Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NADPH-dependent diflavin oxidoreductase 1

Gene

tah18

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 annotation

Cofactori

Protein has several cofactor binding sites:
  • FADUniRule annotation
  • FMNUniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei132 – 1321FMNUniRule annotation
Binding sitei343 – 3431FADUniRule annotation
Binding sitei448 – 4481NADPUniRule annotation
Binding sitei584 – 5841FADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 176FMNUniRule annotation
Nucleotide bindingi59 – 624FMNUniRule annotation
Nucleotide bindingi97 – 10610FMNUniRule annotation
Nucleotide bindingi373 – 3764FADUniRule annotation
Nucleotide bindingi407 – 4104FADUniRule annotation
Nucleotide bindingi503 – 5042NADPUniRule annotation
Nucleotide bindingi509 – 5135NADPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, FMN, NADP

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
ORF Names:SPAC1296.06
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1296.06.
PomBaseiSPAC1296.06. tah18.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Mitochondrion UniRule annotation

  • Note: Relocalizes to mitochondria after H2O2 exposure.UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 584584NADPH-dependent diflavin oxidoreductase 1PRO_0000167621Add
BLAST

Proteomic databases

MaxQBiO94613.

PTM databases

SwissPalmiO94613.

Interactioni

Subunit structurei

Interacts with dre2.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliO94613.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 150145Flavodoxin-likeUniRule annotationAdd
BLAST
Domaini199 – 436238FAD-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

HOGENOMiHOG000173033.
InParanoidiO94613.
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.

O94613-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNSHIYILY GSETGTAEGL AESLFRSLTR MGYDVLVNSM DDFNLENLLR
60 70 80 90 100
PLQCVFICST TGQGEMPLNM RKFWRFLLRK KLPNTFLNDM QYAVFGCGDT
110 120 130 140 150
SYTRFNWASK KLDSRLRQLG AQSFSSRGEG DEQHPDGVEG VFAYWCNHLY
160 170 180 190 200
SQLAAIKTPS RPAFGEFDLL PPSFQIIIDE SLGCKVKGFE DNNIVRHSRG
210 220 230 240 250
KIEATLVHNK RISNIKHWQD VRHLAFKIPN FERWKPGDVA VLYPWNDDMS
260 270 280 290 300
VNSFIECMGW ESIKYSPLII SSNVAERKLP WFPNILNVFN LVKYVLSIHS
310 320 330 340 350
VPSRTFFEMA SHFSNNKMHK ERLQEFSSYK NIDDYYDYTT RPRRTVLETL
360 370 380 390 400
QEFKSVQIPI EYALDAFPVI RGRQYSIANR CDNSTGILEL AVALVKYQTI
410 420 430 440 450
LKSPRQGICS RWICDLHENT SFNIDILPGF LNLSYQSNKP LIMVGPGTGV
460 470 480 490 500
APLRALIQER IYNGLKENLL FFGCRNKSMD FLFEKDWEKY TEEGTLKLFC
510 520 530 540 550
AFSRDQEKKK YVQHSIQENG ELVYNLLNEK DGMFFVSGSS GKMPSSVKDA
560 570 580
IAGIVSKYSG CSISDGYSFV TSLEKKNRYY QETW
Length:584
Mass (Da):67,267
Last modified:February 22, 2012 - v2
Checksum:iF17B3435111A703D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB36512.3.
PIRiT37567.
RefSeqiNP_593046.2. NM_001018445.2.

Genome annotation databases

EnsemblFungiiSPAC1296.06.1; SPAC1296.06.1:pep; SPAC1296.06.
GeneIDi2542966.
KEGGispo:SPAC1296.06.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB36512.3.
PIRiT37567.
RefSeqiNP_593046.2. NM_001018445.2.

3D structure databases

ProteinModelPortaliO94613.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

SwissPalmiO94613.

Proteomic databases

MaxQBiO94613.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1296.06.1; SPAC1296.06.1:pep; SPAC1296.06.
GeneIDi2542966.
KEGGispo:SPAC1296.06.

Organism-specific databases

EuPathDBiFungiDB:SPAC1296.06.
PomBaseiSPAC1296.06. tah18.

Phylogenomic databases

HOGENOMiHOG000173033.
InParanoidiO94613.
OMAiAIPPDYL.
OrthoDBiEOG744TKC.

Miscellaneous databases

NextBioi20804001.
PROiO94613.

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 genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Comparative functional genomics of the fission yeasts."
    Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
    , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
    Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL.

Entry informationi

Entry nameiNDOR1_SCHPO
AccessioniPrimary (citable) accession number: O94613
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: February 22, 2012
Last modified: February 17, 2016
This is version 104 of the entry and version 2 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.