ID   ALDR_PIG                Reviewed;         316 AA.
AC   P80276;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 164.
DE   RecName: Full=Aldo-keto reductase family 1 member B1;
DE            EC=1.1.1.21 {ECO:0000250|UniProtKB:P15121};
DE            EC=1.1.1.300 {ECO:0000250|UniProtKB:P15121};
DE            EC=1.1.1.372 {ECO:0000250|UniProtKB:P15121};
DE            EC=1.1.1.54 {ECO:0000250|UniProtKB:P15121};
DE   AltName: Full=Aldehyde reductase;
DE   AltName: Full=Aldose reductase;
DE            Short=AR;
GN   Name=AKR1B1; Synonyms=ALR2;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=8493902; DOI=10.1007/978-1-4615-2904-0_28;
RA   Kubiseski T.J., Green N.C., Flynn T.G.;
RT   "Location of an essential arginine residue in the primary structure of pig
RT   aldose reductase.";
RL   Adv. Exp. Med. Biol. 328:259-265(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-316, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC   TISSUE=Lens;
RX   PubMed=8281941; DOI=10.1111/j.1432-1033.1993.tb18445.x;
RA   Jaquinod M., Potier N., Klarskov K., Reymann J.-M., Sorokine O.,
RA   Kieffer S., Barth P., Andriantomanga V., Biellmann J.-F.,
RA   van Dorsselaer A.;
RT   "Sequence of pig lens aldose reductase and electrospray mass spectrometry
RT   of non-covalent and covalent complexes.";
RL   Eur. J. Biochem. 218:893-903(1993).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=1734286; DOI=10.1038/355469a0;
RA   Rondeau J.-M., Tete-Favier F., Podjarny A., Reymann J.-M., Barth P.,
RA   Biellmann J.-F., Moras D.;
RT   "Novel NADPH-binding domain revealed by the crystal structure of aldose
RT   reductase.";
RL   Nature 355:469-472(1992).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=9195881; DOI=10.1016/s0969-2126(97)00216-5;
RA   Urzhumtsev A., Tete-Favier F., Mitschler A., Barbanton J., Barth P.,
RA   Urzhumtseva L., Biellmann J.-F., Podjarny A.D., Moras D.;
RT   "A 'specificity' pocket inferred from the crystal structures of the
RT   complexes of aldose reductase with the pharmaceutically important
RT   inhibitors tolrestat and sorbinil.";
RL   Structure 5:601-612(1997).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of
CC       carbonyl-containing compounds to their corresponding alcohols. Displays
CC       enzymatic activity towards endogenous metabolites such as aromatic and
CC       aliphatic aldehydes, ketones, monosaccharides, bile acids and
CC       xenobiotics substrates. It catalyzes the reduction of glucose to
CC       sorbitol, the first step of the polyol pathway, an alternative route of
CC       glucose metabolism that converts glucose to fructose. This pathway
CC       becomes highly active under elevated glucose levels, such as during
CC       hyperglycemia. Reduces steroids and their derivatives and
CC       prostaglandins. Displays low enzymatic activity toward all-trans-
CC       retinal, 9-cis-retinal, and 13-cis-retinal. Catalyzes the reduction of
CC       diverse phospholipid aldehydes such as 1-palmitoyl-2-(5-oxovaleroyl)-sn
CC       -glycero-3-phosphoethanolamin (POVPC) and related phospholipid
CC       aldehydes that are generated from the oxydation of phosphotidylcholine
CC       and phosphatdyleethanolamides. Plays a role in detoxifying dietary and
CC       lipid-derived unsaturated carbonyls, such as crotonaldehyde, 4-
CC       hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal and their
CC       glutathione-conjugates carbonyls (GS-carbonyls).
CC       {ECO:0000250|UniProtKB:P15121}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alditol + NADP(+) = an aldose + NADPH + H(+);
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:0000250|UniProtKB:P15121};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12791;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-sorbitol + NADP(+) = D-glucose + NADPH + H(+);
CC         Xref=Rhea:RHEA:59924, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17924, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:59926;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=erythritol + NADP(+) = D-erythrose + NADPH + H(+);
CC         Xref=Rhea:RHEA:59928, ChEBI:CHEBI:15378, ChEBI:CHEBI:17113,
CC         ChEBI:CHEBI:27904, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=xylitol + NADP(+) = D-xylose + NADPH + H(+);
CC         Xref=Rhea:RHEA:27445, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151,
CC         ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arabinitol + NADP(+) = L-arabinose + NADPH + H(+);
CC         Xref=Rhea:RHEA:25229, ChEBI:CHEBI:15378, ChEBI:CHEBI:17535,
CC         ChEBI:CHEBI:18403, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.21;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=galactitol + NADP(+) = D-galactose + NADPH + H(+);
CC         Xref=Rhea:RHEA:37967, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16813, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.21;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ribitol + NADP(+) = D-ribose + NADPH + H(+);
CC         Xref=Rhea:RHEA:59932, ChEBI:CHEBI:15378, ChEBI:CHEBI:15963,
CC         ChEBI:CHEBI:47013, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-gulonate + NADP(+) = aldehydo-D-glucuronate + NADPH + H(+);
CC         Xref=Rhea:RHEA:14909, ChEBI:CHEBI:13115, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142686;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + NADPH +
CC         H(+); Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC         ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.300; Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=9-cis-retinol + NADP(+) = 9-cis-retinal + NADPH + H(+);
CC         Xref=Rhea:RHEA:54916, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=13-cis-retinol + NADP(+) = 13-cis-retinal + NADPH + H(+);
CC         Xref=Rhea:RHEA:54920, ChEBI:CHEBI:15378, ChEBI:CHEBI:45479,
CC         ChEBI:CHEBI:45487, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycerol + NADP(+) = D-glyceraldehyde + NADPH + H(+);
CC         Xref=Rhea:RHEA:23592, ChEBI:CHEBI:15378, ChEBI:CHEBI:17378,
CC         ChEBI:CHEBI:17754, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.372; Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycerol + NADP(+) = L-glyceraldehyde + NADPH + H(+);
CC         Xref=Rhea:RHEA:38111, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC         ChEBI:CHEBI:27975, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.372; Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=benzyl alcohol + NADP(+) = benzaldehyde + NADPH + H(+);
CC         Xref=Rhea:RHEA:59944, ChEBI:CHEBI:15378, ChEBI:CHEBI:17169,
CC         ChEBI:CHEBI:17987, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prenol + NADP(+) = 3-methyl-2-butenal + NADPH + H(+);
CC         Xref=Rhea:RHEA:58420, ChEBI:CHEBI:15378, ChEBI:CHEBI:15825,
CC         ChEBI:CHEBI:16019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-hex-2-en-1-ol + NADP(+) = (E)-hex-2-enal + NADPH + H(+);
CC         Xref=Rhea:RHEA:58424, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:141205;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E,E)-2,4-hexadien-1-ol + NADP(+) = (E,E)-2,4-hexadienal +
CC         NADPH + H(+); Xref=Rhea:RHEA:58428, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:82334,
CC         ChEBI:CHEBI:142625; Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-hydroxynonen-1-ol + NADP(+) = a 4-hydroxynonenal + NADPH +
CC         H(+); Xref=Rhea:RHEA:58336, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:142593, ChEBI:CHEBI:142606;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prostaglandin F2alpha + NADP(+) = prostaglandin H2 + NADPH +
CC         H(+); Xref=Rhea:RHEA:45312, ChEBI:CHEBI:15378, ChEBI:CHEBI:57404,
CC         ChEBI:CHEBI:57405, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=allyl alcohol + NADP(+) = acrolein + NADPH + H(+);
CC         Xref=Rhea:RHEA:12168, ChEBI:CHEBI:15368, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16605, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.54;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pyridine 3-methanol + NADP(+) = pyridine-3-carbaldehyde +
CC         NADPH + H(+); Xref=Rhea:RHEA:58776, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28345, ChEBI:CHEBI:45213, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine
CC         + NADPH + H(+) = 1-hexadecanoyl-2-(5-hydroxypentanoyl)-sn-glycero-3-
CC         phosphocholine + NADP(+); Xref=Rhea:RHEA:58512, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77890,
CC         ChEBI:CHEBI:142747; Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(7-oxoheptanoyl)-sn-glycero-3-phosphocholine
CC         + NADPH + H(+) = 1-hexadecanoyl-2-(7-hydroxyheptanoyl)-sn-glycero-3-
CC         phosphocholine + NADP(+); Xref=Rhea:RHEA:58752, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:134601,
CC         ChEBI:CHEBI:142748; Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine +
CC         NADPH + H(+) = 1-hexadecanoyl-2-(9-hydroxynonanoyl)-sn-glycero-3-
CC         phosphocholine + NADP(+); Xref=Rhea:RHEA:58592, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61042,
CC         ChEBI:CHEBI:142749; Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-
CC         phosphoethanolamine + NADPH + H(+) = 1-hexadecanoyl-2-(5-
CC         hydroxypentanoyl)-sn-glycero-3-phosphoethanolamine + NADP(+);
CC         Xref=Rhea:RHEA:58756, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:142750, ChEBI:CHEBI:142751;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- ACTIVITY REGULATION: Cys-299 acts as a redox-sensitive regulatory site.
CC       Its thiol group undergoes reversible oxidative and nitrosative
CC       modifications (S-nitrosylation, S-glutathiolation) that modulate enzyme
CC       activity, linking AKR1B1 function to the cellular redox environment.
CC       Tolrestat inhibits retinal reduction. {ECO:0000250|UniProtKB:P15121}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P15121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MASS SPECTROMETRY: Mass=35778; Mass_error=3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:8281941};
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; L14950; AAA30989.1; -; mRNA.
DR   EMBL; U46065; AAC48515.1; -; mRNA.
DR   PIR; A59021; A59021.
DR   RefSeq; NP_001001539.1; NM_001001539.2.
DR   PDB; 1AH0; X-ray; 2.30 A; A=2-316.
DR   PDB; 1AH3; X-ray; 2.30 A; A=2-316.
DR   PDB; 1AH4; X-ray; 2.00 A; A=2-316.
DR   PDB; 1DLA; X-ray; 3.00 A; A/B/C/D=3-316.
DR   PDB; 1EKO; X-ray; 2.20 A; A=2-316.
DR   AlphaFoldDB; P80276; -.
DR   MDposit; P80276; -.
DR   SMR; P80276; -.
DR   FunCoup; P80276; 1494.
DR   STRING; 9823.ENSSSCP00000064633; -.
DR   BindingDB; P80276; -.
DR   ChEMBL; CHEMBL4559; -.
DR   DrugCentral; P80276; -.
DR   iPTMnet; P80276; -.
DR   PaxDb; 9823-ENSSSCP00000064633; -.
DR   PeptideAtlas; P80276; -.
DR   GeneID; 396816; -.
DR   KEGG; ssc:396816; -.
DR   CTD; 231; -.
DR   eggNOG; KOG1577; Eukaryota.
DR   HOGENOM; CLU_023205_0_0_1; -.
DR   InParanoid; P80276; -.
DR   OrthoDB; 416253at2759; -.
DR   SABIO-RK; P80276; -.
DR   EvolutionaryTrace; P80276; -.
DR   PRO; PR:P80276; -.
DR   Proteomes; UP000008227; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004032; F:aldose reductase (NADPH) activity; ISS:UniProtKB.
DR   GO; GO:0052650; F:all-trans-retinol dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR   GO; GO:0047655; F:allyl-alcohol dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0047681; F:aryl-alcohol dehydrogenase (NADP+) activity; IEA:RHEA.
DR   GO; GO:0032866; F:D-xylose reductase (NADPH) activity; IEA:RHEA.
DR   GO; GO:0047956; F:glycerol dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR   GO; GO:0032867; F:L-arabinose reductase (NADPH) activity; IEA:RHEA.
DR   GO; GO:0047939; F:L-glucuronate reductase activity; IEA:RHEA.
DR   GO; GO:0036130; F:prostaglandin H2 endoperoxidase reductase activity; ISS:UniProtKB.
DR   GO; GO:0001758; F:retinal dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0006060; P:D-sorbitol metabolic process; ISS:UniProtKB.
DR   GO; GO:0001523; P:retinoid metabolic process; ISS:UniProtKB.
DR   CDD; cd19107; AKR_AKR1B1-19; 1.
DR   FunFam; 3.20.20.100:FF:000009; Aldo-keto reductase family 1 member B1; 1.
DR   Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR036812; NAD(P)_OxRdtase_dom_sf.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   PANTHER; PTHR11732; ALDO/KETO REDUCTASE; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
DR   PDBsum; 1AH0; -.
DR   PDBsum; 1AH3; -.
DR   PDBsum; 1AH4; -.
DR   PDBsum; 1DLA; -.
DR   PDBsum; 1EKO; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Lipid metabolism; NADP; Oxidoreductase; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8281941"
FT   CHAIN           2..316
FT                   /note="Aldo-keto reductase family 1 member B1"
FT                   /id="PRO_0000124625"
FT   ACT_SITE        49
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         20
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         21
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         22
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         44
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         49
FT                   /ligand="alpha-D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58225"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         160
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         161
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         211
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         213
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         215
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         263
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         264
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         265
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         266
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         269
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         272
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         273
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         299
FT                   /ligand="alpha-D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58225"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   SITE            78
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
FT   SITE            299
FT                   /note="Redox-sensitive site"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:8281941"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07943"
FT   MOD_RES         222
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   MOD_RES         263
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   CONFLICT        99
FT                   /note="D -> N (in Ref. 1; AAA30989/AAC48515)"
FT                   /evidence="ECO:0000305"
FT   STRAND          4..6
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   STRAND          12..16
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   HELIX           25..38
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   HELIX           47..49
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   HELIX           52..64
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   STRAND          74..79
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   HELIX           81..83
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   HELIX           89..100
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   STRAND          105..110
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:1EKO"
FT   STRAND          129..131
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   HELIX           138..151
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   STRAND          153..155
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   STRAND          157..161
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   HELIX           164..171
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   STRAND          181..186
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   HELIX           194..203
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   STRAND          206..210
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   STRAND          223..225
FT                   /evidence="ECO:0007829|PDB:1AH0"
FT   HELIX           228..230
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   HELIX           232..241
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   HELIX           245..255
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   HELIX           267..272
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   TURN            273..278
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   HELIX           283..290
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   HELIX           302..304
FT                   /evidence="ECO:0007829|PDB:1AH4"
FT   HELIX           311..313
FT                   /evidence="ECO:0007829|PDB:1AH4"
SQ   SEQUENCE   316 AA;  35868 MW;  7218B663AC1B4E92 CRC64;
     MASHLVLYTG AKMPILGLGT WKSPPGKVTE AVKVAIDLGY RHIDCAHVYQ NENEVGLGLQ
     EKLQGQVVKR EDLFIVSKLW CTDHEKNLVK GACQTTLRDL KLDYLDLYLI HWPTGFKPGK
     DPFPLDGDGN VVPDESDFVE TWEAMEELVD EGLVKAIGVS NFNHLQVEKI LNKPGLKYKP
     AVNQIEVHPY LTQEKLIEYC KSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK
     YNKTTAQVLI RFPMQRNLIV IPKSVTPERI AENFQVFDFE LSPEDMNTLL SYNRNWRVCA
     LMSCASHKDY PFHEEY
//