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Protein

NADPH-dependent diflavin oxidoreductase 1

Gene

TAH18

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 H2O(2)-induced cell death.UniRule annotation4 Publications

Cofactori

Protein has several cofactor binding sites:
  • FADUniRule annotation1 Publication
  • FMNUniRule annotation1 Publication

Kineticsi

kcat is 0.14 sec(-1) for cytochrome c reduction.

  1. KM=26 µM for NADPH
  2. KM=12 µM for cytochrome c

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei142 – 1421FMNUniRule annotation
    Binding sitei383 – 3831FADUniRule annotation
    Binding sitei623 – 6231FADUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 186FMNUniRule annotation
    Nucleotide bindingi60 – 634FMNUniRule annotation
    Nucleotide bindingi106 – 11510FMNUniRule annotation
    Nucleotide bindingi413 – 4164FADUniRule annotation
    Nucleotide bindingi445 – 4484FADUniRule annotation
    Nucleotide bindingi538 – 5392NADPUniRule annotation

    GO - Molecular functioni

    GO - Biological processi

    • iron-sulfur cluster assembly Source: SGD
    • nitric oxide biosynthetic process Source: SGD
    • oxidation-reduction process Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, FMN, NADP

    Enzyme and pathway databases

    BioCyciYEAST:G3O-34203-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH-dependent diflavin oxidoreductase 1UniRule annotation (EC:1.18.1.-UniRule annotation)
    Alternative name(s):
    NADPH-dependent FMN and FAD-containing oxidoreductaseUniRule annotation
    Gene namesi
    Name:TAH18UniRule annotation
    Ordered Locus Names:YPR048W
    ORF Names:YP9499.06
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome XVI

    Organism-specific databases

    EuPathDBiFungiDB:YPR048W.
    SGDiS000006252. TAH18.

    Subcellular locationi

    • Cytoplasm UniRule annotation1 Publication
    • Mitochondrion UniRule annotation1 Publication

    • Note: Relocalizes to mitochondria after H2O2 exposure.UniRule annotation1 Publication

    GO - Cellular componenti

    • cytosol Source: Reactome
    • mitochondrion Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 623623NADPH-dependent diflavin oxidoreductase 1PRO_0000167624Add
    BLAST

    Proteomic databases

    MaxQBiQ12181.
    PeptideAtlasiQ12181.

    Interactioni

    Subunit structurei

    Interacts with DRE2.UniRule annotation2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DRE2P361523EBI-37624,EBI-26482

    Protein-protein interaction databases

    BioGridi36224. 18 interactions.
    DIPiDIP-1688N.
    IntActiQ12181. 7 interactions.
    MINTiMINT-389084.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12181.
    SMRiQ12181. Positions 3-623.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 168162Flavodoxin-likeUniRule annotationAdd
    BLAST
    Domaini224 – 491268FAD-binding FR-typeUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the NADPH-dependent diflavin oxidoreductase NDOR1 family.UniRule annotation
    In the N-terminal section; belongs to the flavodoxin family.UniRule annotation
    In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.UniRule annotation
    Contains 1 FAD-binding FR-type domain.UniRule annotation
    Contains 1 flavodoxin-like domain.UniRule annotation

    Phylogenomic databases

    GeneTreeiENSGT00840000129757.
    HOGENOMiHOG000173033.
    InParanoidiQ12181.
    OMAiAIPPDYL.
    OrthoDBiEOG744TKC.

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    HAMAPiMF_03178. NDOR1.
    InterProiIPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001094. Flavdoxin-like.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like_dom.
    IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
    IPR028879. NDOR1.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00667. FAD_binding_1. 1 hit.
    PF00258. Flavodoxin_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view]
    PRINTSiPR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SUPFAMiSSF52218. SSF52218. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEiPS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q12181-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSSSKKIVIL YGSETGNAHD FATILSHRLH RWHFSHTFCS IGDYDPQDIL
    60 70 80 90 100
    KCRYLFIICS TTGQGELPRN VNALKGERPV TFWSFLKRKN LPSNLLNHIQ
    110 120 130 140 150
    TAMLGLGDSS YPKFNYGIRK LHQRIVTQLG ANELFDRLEA DDQAMAGSNK
    160 170 180 190 200
    GTGLGIESVY FEYEKKVLSF LLSKYPNRKV NGQIIKREEL DPEVYLEPAS
    210 220 230 240 250
    YLQLSDEHAN EKFTSTKVIF EGDESLKVGR VNINKRITSE GHFQDVRQFK
    260 270 280 290 300
    FSNVDKIQEN YEPGDTVTIY PCNTDEDVSR FLANQSHWLE IADKPLNFTS
    310 320 330 340 350
    GVPNDLKDGG LVRPMTLRNL LKYHCDFMSI PRTSFFLKIW TFATDVTKME
    360 370 380 390 400
    RGQEQLNDQR EKLRQFATDQ DMQDLYDYCN RPRRSILEVL EDFISVKLPW
    410 420 430 440 450
    KYVLDYLPII KPRYYSISSG PGDPNIELTV AIVKYKTILR KIRRGICTNY
    460 470 480 490 500
    IARLQEGEQI RYKLQNNHII KKEFLNKPMI LVGPGVGLAP LLSVVKAEIS
    510 520 530 540 550
    KDIKLLFGCR YKDKDYIYKD MLEDWFRKGK IALHSSFSRD EENSPGVKYV
    560 570 580 590 600
    QDYLWRLGEE ITNLVVNKDA VFFLCGSSGK MPIQVRLTFI EMLKKWGNFS
    610 620
    DEETAKKYLK EMEKSDRYIQ ETW
    Length:623
    Mass (Da):72,328
    Last modified:November 1, 1996 - v1
    Checksum:i5248B9512F77D628
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z71255 Genomic DNA. Translation: CAA94995.1.
    Z49219 Genomic DNA. Translation: CAA89168.1.
    BK006949 Genomic DNA. Translation: DAA11472.1.
    PIRiS54072.
    RefSeqiNP_015373.1. NM_001184145.1.

    Genome annotation databases

    EnsemblFungiiYPR048W; YPR048W; YPR048W.
    GeneIDi856161.
    KEGGisce:YPR048W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z71255 Genomic DNA. Translation: CAA94995.1.
    Z49219 Genomic DNA. Translation: CAA89168.1.
    BK006949 Genomic DNA. Translation: DAA11472.1.
    PIRiS54072.
    RefSeqiNP_015373.1. NM_001184145.1.

    3D structure databases

    ProteinModelPortaliQ12181.
    SMRiQ12181. Positions 3-623.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi36224. 18 interactions.
    DIPiDIP-1688N.
    IntActiQ12181. 7 interactions.
    MINTiMINT-389084.

    Proteomic databases

    MaxQBiQ12181.
    PeptideAtlasiQ12181.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYPR048W; YPR048W; YPR048W.
    GeneIDi856161.
    KEGGisce:YPR048W.

    Organism-specific databases

    EuPathDBiFungiDB:YPR048W.
    SGDiS000006252. TAH18.

    Phylogenomic databases

    GeneTreeiENSGT00840000129757.
    HOGENOMiHOG000173033.
    InParanoidiQ12181.
    OMAiAIPPDYL.
    OrthoDBiEOG744TKC.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-34203-MONOMER.

    Miscellaneous databases

    NextBioi981304.
    PROiQ12181.

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    HAMAPiMF_03178. NDOR1.
    InterProiIPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001094. Flavdoxin-like.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like_dom.
    IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
    IPR028879. NDOR1.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00667. FAD_binding_1. 1 hit.
    PF00258. Flavodoxin_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view]
    PRINTSiPR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SUPFAMiSSF52218. SSF52218. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEiPS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
      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.
      Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Characterization of mutations that are synthetic lethal with pol3-13, a mutated allele of DNA polymerase delta in Saccharomyces cerevisiae."
      Chanet R., Heude M.
      Curr. Genet. 43:337-350(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "A newly identified essential complex, Dre2-Tah18, controls mitochondria integrity and cell death after oxidative stress in yeast."
      Vernis L., Facca C., Delagoutte E., Soler N., Chanet R., Guiard B., Faye G., Baldacci G.
      PLoS ONE 4:E4376-E4376(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APOPTOSIS, INTERACTION WITH DRE2, SUBCELLULAR LOCATION.
    5. "Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein biogenesis."
      Netz D.J., Stumpfig M., Dore C., Muhlenhoff U., Pierik A.J., Lill R.
      Nat. Chem. Biol. 6:758-765(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR.
    6. "Interaction between the reductase Tah18 and highly conserved Fe-S containing Dre2 C-terminus is essential for yeast viability."
      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.
      Mol. Microbiol. 82:54-67(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DRE2.

    Entry informationi

    Entry nameiNDOR1_YEAST
    AccessioniPrimary (citable) accession number: Q12181
    Secondary accession number(s): D6W456
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: November 1, 1996
    Last modified: May 11, 2016
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.