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NDOR1_CRYNB
ID   NDOR1_CRYNB             Reviewed;         617 AA.
AC   P0CP13; Q55RG0; Q5KER0;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 46.
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=TAH18 {ECO:0000255|HAMAP-Rule:MF_03178}; OrderedLocusNames=CNBF0310;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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: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 DRE2; as part of the cytosolic iron-sulfur (Fe-
CC       S) protein assembly (CIA) machinery. {ECO:0000255|HAMAP-Rule:MF_03178}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03178}.
CC       Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03178}. Note=Relocalizes to
CC       mitochondria after H(2)O(2) exposure. {ECO:0000255|HAMAP-
CC       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; AAEY01000030; EAL20219.1; -; Genomic_DNA.
DR   RefSeq; XP_774866.1; XM_769773.1.
DR   AlphaFoldDB; P0CP13; -.
DR   SMR; P0CP13; -.
DR   EnsemblFungi; AAW44330; AAW44330; CNF04590.
DR   EnsemblFungi; EAL20219; EAL20219; CNBF0310.
DR   GeneID; 4936583; -.
DR   KEGG; cnb:CNBF0310; -.
DR   VEuPathDB; FungiDB:CNBF0310; -.
DR   HOGENOM; CLU_001570_17_6_1; -.
DR   Proteomes; UP000001435; Chromosome 6.
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; 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   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; FMN; Mitochondrion; NADP; Oxidoreductase.
FT   CHAIN           1..617
FT                   /note="NADPH-dependent diflavin oxidoreductase 1"
FT                   /id="PRO_0000410163"
FT   DOMAIN          3..147
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT   DOMAIN          226..465
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT   BINDING         9..14
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT   BINDING         56..59
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT   BINDING         94..103
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT   BINDING         129
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT   BINDING         404..407
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT   BINDING         438..441
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT   BINDING         479
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT   BINDING         534..535
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT   BINDING         540..544
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT   BINDING         617
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
SQ   SEQUENCE   617 AA;  70183 MW;  9EDFA8A25A9D5795 CRC64;
     MIPMILYASE TGNAQDTAER VARAFRANGR AVTCLPMDQF PISALPHTYL LILLTSTHGR
     GDPPPAMLPL WTALLRSSLP EDILEDVHFA LFGLGDSSYE RFCYAGKMLL RRMEQLGATK
     MGEPAWGDER SPNGIEDAFL PWLQQTLDLY LPYLPLISPT PKIIESTVLP PPIYKISPAS
     TSKSVEHDLS LERLSISFPI PNGKPAPVRV EDQARDKAST SRTKPDDWVW ATLKKNIRLT
     SKDWWQDVRE IELEFDDPDT KPYTAGSICS LQPQSREDDV NMFLEMMELT SQADEVVTIE
     SLLDEQPLPS HLPPAGTPTT LRSLLTNHLD IRYSPRKSFF EWLRRLSTNE MERERLDEFI
     SDPDEIHTYA TRPSRTIVET LADFRFTRIP MSHILEILPP LRRRQFSIAS SWEDHPGKVQ
     LLVALIEYKT NLKIPRKGLC SSWLNGLPVG TRIPIHIASP TLFLPQDPEV PIILVGPGTG
     VAPMRAFVEI RVRQGAAKNT SLYFGCRSST TDYFFESEWD VHREKGVKIQ VAASRDQEER
     IYVQHLIKRD KEYVKEWIVD KKGWLFISGS SNAMPREVRE AVAWCISKEG AGDMTEEESK
     AYVEQMFEDK RGGEESW
 
 
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