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Database: UniProt
Entry: I3M3R8_ICTTR
LinkDB: I3M3R8_ICTTR
Original site: I3M3R8_ICTTR 
ID   I3M3R8_ICTTR            Unreviewed;       597 AA.
AC   I3M3R8;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   08-NOV-2023, entry version 70.
DE   RecName: Full=NADPH-dependent diflavin oxidoreductase 1 {ECO:0000256|HAMAP-Rule:MF_03178};
DE            EC=1.18.1.- {ECO:0000256|HAMAP-Rule:MF_03178};
DE   AltName: Full=NADPH-dependent FMN and FAD-containing oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03178};
GN   Name=NDOR1 {ECO:0000256|HAMAP-Rule:MF_03178,
GN   ECO:0000313|Ensembl:ENSSTOP00000003759.3};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000003759.3, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000003759.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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:0000256|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:0000256|HAMAP-Rule:MF_03178};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|HAMAP-Rule:MF_03178};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917,
CC         ECO:0000256|HAMAP-Rule:MF_03178};
CC   -!- SUBUNIT: Interacts with CIAPIN1; as part of the cytosolic iron-sulfur
CC       (Fe-S) protein assembly (CIA) machinery. {ECO:0000256|HAMAP-
CC       Rule:MF_03178}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000256|HAMAP-
CC       Rule:MF_03178}. Note=Concentrated in perinuclear structure.
CC       {ECO:0000256|HAMAP-Rule:MF_03178}.
CC   -!- SIMILARITY: Belongs to the NADPH-dependent diflavin oxidoreductase
CC       NDOR1 family. {ECO:0000256|HAMAP-Rule:MF_03178}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family. {ECO:0000256|HAMAP-
CC       Rule:MF_03178}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC       family. {ECO:0000256|HAMAP-Rule:MF_03178}.
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DR   EMBL; AGTP01090693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005336941.1; XM_005336884.2.
DR   AlphaFoldDB; I3M3R8; -.
DR   STRING; 43179.ENSSTOP00000003759; -.
DR   Ensembl; ENSSTOT00000004185.3; ENSSTOP00000003759.3; ENSSTOG00000004178.3.
DR   GeneID; 101974598; -.
DR   CTD; 27158; -.
DR   eggNOG; KOG1159; Eukaryota.
DR   GeneTree; ENSGT00930000151050; -.
DR   HOGENOM; CLU_001570_17_6_1; -.
DR   InParanoid; I3M3R8; -.
DR   OrthoDB; 276396at2759; -.
DR   TreeFam; TF105716; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0071949; F:FAD binding; IEA:Ensembl.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070402; F:NADPH binding; IEA:Ensembl.
DR   GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:Ensembl.
DR   GO; GO:0016731; F:oxidoreductase activity, acting on iron-sulfur proteins as donors, NAD or NADP as acceptor; IEA:Ensembl.
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   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03178};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_03178};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_03178};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_03178};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_03178};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_03178}; Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT   DOMAIN          6..150
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          206..447
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         12..17
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT   BINDING         59..62
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT   BINDING         97..106
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT   BINDING         132
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT   BINDING         350
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT   BINDING         382..385
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT   BINDING         416..419
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT   BINDING         460
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT   BINDING         515..516
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT   BINDING         521..525
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT   BINDING         558
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT   BINDING         596
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
SQ   SEQUENCE   597 AA;  66722 MW;  8B39DE1D0ECB17E2 CRC64;
     MTAPQLLVLF GSQTGTAQDV AERLGREARR RRLGCRVQAL DSYAVANLIR EPLVVFVCAT
     TGQGDPPDNM KNFWRFIFRK NLPSTSLCQM DFAVLGLGDS SYARFNFVAK KLHRRLLQLG
     ASALLPICLG DDQHELGPDA IIDPWLGDLW EKVLELYPVP IDLPVIPHGV PLPSKFTLQF
     LLEAPNPSSK ESCLAISDSL GPPSESQPFL APMVTNQRVT GPSHFQDVRL IEFDITDSGI
     SFAAGDVVLI QPSNSAAHTQ QFCHVLGLDP SQCFVLQPRE PDVPCPPGLP QPCSVWQLVS
     QYLDIASVPR RSFFELLACL SPHELEREKL LELSSAQGQE DLCEYCSRPR RTILEVLCDF
     PHTAGAIPPD YLLDLIPQIR PRAFSIASSL LVHPKKLQIL VAVVQYRTRL KEPRRGLCSS
     WLASLDPEKG PVQVPLWVRP GGLAFPETPD TPVIMVGPGT GVAPFRAAVQ ERVAQGQTGN
     FLFFGCRWRD QDFYWGDEWQ ELEKRGCLTL VTAFSREQGR KVYVQHRLRE LGPLVWELLD
     RRGAYFYLAG NAKYMPTDVT EALMSIFQEE GGLSHPNAAT YLARLQRTLR FQTETWA
//
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