GENTAUR Molecular Products.

 NDOR1_YEAST             Reviewed;         623 AA.
 Q12181; D6W456;
 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
 01-NOV-1996, sequence version 1.
 13-FEB-2019, entry version 149.
 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=3; IntAct=EBI-37624, EBI-26482;
 -!- 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; 149.
 ComplexPortal; CPX-386; TAH18-DRE2 complex.
 DIP; DIP-1688N; -.
 IntAct; Q12181; 7.
 MINT; Q12181; -.
 STRING; 4932.YPR048W; -.
 MaxQB; Q12181; -.
 PaxDb; Q12181; -.
 PRIDE; Q12181; -.
 EnsemblFungi; YPR048W_mRNA; YPR048W_mRNA; YPR048W.
 GeneID; 856161; -.
 KEGG; sce:YPR048W; -.
 EuPathDB; FungiDB:YPR048W; -.
 SGD; S000006252; TAH18.
 GeneTree; ENSGT00930000151050; -.
 HOGENOM; HOG000173033; -.
 InParanoid; Q12181; -.
 OMA; FEMMPLI; -.
 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; IBA:GO_Central.
 GO; GO:0005739; C:mitochondrion; IDA:SGD.
 GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
 GO; GO:0010181; F:FMN binding; IBA:GO_Central.
 GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
 GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:GO_Central.
 GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
 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; CysJ-like_FAD-binding.
 InterPro; IPR017927; FAD-bd_FR_type.
 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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