ID A0A0A0AWM2_CHAVO Unreviewed; 596 AA.
AC A0A0A0AWM2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 22-FEB-2023, entry version 25.
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 ORFNames=N301_09834 {ECO:0000313|EMBL:KGL97475.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL97475.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL97475.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL97475.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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: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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03178}.
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DR EMBL; KL872976; KGL97475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0AWM2; -.
DR STRING; 50402.A0A0A0AWM2; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:InterPro.
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:UP000053858}.
FT DOMAIN 6..150
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 205..445
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
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 349
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 381..384
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 415..418
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 459
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 514..515
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 520..524
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 595
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
SQ SEQUENCE 596 AA; 67229 MW; 4F18DF22A6CF5028 CRC64;
MVERKLLILY GRQTGTAQDT AERIGRGAKR RHFQCRVEAL DSYEVANLIN ELLVVFVCAT
TGQGDPPDNM KMFWRFLFRK NLPPGSLCQL DYAVLGLGDS SYPKFNFVAK KLHKRVLQLG
GNPLLPVALG DDQHDLGPDA VVDPWLLALW DKILALYPLP PGLEIISPNV RLPPKYTLHY
LAEDSPHPDG GLLQPTAPRA VPSELRPFAA RMVSNQRVTA ESHFQDVRLI EFDVTGSGIM
FSAGDVVMIQ PQNCPEDVQQ FCQLLRLDPD RCFMLKPTEP GTSLPALLPQ PCTIRYLVTH
YLDISCVPRR SFFELLSYFS TNELEREKLQ EFSSAQGQEE LYSYCNRPRR TTLEALWDFP
HTTCAVPPDY LLDLIPRIRP RAFSIASSML AHPDRIQILM AVVRYKTRLS KPRRGLCSTW
LASLDPEQGD VRVPLWVKKG GMKFPADPDT PVIMIGPGTG VAPFRAAIQE RVAQGRRGNC
LFFGCRQKSK DFYCQAEWEE LVTKGFLTLF TAFSRDQEEK VYVQHCIREN RRLVWELLSG
GSAHVYLAGN AKQMPVAVAE ALQSVLQLEG GLSPSEAEEH LTALERSQRF QSETWS
//
