ID   ALRA_DICDI              Reviewed;         297 AA.
AC   Q6IMN8; Q54B70;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 32.
DE   RecName: Full=Aldose reductase A;
DE            Short=ARA;
DE            EC=1.1.1.21;
DE   AltName: Full=Aldehyde reductase A;
GN   Name=alrA; ORFNames=DDB_G0293850;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; 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.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   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.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   IDENTIFICATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=AX4;
RX   PubMed=14551196; DOI=10.1074/jbc.M310539200;
RA   Ehrenman K., Yang G., Hong W.-P., Gao T., Jang W., Brock D.A.,
RA   Hatton R.D., Shoemaker J.D., Gomer R.H.;
RT   "Disruption of aldehyde reductase increases group size in
RT   dictyostelium.";
RL   J. Biol. Chem. 279:837-847(2004).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of a wide
CC       variety of carbonyl-containing compounds to their corresponding
CC       alcohols with a broad range of catalytic efficiencies (By
CC       similarity). Probably affects several metabolic pathways in
CC       addition to converting glucose to sorbitol. Affects group size.
CC   -!- CATALYTIC ACTIVITY: Alditol + NAD(P)(+) = aldose + NAD(P)H.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DEVELOPMENTAL STAGE: Present in vegetative cells; the levels
CC       decrease slightly upon starvation and remain constant until 10
CC       hours of development and then decline. At 25 hours there is very
CC       little detectable protein.
CC   -!- DISRUPTION PHENOTYPE: Cells show a decrease in the ability to
CC       reduce both glyceraldehyde and glucose in an NADPH-coupled
CC       reaction and a decrease in glucose levels. They grow normally but
CC       form long unbroken streams and huge groups. They show normal
CC       adhesion but a reduced motility. They secrete low levels of
CC       countin and CF50, two component of the counting factor (CF) but
CC       are responsive to CF and partially responsive to recombinant
CC       countin and CF50.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family.
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DR   EMBL; AAFI02000223; EAL60496.1; -; Genomic_DNA.
DR   EMBL; BK001032; DAA01127.1; -; mRNA.
DR   RefSeq; XP_628918.1; -.
DR   HSSP; P15121; 1PWL.
DR   GeneID; 3385573; -.
DR   KEGG; ddi:DDB_0215363; -.
DR   dictyBase; DDB_G0293850; alrA.
DR   OMA; Q6IMN8; ETWEEME.
DR   BRENDA; 1.1.1.21; 424.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004032; F:aldehyde reductase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001395; Aldo/ket_red.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   Gene3D; G3DSA:3.20.20.100; Aldo/ket_red; 1.
DR   PANTHER; PTHR11732; Aldo/ket_red; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   ProDom; PD000288; Aldo/ket_red; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Complete proteome; Cytoplasm; NADP; Oxidoreductase.
FT   CHAIN         1    297       Aldose reductase A.
FT                                /FTId=PRO_0000327645.
FT   NP_BIND      10     19       NADP (Potential).
FT   NP_BIND     207    259       NADP (By similarity).
FT   ACT_SITE     49     49       Proton donor (By similarity).
FT   BINDING     112    112       Substrate (By similarity).
SQ   SEQUENCE   297 AA;  33649 MW;  4716A0B09F61D861 CRC64;
     MEPSFKLSSG HKIPLVGFGT WKAETTLVGK AVEVALDAGY RHIDCAAVYL NEKEVGEAFT
     KKFTTEATVK REDVFITSKL WNTFHKKEHV RPALERTLSD LGLQYLDLYL VHWPVAFEYT
     SNDIQTSGST QEFVSIRETW EEMEKLVDAG LVKSIGLSNF NVQGLMEVLS YARIKPAANQ
     VELHPFLSQP ELKKFCDKHN IHLTAYSPLG NGAFVDNEEV GAIAKKYNKT IPNVLCKWAI
     QKNFSVIPKS STPSRVAENF DLFNFEIEEA DMLFLDKMDK NLRTCDPAKF WGVPLFN
//