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REDA_DICDI
ID   REDA_DICDI              Reviewed;         631 AA.
AC   Q54B10; O15702; Q27XC6;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=NADPH oxidoreductase A;
DE            EC=1.6.-.-;
GN   Name=redA; ORFNames=DDB_G0293904;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-614,
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=18218133; DOI=10.1186/1471-213x-8-8;
RA   Gonzalez-Kristeller D.C., Farage L., Fiorini L.C., Loomis W.F.,
RA   da Silva A.M.;
RT   "The P450 oxidoreductase, RedA, controls development beyond the mound stage
RT   in Dictyostelium discoideum.";
RL   BMC Dev. Biol. 8:8-8(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Probable NADPH oxidoreductase that controls development
CC       beyond the mound stage. {ECO:0000269|PubMed:18218133}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC       Note=Binds 1 FMN per subunit. {ECO:0000250};
CC   -!- DEVELOPMENTAL STAGE: Expressed during growth and early development but
CC       then decline, reaching undetectable levels after the mound stage.
CC       {ECO:0000269|PubMed:18218133}.
CC   -!- DISRUPTION PHENOTYPE: Cells develop only to the mound stage and
CC       accumulate a bright yellow pigment. {ECO:0000269|PubMed:18218133}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB70186.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF012946; AAB70186.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; DQ344637; ABC70200.1; -; mRNA.
DR   EMBL; AAFI02000224; EAL60451.1; -; Genomic_DNA.
DR   RefSeq; XP_628906.1; XM_628904.1.
DR   AlphaFoldDB; Q54B10; -.
DR   SMR; Q54B10; -.
DR   STRING; 44689.DDB0215407; -.
DR   PaxDb; Q54B10; -.
DR   PRIDE; Q54B10; -.
DR   EnsemblProtists; EAL60451; EAL60451; DDB_G0293904.
DR   GeneID; 8629523; -.
DR   KEGG; ddi:DDB_G0293904; -.
DR   dictyBase; DDB_G0293904; redA.
DR   eggNOG; KOG1158; Eukaryota.
DR   HOGENOM; CLU_001570_17_7_1; -.
DR   InParanoid; Q54B10; -.
DR   OMA; ARPFFDY; -.
DR   PhylomeDB; Q54B10; -.
DR   PRO; PR:Q54B10; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:dictyBase.
DR   GO; GO:0010181; F:FMN binding; ISS:dictyBase.
DR   GO; GO:0050661; F:NADP binding; ISS:dictyBase.
DR   GO; GO:0003958; F:NADPH-hemoprotein reductase activity; ISS:dictyBase.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR   Gene3D; 1.20.990.10; -; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.40.50.80; -; 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; 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   2: Evidence at transcript level;
KW   Developmental protein; FAD; Flavoprotein; FMN; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..631
FT                   /note="NADPH oxidoreductase A"
FT                   /id="PRO_0000351222"
FT   DOMAIN          73..212
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   DOMAIN          247..480
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         79..83
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   BINDING         160..191
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   BINDING         249..299
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         504..630
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   631 AA;  71146 MW;  04BAA9B6B1D9007B CRC64;
     MKSVILKPKN LVLLGAGVTT TYYLYKFFSA PSVSKDEGDK FGFNAPDPAA LARAAVKEKK
     ERFVKPSDNV CPILILYGTE YGLSAEVAKK LEESINSKLE GFWARIIDME EYEIIEFEKE
     QIVLIITSTY GDGVPPTTAR PFFDYLEANR LNLSHIQFSV LALGDRSYPH YCAAGKTLDK
     QFEEMGAKRF RDRIEVDQED WTCFDRYIDT VCGLVPTLGG VEKREGQDYL YEKAKLFALS
     QGKYNKKKPY SSKLLVKRVL TKGDKVGIHL EFELGDSELK YVPGDALAIL PDNAASEVSA
     IISLLKLSPS FKVSTPGWHY QEGEQPNPSQ ITLTHILTKC FDIHNCKPEL LQLLKDNVKN
     QQEKEKLTNL LAQGTGKSNT QLVEFLENHH LIDILKMFSS ARPPIDDLLA QLAKLLPRYY
     SIASSMSENK LAVSLCVAVV KYDLHGSERV GIASTHMADR MNVGDRVSIF INNNPDFRLP
     EDPTTPILMV GPGTGIAPFV SFIQERKALG HTGENHLYFG CRRSDEDFLY SKELQQYHND
     GLIKLYTAFS RETSQKVYVQ NRLLENSQQI CDLINAGGHI YICGDAKSMA PQVHETLSLI
     ITKHMSIDEA DAQALLHKLE KEKRYQKDVW F
 
 
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