ID NDOR1_BOVIN Reviewed; 597 AA.
AC Q1JPJ0; G3MXY0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 24-JAN-2024, entry version 99.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-577.
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
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 (By similarity). In vitro can fully activate
CC methionine synthase/MTR in the presence of soluble cytochrome b5/CYB5A
CC (By similarity). {ECO:0000250|UniProtKB:Q9UHB4, ECO:0000255|HAMAP-
CC 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 (By similarity). Interacts with
CC DCPS (By similarity). {ECO:0000250|UniProtKB:Q9UHB4, 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; BT025363; ABF57319.1; -; mRNA.
DR EMBL; DAAA02032411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001039623.2; NM_001046158.2.
DR AlphaFoldDB; Q1JPJ0; -.
DR SMR; Q1JPJ0; -.
DR PaxDb; 9913-ENSBTAP00000054403; -.
DR Ensembl; ENSBTAT00000066145.2; ENSBTAP00000054403.1; ENSBTAG00000047061.2.
DR GeneID; 513873; -.
DR KEGG; bta:513873; -.
DR CTD; 27158; -.
DR VEuPathDB; HostDB:ENSBTAG00000047061; -.
DR VGNC; VGNC:31938; NDOR1.
DR eggNOG; KOG1159; Eukaryota.
DR GeneTree; ENSGT00930000151050; -.
DR HOGENOM; CLU_001570_17_6_1; -.
DR InParanoid; Q1JPJ0; -.
DR OMA; DIMSIPR; -.
DR OrthoDB; 276396at2759; -.
DR TreeFam; TF105716; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000047061; Expressed in laryngeal cartilage and 105 other cell types or tissues.
DR ExpressionAtlas; Q1JPJ0; baseline.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0071949; F:FAD binding; IEA:Ensembl.
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:0070402; F:NADPH binding; IEA:Ensembl.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:Ensembl.
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:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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 PANTHER; PTHR19384:SF10; NADPH-DEPENDENT DIFLAVIN OXIDOREDUCTASE 1; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
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; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 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..597
FT /note="NADPH-dependent diflavin oxidoreductase 1"
FT /id="PRO_0000319538"
FT DOMAIN 6..150
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT DOMAIN 206..446
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 350
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 382..385
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 416..419
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 460
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 515..516
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 521..525
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 558
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 596
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT CONFLICT 331
FT /note="W -> R (in Ref. 1; ABF57319)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="Q -> H (in Ref. 1; ABF57319)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="R -> G (in Ref. 1; ABF57319)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 597 AA; 66568 MW; 01CA1B51157D58E5 CRC64;
MPSARLLVLF GSQTGTAQDV SERLGREARR RQLSCRVEEL DSYPVVNLIN EPLVIFVCAT
TGQGDPPDNM KSFWRFIFRR SLPSTALRQM DFAVLGLGDS SYAKFNFVAK KLHRRLLQLG
GSALLPVCLG DDQHELGPDA AIDPWLQDLW EKVLGPHPVP LNLDLSPPGV LWPSKFTLQF
LKDTPSSGPE ELCAAGTDPQ GPPSELQPFL APMVSNQRVT GPSHFQDVRL IEFDISGSGI
SFAAGDLVLI QPENTASHVQ QFCQALGLDP EQHFTLQPRE PGVTCPTRLP QPCSVRRLVS
QYLDIASVPR RSFFELLACL SPHELEREKL WEFGSARGQE ELCEYCTRPR RTALEVLCDF
PHTAAAVPPD YLLDLLPLIR PRAFSIASSL RAHPSRLQIL VAVVQYQTRL REPRRGLCSS
WLASLDPAQG PVRVPLWVRS GGLTFPKTPD VPVIMVGPGT GVAPFRAAIQ ERVAQGETGN
VLFFGCRRRD QDFYWEAEWE QLQARGCLTL VTAFSREQEQ KVYVQHRLRA LGPLVWELLD
GRGAHFYLAG NAKYMPADVC DTLLSIFREE GGLSDPDAAA YLAQLQRTLR FQTETWA
//
