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