ALDR_HORVU
ID ALDR_HORVU Reviewed; 320 AA.
AC P23901;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Aldose reductase;
DE Short=AR;
DE EC=1.1.1.21;
DE AltName: Full=Aldehyde reductase;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Aura;
RX PubMed=1827067; DOI=10.1002/j.1460-2075.1991.tb08042.x;
RA Bartels D., Engelhardt K., Roncarati R., Schneider K., Rotter M.,
RA Salamini F.;
RT "An ABA and GA modulated gene expressed in the barley embryo encodes an
RT aldose reductase related protein.";
RL EMBO J. 10:1037-1043(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 2-320.
RX PubMed=18300247; DOI=10.1002/prot.21996;
RA Olsen J.G., Pedersen L., Christensen C.L., Olsen O., Henriksen A.;
RT "Barley aldose reductase: structure, cofactor binding, and substrate
RT recognition in the aldo/keto reductase 4C family.";
RL Proteins 71:1572-1581(2008).
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 -!- INDUCTION: By abscisic acid (ABA) and gibberellic acid (GA).
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; X57526; CAA40747.1; -; Genomic_DNA.
DR PIR; S15024; S15024.
DR PDB; 2BGQ; X-ray; 2.50 A; A=2-320.
DR PDB; 2BGS; X-ray; 1.64 A; A=2-320.
DR PDB; 2VDG; X-ray; 1.92 A; A=2-320.
DR PDBsum; 2BGQ; -.
DR PDBsum; 2BGS; -.
DR PDBsum; 2VDG; -.
DR AlphaFoldDB; P23901; -.
DR SMR; P23901; -.
DR EvolutionaryTrace; P23901; -.
DR ExpressionAtlas; P23901; baseline and differential.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IEA:UniProtKB-EC.
DR CDD; cd19125; AKR_AKR4C1-15; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044498; AKR4C.
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 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Stress response.
FT CHAIN 1..320
FT /note="Aldose reductase"
FT /id="PRO_0000124628"
FT ACT_SITE 60
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 215..269
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 88
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:2BGS"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:2BGS"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:2BGS"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:2BGS"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2BGS"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2BGS"
FT HELIX 63..75
FT /evidence="ECO:0007829|PDB:2BGS"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2BGS"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:2BGS"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:2BGS"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:2BGS"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:2BGS"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:2BGS"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:2BGS"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:2BGS"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:2BGS"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:2BGS"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:2BGS"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:2BGS"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:2BGS"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:2BGQ"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:2BGS"
FT HELIX 241..252
FT /evidence="ECO:0007829|PDB:2BGS"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:2BGQ"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:2BGS"
FT HELIX 279..287
FT /evidence="ECO:0007829|PDB:2BGS"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:2BGS"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:2BGS"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:2BGS"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:2BGS"
SQ SEQUENCE 320 AA; 35807 MW; 5AA72C021E9A93C0 CRC64;
MASAKATMGQ GEQDHFVLKS GHAMPAVGLG TWRAGSDTAH SVRTAITEAG YRHVDTAAEY
GVEKEVGKGL KAAMEAGIDR KDLFVTSKIW CTNLAPERVR PALENTLKDL QLDYIDLYHI
HWPFRLKDGA HMPPEAGEVL EFDMEGVWKE MENLVKDGLV KDIGVCNYTV TKLNRLLRSA
KIPPAVCQME MHPGWKNDKI FEACKKHGIH VTAYSPLGSS EKNLAHDPVV EKVANKLNKT
PGQVLIKWAL QRGTSVIPKS SKDERIKENI QVFGWEIPEE DFKVLCSIKD EKRVLTGEEL
FVNKTHGPYR SAADVWDHEN
