NDOR1_DANRE
ID NDOR1_DANRE Reviewed; 595 AA.
AC Q6PFP6; Q5RL12;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=ndor1 {ECO:0000255|HAMAP-Rule:MF_03178};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
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 ciapin1, another key component of the CIA
CC machinery. In turn, this reduced cluster provides electrons for
CC assembly of cytosolic iron-sulfur cluster proteins. It can also reduce
CC the [2Fe-2S] cluster of cisd1 and activate this protein implicated in
CC Fe/S cluster repair. {ECO:0000255|HAMAP-Rule:MF_03178}.
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 ciapin1; as part of the cytosolic iron-sulfur
CC (Fe-S) protein assembly (CIA) machinery. {ECO:0000255|HAMAP-
CC Rule:MF_03178}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000255|HAMAP-
CC Rule:MF_03178}. Note=Concentrated in perinuclear structure.
CC {ECO:0000255|HAMAP-Rule:MF_03178}.
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}.
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DR EMBL; BC049440; AAH49440.1; -; mRNA.
DR EMBL; BC057471; AAH57471.1; -; mRNA.
DR RefSeq; NP_956942.1; NM_200648.1.
DR AlphaFoldDB; Q6PFP6; -.
DR SMR; Q6PFP6; -.
DR STRING; 7955.ENSDARP00000031709; -.
DR PaxDb; Q6PFP6; -.
DR GeneID; 393621; -.
DR KEGG; dre:393621; -.
DR CTD; 27158; -.
DR ZFIN; ZDB-GENE-040426-1555; ndor1.
DR eggNOG; KOG1159; Eukaryota.
DR InParanoid; Q6PFP6; -.
DR OrthoDB; 318396at2759; -.
DR PhylomeDB; Q6PFP6; -.
DR PRO; PR:Q6PFP6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; ISS: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:0016731; F:oxidoreductase activity, acting on iron-sulfur proteins as donors, NAD or NADP as acceptor; ISS:UniProtKB.
DR GO; GO:0016653; F:oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor; ISS:UniProtKB.
DR GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR GO; GO:0036245; P:cellular response to menadione; ISS: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 2: Evidence at transcript level;
KW Cytoplasm; FAD; Flavoprotein; FMN; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..595
FT /note="NADPH-dependent diflavin oxidoreductase 1"
FT /id="PRO_0000319541"
FT DOMAIN 6..150
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT DOMAIN 204..444
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 12..17
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 59..62
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 97..106
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 132
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 348
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 380..383
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 414..417
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 458
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 513..514
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 519..523
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 594
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT CONFLICT 46
FT /note="V -> A (in Ref. 1; AAH49440)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="P -> S (in Ref. 1; AAH49440)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="T -> I (in Ref. 1; AAH49440)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="R -> C (in Ref. 1; AAH49440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 66890 MW; 106DEEB1D47EB28D CRC64;
MSGHTVLVLY GSQTGTAQDT AERIGRQAQR RRLRVKVEAL DTYNVVNLIS ESLVVFVCAT
TGQGDPPDNM KKFWRFLFRK SLPADSLSRL DCAVLGLGDS SYPKFNFVAK KLHKRLLQLG
ANMLLPVGLA DDQHDLGPDG VIDPWLLSFW QKTLSLYPPP AGLAPLREED KLPPRYIFHF
LSEVPNKLTE HLQTVDNKSS PTPLRPFPAP LVFNQRVTHT AHFQDVRHIE FDITGSNIEF
SAGDTVMMRP CNTSEDVEQL CQLLKLDPES YFTLTPTDSS TEVPARLPQP CSIRFLLEHF
LDISAVPRRS FFELLATFAT DELEQEKLLE FSSAAGQDTL HSYCNRPRRT ALEVLTDFPH
TTAELSIGRL LDLFPEIQPR SFSIASSLLE HPNRIQILLA VVKYKTMLVK PRKGLCSSWL
ASLDPSKGDV YVPLWVKKGS LKFPQDPESP VIMVGPGTGV APFRSAIQER VAQGKMANVL
FFGCRSESKD FYCGSEWQEK VQAGQMILVT AFSRDQEDKV YVQHRVKEQG KLLWDLIAKK
NAFFYIAGNA KQMPTSVCDA LKAVFQKEGG MSENQAQEML DGMEKNGRFQ SETWS
