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NADPH-dependent diflavin oxidoreductase 1 (EC 1.18.1.-) (NADPH-dependent FMN and FAD-containing oxidoreductase)

 NDOR1_YEAST             Reviewed;         623 AA.
Q12181; D6W456;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 143.
RecName: Full=NADPH-dependent diflavin oxidoreductase 1 {ECO:0000255|HAMAP-Rule:MF_03178};
EC=1.18.1.- {ECO:0000255|HAMAP-Rule:MF_03178};
AltName: Full=NADPH-dependent FMN and FAD-containing oxidoreductase {ECO:0000255|HAMAP-Rule:MF_03178};
Name=TAH18 {ECO:0000255|HAMAP-Rule:MF_03178};
OrderedLocusNames=YPR048W; ORFNames=YP9499.06;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169875;
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION.
PubMed=12759774; DOI=10.1007/s00294-003-0407-2;
Chanet R., Heude M.;
"Characterization of mutations that are synthetic lethal with pol3-13,
a mutated allele of DNA polymerase delta in Saccharomyces
cerevisiae.";
Curr. Genet. 43:337-350(2003).
[4]
FUNCTION IN APOPTOSIS, INTERACTION WITH DRE2, AND SUBCELLULAR
LOCATION.
PubMed=19194512; DOI=10.1371/journal.pone.0004376;
Vernis L., Facca C., Delagoutte E., Soler N., Chanet R., Guiard B.,
Faye G., Baldacci G.;
"A newly identified essential complex, Dre2-Tah18, controls
mitochondria integrity and cell death after oxidative stress in
yeast.";
PLoS ONE 4:E4376-E4376(2009).
[5]
FUNCTION, AND COFACTOR.
PubMed=20802492; DOI=10.1038/nchembio.432;
Netz D.J., Stumpfig M., Dore C., Muhlenhoff U., Pierik A.J., Lill R.;
"Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein
biogenesis.";
Nat. Chem. Biol. 6:758-765(2010).
[6]
FUNCTION, AND INTERACTION WITH DRE2.
PubMed=21902732; DOI=10.1111/j.1365-2958.2011.07788.x;
Soler N., Delagoutte E., Miron S., Facca C., Baille D., d'Autreaux B.,
Craescu G., Frapart Y.M., Mansuy D., Baldacci G., Huang M.E.,
Vernis L.;
"Interaction between the reductase Tah18 and highly conserved Fe-S
containing Dre2 C-terminus is essential for yeast viability.";
Mol. Microbiol. 82:54-67(2011).
-!- FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein
assembly (CIA) machinery. Required for the maturation of
extramitochondrial Fe-S proteins. Part of an electron transfer
chain functioning in an early step of cytosolic Fe-S biogenesis.
Transfers electrons from NADPH to the Fe-S cluster of DRE2.
Positively controls H(2)O(2)-induced cell death.
{ECO:0000255|HAMAP-Rule:MF_03178, ECO:0000269|PubMed:12759774,
ECO:0000269|PubMed:19194512, ECO:0000269|PubMed:20802492,
ECO:0000269|PubMed:21902732}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000255|HAMAP-Rule:MF_03178,
ECO:0000269|PubMed:20802492};
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000255|HAMAP-Rule:MF_03178,
ECO:0000269|PubMed:20802492};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=26 uM for NADPH;
KM=12 uM for cytochrome c;
Note=kcat is 0.14 sec(-1) for cytochrome c reduction.;
-!- SUBUNIT: Interacts with DRE2. {ECO:0000255|HAMAP-Rule:MF_03178,
ECO:0000269|PubMed:19194512, ECO:0000269|PubMed:21902732}.
-!- INTERACTION:
P36152:DRE2; NbExp=7; IntAct=EBI-37624, EBI-26482;
O14641:DVL2 (xeno); NbExp=3; IntAct=EBI-37624, EBI-740850;
P48775:TDO2 (xeno); NbExp=3; IntAct=EBI-37624, EBI-743494;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03178,
ECO:0000269|PubMed:19194512}. Mitochondrion {ECO:0000255|HAMAP-
Rule:MF_03178, ECO:0000269|PubMed:19194512}. Note=Relocalizes to
mitochondria after H(2)O(2) exposure. {ECO:0000255|HAMAP-
Rule:MF_03178, ECO:0000269|PubMed:19194512}.
-!- SIMILARITY: Belongs to the NADPH-dependent diflavin oxidoreductase
NDOR1 family. {ECO:0000255|HAMAP-Rule:MF_03178}.
-!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
family. {ECO:0000255|HAMAP-Rule:MF_03178}.
-!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
pyridine nucleotide cytochrome reductase family.
{ECO:0000255|HAMAP-Rule:MF_03178}.
-----------------------------------------------------------------------
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EMBL; Z71255; CAA94995.1; -; Genomic_DNA.
EMBL; Z49219; CAA89168.1; -; Genomic_DNA.
EMBL; BK006949; DAA11472.1; -; Genomic_DNA.
PIR; S54072; S54072.
RefSeq; NP_015373.1; NM_001184145.1.
ProteinModelPortal; Q12181; -.
SMR; Q12181; -.
BioGrid; 36224; 148.
ComplexPortal; CPX-386; TAH18-DRE2 complex.
DIP; DIP-1688N; -.
IntAct; Q12181; 9.
MINT; Q12181; -.
STRING; 4932.YPR048W; -.
MaxQB; Q12181; -.
PaxDb; Q12181; -.
PRIDE; Q12181; -.
EnsemblFungi; YPR048W; YPR048W; YPR048W.
GeneID; 856161; -.
KEGG; sce:YPR048W; -.
EuPathDB; FungiDB:YPR048W; -.
SGD; S000006252; TAH18.
GeneTree; ENSGT00920000149089; -.
HOGENOM; HOG000173033; -.
InParanoid; Q12181; -.
OMA; GPSHFQD; -.
OrthoDB; EOG092C1RRH; -.
BioCyc; YEAST:G3O-34203-MONOMER; -.
Reactome; R-SCE-2564818; Cytosolic iron-sulfur cluster assembly (yeast).
PRO; PR:Q12181; -.
Proteomes; UP000002311; Chromosome XVI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:SGD.
GO; GO:0010181; F:FMN binding; IEA:InterPro.
GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:InterPro.
GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IDA:SGD.
GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:SGD.
GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:SGD.
GO; GO:0055114; P:oxidation-reduction process; IDA:SGD.
GO; GO:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; IMP:SGD.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:SGD.
Gene3D; 1.20.990.10; -; 1.
Gene3D; 3.40.50.360; -; 1.
Gene3D; 3.40.50.80; -; 1.
HAMAP; MF_03178; NDOR1; 1.
InterPro; IPR003097; FAD-binding_1.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR001094; Flavdoxin-like.
InterPro; IPR008254; Flavodoxin/NO_synth.
InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
InterPro; IPR029039; Flavoprotein-like_sf.
InterPro; IPR039261; FNR_nucleotide_bd.
InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
InterPro; IPR028879; NDOR1.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00667; FAD_binding_1; 1.
Pfam; PF00258; Flavodoxin_1; 1.
Pfam; PF00175; NAD_binding_1; 1.
PRINTS; PR00369; FLAVODOXIN.
PRINTS; PR00371; FPNCR.
SUPFAM; SSF52218; SSF52218; 1.
SUPFAM; SSF52343; SSF52343; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; FAD; Flavoprotein; FMN; Mitochondrion;
NADP; Oxidoreductase; Reference proteome.
CHAIN 1 623 NADPH-dependent diflavin oxidoreductase
1.
/FTId=PRO_0000167624.
DOMAIN 7 168 Flavodoxin-like. {ECO:0000255|HAMAP-
Rule:MF_03178}.
DOMAIN 224 491 FAD-binding FR-type. {ECO:0000255|HAMAP-
Rule:MF_03178}.
NP_BIND 13 18 FMN. {ECO:0000255|HAMAP-Rule:MF_03178}.
NP_BIND 60 63 FMN. {ECO:0000255|HAMAP-Rule:MF_03178}.
NP_BIND 106 115 FMN. {ECO:0000255|HAMAP-Rule:MF_03178}.
NP_BIND 413 416 FAD. {ECO:0000255|HAMAP-Rule:MF_03178}.
NP_BIND 445 448 FAD. {ECO:0000255|HAMAP-Rule:MF_03178}.
NP_BIND 538 539 NADP. {ECO:0000255|HAMAP-Rule:MF_03178}.
BINDING 142 142 FMN. {ECO:0000255|HAMAP-Rule:MF_03178}.
BINDING 383 383 FAD. {ECO:0000255|HAMAP-Rule:MF_03178}.
BINDING 623 623 FAD. {ECO:0000255|HAMAP-Rule:MF_03178}.
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


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