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Database: UniProt
Entry: A0A167IBP2_CALVF
LinkDB: A0A167IBP2_CALVF
Original site: A0A167IBP2_CALVF 
ID   A0A167IBP2_CALVF        Unreviewed;       587 AA.
AC   A0A167IBP2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-FEB-2023, entry version 23.
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=TAH18 {ECO:0000256|HAMAP-Rule:MF_03178};
GN   ORFNames=CALVIDRAFT_487509 {ECO:0000313|EMBL:KZO92486.1};
OS   Calocera viscosa (strain TUFC12733).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO92486.1, ECO:0000313|Proteomes:UP000076738};
RN   [1] {ECO:0000313|EMBL:KZO92486.1, ECO:0000313|Proteomes:UP000076738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO92486.1,
RC   ECO:0000313|Proteomes:UP000076738};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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 DRE2, another key component of the CIA
CC       machinery. In turn, this reduced cluster provides electrons for
CC       assembly of cytosolic iron-sulfur cluster proteins. Positively controls
CC       H(2)O(2)-induced cell death. {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 DRE2; as part of the cytosolic iron-sulfur (Fe-
CC       S) protein assembly (CIA) machinery. {ECO:0000256|HAMAP-Rule:MF_03178}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03178}.
CC       Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03178}. Note=Relocalizes to
CC       mitochondria after H(2)O(2) exposure. {ECO:0000256|HAMAP-
CC       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; KV417310; KZO92486.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A167IBP2; -.
DR   STRING; 1330018.A0A167IBP2; -.
DR   OrthoDB; 276396at2759; -.
DR   Proteomes; UP000076738; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; 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   Mitochondrion {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:UP000076738}.
FT   DOMAIN          6..150
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          196..435
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         344
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT   BINDING         374..377
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT   BINDING         408..411
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT   BINDING         449
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT   BINDING         505..506
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT   BINDING         511..515
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT   BINDING         586
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
SQ   SEQUENCE   587 AA;  67388 MW;  5485BFD320DA167A CRC64;
     MEQRSLLVLY GSETGNAQDV AERVGRDARR HHFKTRVVAM DAYDIATLIE EPLVIFVCST
     TGQGVEPRNM TKLWKTLLRA DLPADLFDGM DFAVFGLGDS SYARYNWAAK KLQRRLQSLG
     AREIWERGDA DDQHYLGLDG ALDPWIDGLF RVLLVTYPLP LGVSVVPKDY LYPPRVQLEF
     LDGPELPLSE APFSFPGSSP ARLLRMKRLT RPDWYQDVRH IEFEYDKDVS YSPGDIAVLH
     PENDPEEVQR FLQRMGWAET ADKPFRLVPN DQDGLERPLP EYWPEVMTLR IAFTRYLDIL
     GVPRRSFFES LANFTTEEME TEKLREFCSP EGQDDLYAYC HRVRRTIAEV VTEFRSVLIP
     QNYVFDVFPE VRPREFSIAS SVKRHPKQVH LCVAIVQYKT KLKAPRRGVC TSWLTRLREG
     DPVQIAIESG TMHLPPLPST PIILVGPGTG VAPMRSFIED RIYHEKSKEN TLYFGCRSLD
     ADCHFKEEWS SYQDKGQLVC RTAASRDQPK KVYVQNLIIE DAARIWKLVH ENKGYVLVSG
     SSNKMPLAVR HAVEEALTGE GKLTAEDAKE YVKRMEMSGR WQEECWS
//
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