN
CC prosthetic groups to the [2Fe-2S] cluster of DRE2, another key
CC component of the CIA machinery (PubMed:20802492, PubMed:21902732). In
CC turn, this reduced cluster provides electrons for assembly of cytosolic
CC iron-sulfur cluster proteins (PubMed:20802492). Positively controls
CC H(2)O(2)-induced cell death (PubMed:19194512). {ECO:0000255|HAMAP-
CC Rule:MF_03178, ECO:0000269|PubMed:19194512,
CC ECO:0000269|PubMed:20802492, ECO:0000269|PubMed:21902732}.
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 ECO:0000269|PubMed:20802492};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67717;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03178,
CC ECO:0000305|PubMed:20802492};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03178,
CC ECO:0000269|PubMed:20802492};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03178,
CC ECO:0000269|PubMed:20802492};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=26 uM for NADPH {ECO:0000269|PubMed:20802492};
CC KM=12 uM for cytochrome c {ECO:0000269|PubMed:20802492};
CC Vmax=0.11 umol/min/mg enzyme {ECO:0000269|PubMed:20802492};
CC Note=kcat is 0.14 sec(-1) for cytochrome c reduction.
CC {ECO:0000269|PubMed:20802492};
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 ECO:0000269|PubMed:19194512, ECO:0000269|PubMed:21902732}.
CC -!- INTERACTION:
CC Q12181; P36152: DRE2; NbExp=3; IntAct=EBI-37624, EBI-26482;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03178,
CC ECO:0000269|PubMed:19194512}. Mitochondrion {ECO:0000255|HAMAP-
CC Rule:MF_03178, ECO:0000269|PubMed:19194512}. Note=Relocalizes to
CC mitochondria after H(2)O(2) exposure. {ECO:0000255|HAMAP-Rule:MF_03178,
CC ECO:0000269|PubMed:19194512}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z71255; CAA94995.1; -; Genomic_DNA.
DR EMBL; Z49219; CAA89168.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11472.1; -; Genomic_DNA.
DR PIR; S54072; S54072.
DR RefSeq; NP_015373.1; NM_001184145.1.
DR AlphaFoldDB; Q12181; -.
DR SMR; Q12181; -.
DR BioGRID; 36224; 150.
DR ComplexPortal; CPX-386; TAH18-DRE2 complex.
DR DIP; DIP-1688N; -.
DR IntAct; Q12181; 7.
DR MINT; Q12181; -.
DR STRING; 4932.YPR048W; -.
DR MaxQB; Q12181; -.
DR PaxDb; Q12181; -.
DR PRIDE; Q12181; -.
DR EnsemblFungi; YPR048W_mRNA; YPR048W; YPR048W.
DR GeneID; 856161; -.
DR KEGG; sce:YPR048W; -.
DR SGD; S000006252; TAH18.
DR VEuPathDB; FungiDB:YPR048W; -.
DR eggNOG; KOG1159; Eukaryota.
DR GeneTree; ENSGT00930000151050; -.
DR HOGENOM; CLU_001570_17_6_1; -.
DR InParanoid; Q12181; -.
DR OMA; QLFEMMP; -.
DR BioCyc; YEAST:G3O-34203-MON; -.
DR PRO; PR:Q12181; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12181; protein.
DR GO; GO:0097361; C:CIA complex; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
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:0016651; F:oxidoreductase activity, acting on NAD(P)H; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:ComplexPortal.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:ComplexPortal.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:SGD.
DR GO; GO:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; IMP:SGD.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:SGD.
DR GO; GO:1905118; P:positive regulation of ribonucleoside-diphosphate reductase activity; IMP:ComplexPortal.
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 1: Evidence at protein level;
KW Cytoplasm; FAD; Flavoprotein; FMN; Mitochondrion; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..623
FT /note="NADPH-dependent diflavin oxidoreductase 1"
FT /id="PRO_0000167624"
FT DOMAIN 7..168
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT DOMAIN 224..491
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 13..18
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 60..63
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 142
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 383
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 413..416
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 445..448
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 538..539
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 623
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
SQ SEQUENCE 623 AA; 72328 MW; 5248B9512F77D628 CRC64;
MSSSKKIVIL YGSETGNAHD FATILSHRLH RWHFSHTFCS IGDYDPQDIL KCRYLFIICS
TTGQGELPRN VNALKGERPV TFWSFLKRKN LPSNLLNHIQ TAMLGLGDSS YPKFNYGIRK
LHQRIVTQLG ANELFDRLEA DDQAMAGSNK GTGLGIESVY FEYEKKVLSF LLSKYPNRKV
NGQIIKREEL DPEVYLEPAS YLQLSDEHAN EKFTSTKVIF EGDESLKVGR VNINKRITSE
GHFQDVRQFK FSNVDKIQEN YEPGDTVTIY PCNTDEDVSR FLANQSHWLE IADKPLNFTS
GVPNDLKDGG LVRPMTLRNL LKYHCDFMSI PRTSFFLKIW TFATDVTKME RGQEQLNDQR
EKLRQFATDQ DMQDLYDYCN RPRRSILEVL EDFISVKLPW KYVLDYLPII KPRYYSISSG
PGDPNIELTV AIVKYKTILR KIRRGICTNY IARLQEGEQI RYKLQNNHII KKEFLNKPMI
LVGPGVGLAP LLSVVKAEIS KDIKLLFGCR YKDKDYIYKD MLEDWFRKGK IALHSSFSRD
EENSPGVKYV QDYLWRLGEE ITNLVVNKDA VFFLCGSSGK MPIQVRLTFI EMLKKWGNFS
DEETAKKYLK EMEKSDRYIQ ETW
