(data stored in ACNUC7421 zone)

SWISSPROT: Q75BR9_ASHGO

ID   Q75BR9_ASHGO            Unreviewed;       497 AA.
AC   Q75BR9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 123.
DE   RecName: Full=NADPH:adrenodoxin oxidoreductase, mitochondrial {ECO:0000256|PIRNR:PIRNR000362};
DE            EC=1.18.1.6 {ECO:0000256|PIRNR:PIRNR000362};
GN   ORFNames=AGOS_ACR202W {ECO:0000313|EMBL:AAS51428.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51428.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51428.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADP(+) + 2 reduced [adrenodoxin] = NADPH + 2 oxidized
CC         [adrenodoxin]; Xref=Rhea:RHEA:42312, Rhea:RHEA-COMP:9998, Rhea:RHEA-
CC         COMP:9999, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.18.1.6;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000362};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000362,
CC         ECO:0000256|PIRSR:PIRSR000362-1};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|PIRNR:PIRNR000362}.
CC   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC       {ECO:0000256|PIRNR:PIRNR000362}.
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DR   EMBL; AE016816; AAS51428.2; -; Genomic_DNA.
DR   RefSeq; NP_983604.2; NM_208957.2.
DR   STRING; 33169.AAS51428; -.
DR   EnsemblFungi; AAS51428; AAS51428; AGOS_ACR202W.
DR   GeneID; 4619736; -.
DR   KEGG; ago:AGOS_ACR202W; -.
DR   HOGENOM; HOG000249250; -.
DR   InParanoid; Q75BR9; -.
DR   KO; K18914; -.
DR   OMA; RFNFIGN; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:EnsemblFungi.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IEA:EnsemblFungi.
DR   GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:EnsemblFungi.
DR   GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:EnsemblFungi.
DR   GO; GO:0015039; F:NADPH-adrenodoxin reductase activity; IBA:GO_Central.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR021163; Ferredox_Rdtase_adrenod.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PIRSF; PIRSF000362; FNR; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75BR9.
DR   SWISS-2DPAGE; Q75BR9.
KW   FAD {ECO:0000256|PIRNR:PIRNR000362, ECO:0000256|PIRSR:PIRSR000362-1};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR000362};
KW   Mitochondrion {ECO:0000256|PIRNR:PIRNR000362};
KW   NADP {ECO:0000256|PIRNR:PIRNR000362, ECO:0000256|PIRSR:PIRSR000362-2};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000362};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          21..244
FT                   /note="Pyr_redox_2"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   NP_BIND         182..185
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT   NP_BIND         228..229
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT   NP_BIND         417..419
FT                   /note="FAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         30
FT                   /note="FAD; via amide nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         52
FT                   /note="FAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         60
FT                   /note="FAD; via amide nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         105
FT                   /note="FAD; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         240
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT   BINDING         410
FT                   /note="FAD; via amide nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         417
FT                   /note="NADP; via amide nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
SQ   SEQUENCE   497 AA;  55107 MW;  66F7784CBF731353 CRC64;
     MGLATIIARR AYGQCGRARK RVSIVGSGPS GFYTAVHLLT RATEPLHVTL WESLPTPFGL
     SRYGVAPDHP EVKNCEDRFT ELANRYHVAA QPGEHSFEFV GNITVGRDVA LRELLAAEDA
     VVLSYGCSGD RRLGIEGEAD TAGVFTSRQF VNWYNGHPRH AQDAALSGFD WARVRRVGII
     GNGNVALDIA RLLLTAREEA LWGQTDINPH ALQALRRAPL EEVRLIGRRD FLGSKFTNKE
     LREMWELERC GVRGHIAPEH FTPEAWAALP LDRATKRRID MCQQYLLPYA ARGSKSASKY
     PPPAEGYSKA WVSDYLKTPL YIRRDGAGAI SALTVCKNSL TPENKVVRHL DEQLDYELDV
     LITSLGYRGQ PLPEFGALGV AFDADRVSNS RGRVLRQDGS LIPGLFASGW IANGSRGVIM
     TTMMNSFAVG DEVLQYLAQS PPKDHSHGID LRDSTHTTWA DWIQIDKTEK QRAARGQPRQ
     KLLSVAQMLE AARARDT
//

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