ALRB_DICDI
ID ALRB_DICDI Reviewed; 311 AA.
AC Q54NZ7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Aldose reductase B;
DE Short=ARB;
DE EC=1.1.1.21;
DE AltName: Full=Aldehyde reductase B;
GN Name=alrB; ORFNames=DDB_G0285053;
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; AAFI02000073; EAL64990.2; -; Genomic_DNA.
DR RefSeq; XP_639920.2; XM_634828.2.
DR AlphaFoldDB; Q54NZ7; -.
DR SMR; Q54NZ7; -.
DR STRING; 44689.DDB0231282; -.
DR PaxDb; Q54NZ7; -.
DR EnsemblProtists; EAL64990; EAL64990; DDB_G0285053.
DR GeneID; 8624832; -.
DR KEGG; ddi:DDB_G0285053; -.
DR dictyBase; DDB_G0285053; alrB.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_3_1; -.
DR InParanoid; Q54NZ7; -.
DR OMA; WCIDQDI; -.
DR PhylomeDB; Q54NZ7; -.
DR PRO; PR:Q54NZ7; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
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.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..311
FT /note="Aldose reductase B"
FT /id="PRO_0000327646"
FT ACT_SITE 54
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 13..23
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219..273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 311 AA; 35060 MW; F60EBB244639962D CRC64;
MSQPQNTFKL NDDIHHIPMI GLGTYNGAKV GEVGDAVKVA LKSGYRHIDG AAIYMNEKEI
GHALKEVFAE GEIKREDIFY VSKLWNSCHH ASLVRKHCEK TLEDLGLEYL DLYLIHWPIA
FENADPSGTT TQPLRDSDGE PVLAAVSIRE TWQEMEKLVE YGLVKSIGVS NFNVQNLVDL
LTYAKIKPAI NQVEVHPYLS QPNLKYFCDR YGIVLTAYSP LGQGKCDLLS NETLKSIADK
HNKTVANVIF KWLNQRGIVT IPKSSNPARI IENFNIFDFQ LSNEDMDKIN SLNSNLRTCT
PANFCKIPLF D