ID   ALRC_DICDI              Reviewed;         321 AA.
AC   Q55FL3;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Aldose reductase C;
DE            Short=ARC;
DE            EC=1.1.1.21;
DE   AltName: Full=Aldehyde reductase C;
GN   Name=alrC; ORFNames=DDB_G0268058;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
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: Catalyzes the NADPH-dependent reduction of a wide variety of
CC       carbonyl-containing compounds to their corresponding alcohols with a
CC       broad range of catalytic efficiencies. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alditol + NAD(+) = an aldose + H(+) + NADH;
CC         Xref=Rhea:RHEA:12785, Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15693, ChEBI:CHEBI:17522,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.21;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alditol + NADP(+) = an aldose + H(+) + NADPH;
CC         Xref=Rhea:RHEA:12789, Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15693, ChEBI:CHEBI:17522,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.21;
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; AAFI02000003; EAL73482.1; -; Genomic_DNA.
DR   RefSeq; XP_647520.1; XM_642428.1.
DR   AlphaFoldDB; Q55FL3; -.
DR   SMR; Q55FL3; -.
DR   STRING; 44689.DDB0231284; -.
DR   PaxDb; Q55FL3; -.
DR   EnsemblProtists; EAL73482; EAL73482; DDB_G0268058.
DR   GeneID; 8616327; -.
DR   KEGG; ddi:DDB_G0268058; -.
DR   dictyBase; DDB_G0268058; alrC.
DR   eggNOG; KOG1577; Eukaryota.
DR   HOGENOM; CLU_023205_0_0_1; -.
DR   InParanoid; Q55FL3; -.
DR   OMA; WRHPDEP; -.
DR   PhylomeDB; Q55FL3; -.
DR   PRO; PR:Q55FL3; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0043795; F:glyceraldehyde oxidoreductase activity; ISS:dictyBase.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; ISS:dictyBase.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..321
FT                   /note="Aldose reductase C"
FT                   /id="PRO_0000327647"
FT   ACT_SITE        62
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         22..31
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         227..281
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   321 AA;  36529 MW;  2C05C8761CB9377D CRC64;
     MFQNNYNNNT NYNNNNFKLN DGNQIPSIGL GTYYSENPGE VGDAINNALK NGYRHIDGAA
     FYGNEKVIGN SLKEIFKEGE IKREDIFYTS KLWNSCHNSN LVVKHCVKTI EDLGIGYLDL
     YLIHWPIAFE NSNPLGLTIE PLRDQNGNPI IAPVSIRETW QEMEKLVELG LVKSIGVSNF
     NVQNLVDLLT YAKIKPVVNQ VEIHPYLTQF KLQEYCDKYE IKLVAYSPLG QGKCDFFSNK
     ILKSIAGKYK KSVANVIFKW LNQRGIAAIP KSGNHSRIIE NFNIFDFQLS NDDIEKINSL
     NANIRTCSPI TFFGTPFYLF D