ALRA_DICDI
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 03-AUG-2022, entry version 105.
DE RecName: Full=Aldose reductase A;
DE Short=ARA;
DE EC=1.1.1.21 {ECO:0000269|PubMed:14551196};
DE AltName: Full=Aldehyde reductase A {ECO:0000303|PubMed:14551196};
DE Short=AlrA {ECO:0000303|PubMed:14551196};
GN Name=alrA; ORFNames=DDB_G0293850;
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).
RN [2]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND 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., Hatton R.D.,
RA Shoemaker J.D., Gomer R.H.;
RT "Disruption of aldehyde reductase increases group size in dictyostelium.";
RL J. Biol. Chem. 279:837-847(2004).
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 (PubMed:14551196). Probably
CC affects several metabolic pathways in addition to converting glucose to
CC sorbitol (PubMed:14551196). Affects group size (PubMed:14551196).
CC {ECO:0000269|PubMed:14551196, ECO:0000303|PubMed:14551196}.
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 Evidence={ECO:0000269|PubMed:14551196};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12791;
CC Evidence={ECO:0000269|PubMed:14551196};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14551196}.
CC -!- DEVELOPMENTAL STAGE: Present in vegetative cells; the levels decrease
CC slightly upon starvation and remain constant until 10 hours of
CC development and then decline. At 25 hours there is very little
CC detectable protein. {ECO:0000269|PubMed:14551196}.
CC -!- DISRUPTION PHENOTYPE: Cells show a decrease in the ability to reduce
CC both glyceraldehyde and glucose in an NADPH-coupled reaction and a
CC decrease in glucose levels. They grow normally but form long unbroken
CC streams and huge groups. They show normal adhesion but a reduced
CC motility. They secrete low levels of countin and CF50, two component of
CC the counting factor (CF) but are responsive to CF and partially
CC responsive to recombinant countin and CF50.
CC {ECO:0000269|PubMed:14551196}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AAFI02000223; EAL60496.1; -; Genomic_DNA.
DR EMBL; BK001032; DAA01127.1; -; mRNA.
DR RefSeq; XP_628918.1; XM_628916.1.
DR AlphaFoldDB; Q6IMN8; -.
DR SMR; Q6IMN8; -.
DR STRING; 44689.DDB0215363; -.
DR PaxDb; Q6IMN8; -.
DR EnsemblProtists; EAL60496; EAL60496; DDB_G0293850.
DR GeneID; 8629459; -.
DR KEGG; ddi:DDB_G0293850; -.
DR dictyBase; DDB_G0293850; alrA.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; Q6IMN8; -.
DR OMA; KLWPTDQ; -.
DR PhylomeDB; Q6IMN8; -.
DR BRENDA; 1.1.1.283; 1939.
DR PRO; PR:Q6IMN8; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IDA:dictyBase.
DR GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR GO; GO:0042593; P:glucose homeostasis; IMP:dictyBase.
DR GO; GO:0031158; P:negative regulation of aggregate size involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP: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 1: Evidence at protein level;
KW Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..297
FT /note="Aldose reductase A"
FT /id="PRO_0000327645"
FT ACT_SITE 49
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 10..19
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 207..259
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
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
