NDOR1_ARATH
ID NDOR1_ARATH Reviewed; 623 AA.
AC Q6NPS8; A0A1I9LRQ3; Q9SRU4;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
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};
DE AltName: Full=NADPH-dependent FMN and FAD-containing oxidoreductase {ECO:0000255|HAMAP-Rule:MF_03178};
GN Name=ATR3; OrderedLocusNames=At3g02280; ORFNames=F14P3.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INTERACTION WITH AT5G18400, AND DISRUPTION PHENOTYPE.
RX PubMed=20406405; DOI=10.1111/j.1469-8137.2010.03254.x;
RA Varadarajan J., Guilleminot J., Saint-Jore-Dupas C., Piegu B.,
RA Chaboute M.E., Gomord V., Coolbaugh R.C., Devic M., Delorme V.;
RT "ATR3 encodes a diflavin reductase essential for Arabidopsis embryo
RT development.";
RL New Phytol. 187:67-82(2010).
CC -!- FUNCTION: NADPH-dependent reductase which is a central component of the
CC cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery.
CC Transfers electrons from NADPH via its FAD and FMN prosthetic groups to
CC the [2Fe-2S] cluster of the anamorsin/DRE2 homolog, another key
CC component of the CIA machinery. In turn, this reduced cluster provides
CC electrons for assembly of cytosolic iron-sulfur cluster proteins (By
CC similarity). Catalyzes the NADP-dependent reduction of cytochrome c,
CC but not cytochrome P450 in vitro. Required for embryo development
CC (PubMed:20406405). {ECO:0000255|HAMAP-Rule:MF_03178,
CC ECO:0000269|PubMed:20406405}.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67717;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03178};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03178};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03178};
CC -!- SUBUNIT: Interacts with At5g18400. {ECO:0000269|PubMed:20406405}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03178,
CC ECO:0000269|PubMed:20406405}. Nucleus {ECO:0000269|PubMed:20406405}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:20406405}.
CC -!- DEVELOPMENTAL STAGE: Expressed in cell cycle-dependent manner. Most
CC abundant at the G2 and G2/M transition. Lowest expression in S and M
CC phases. {ECO:0000269|PubMed:20406405}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous. Embryo
CC development arrested at 2 to 4-cell stages.
CC {ECO:0000269|PubMed:20406405}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAF02110.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009755; AAF02110.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE73787.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65261.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65262.1; -; Genomic_DNA.
DR EMBL; BT010739; AAR23709.1; -; mRNA.
DR EMBL; AK229452; BAF01311.1; -; mRNA.
DR RefSeq; NP_001327241.1; NM_001337391.1.
DR RefSeq; NP_001327242.1; NM_001337392.1.
DR RefSeq; NP_186877.2; NM_111095.5.
DR AlphaFoldDB; Q6NPS8; -.
DR SMR; Q6NPS8; -.
DR BioGRID; 5751; 1.
DR STRING; 3702.AT3G02280.1; -.
DR PaxDb; Q6NPS8; -.
DR PRIDE; Q6NPS8; -.
DR ProteomicsDB; 251144; -.
DR EnsemblPlants; AT3G02280.1; AT3G02280.1; AT3G02280.
DR EnsemblPlants; AT3G02280.2; AT3G02280.2; AT3G02280.
DR EnsemblPlants; AT3G02280.3; AT3G02280.3; AT3G02280.
DR GeneID; 820417; -.
DR Gramene; AT3G02280.1; AT3G02280.1; AT3G02280.
DR Gramene; AT3G02280.2; AT3G02280.2; AT3G02280.
DR Gramene; AT3G02280.3; AT3G02280.3; AT3G02280.
DR KEGG; ath:AT3G02280; -.
DR Araport; AT3G02280; -.
DR TAIR; locus:2076547; AT3G02280.
DR eggNOG; KOG1159; Eukaryota.
DR HOGENOM; CLU_001570_17_6_1; -.
DR InParanoid; Q6NPS8; -.
DR OMA; QLFEMMP; -.
DR OrthoDB; 318396at2759; -.
DR PhylomeDB; Q6NPS8; -.
DR BioCyc; ARA:AT3G02280-MON; -.
DR PRO; PR:Q6NPS8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q6NPS8; baseline and differential.
DR Genevisible; Q6NPS8; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
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; NADP; Nucleus; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..623
FT /note="NADPH-dependent diflavin oxidoreductase 1"
FT /id="PRO_0000416841"
FT DOMAIN 8..153
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT DOMAIN 221..467
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 14..19
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 62..65
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 135
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 399..402
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 433..436
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 475
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 541..542
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 547..551
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 583
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 622
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
SQ SEQUENCE 623 AA; 70412 MW; 6778218FB5004A95 CRC64;
MGEKQRKLLV LYASQTGNAL DAAERIGREA ERRGLPASVV STDEFDTSSL PHHEEAVVFV
VSTTGQGDSP DSFKAFWRFL LQRNLGNYWL QQVRYAVFGL GDSGYQKYNF VAKKLDKRLS
DLGATTIIEK GLGDDQHPSG YEGTLDPWML SLWRTLYQIN PKYFPKGPDV KIPQDEVIDK
PKYRILFHKQ EKLEPKLLSD SDIIQRARGM SPGKLFKDKS KPDCFLKMTR NEVLTKAEST
KDVRHFEFQF VSSTIEYEVG DVVELLPSQN SSVVDAFIER CGLDPESFIT VGPRETENSS
FSEEMITQIP IKLKTFVELT MDVTSASPRR YFFEIMSFYA TAEHEKERLQ YFASPEGRDD
LYNYNQKERR SILEVLEDFP SVQIPFDWLV QLVPPLKPRA FSISSSPLAH PAAVHLTVSI
VSWITPYKRT RKGLCSSWLA SLAPEQEVNI PVWFHKGSLP APSQSLPLIL VGPGTGCAPF
RGFIAERAVQ AQSSPVAPVM FFFGCRNKDT DFLYRDFWES HAREGGMLSE GKGGGFYTAF
SRDQPKKVYV QHKIREMSKR VWDLLCDGAA VYVAGSSTKM PCDVMSAFED IVSEETGGGS
KEVASRWLKA LEKTGRYNVE AWS
