ID Q6EM44_MALDO Unreviewed; 322 AA.
AC Q6EM44;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=NAD-dependent sorbitol dehydrogenase 2 {ECO:0000313|EMBL:AAP69751.1};
DE EC=1.1.1.14 {ECO:0000313|EMBL:AAP69751.1};
DE Flags: Fragment;
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:AAP69751.1};
RN [1] {ECO:0000313|EMBL:AAP69751.1}
RP NUCLEOTIDE SEQUENCE.
RA Nosarzewski M., Clements A.M., Downie A.B., Archbold D.D.;
RT "Sorbitol dehydrogenase expression and activity during apple fruit set and
RT early development.";
RL Physiol. Plantarum 121:391-398(2004).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; AY244808; AAP69751.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6EM44; -.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR CDD; cd05285; sorbitol_DH; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR045306; SDH-like.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43161:SF9; SORBITOL DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AAP69751.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 2..322
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAP69751.1"
FT NON_TER 322
FT /evidence="ECO:0000313|EMBL:AAP69751.1"
SQ SEQUENCE 322 AA; 34471 MW; F7DD1E326DD967A1 CRC64;
ILPFKLPAIG PNDVRIRIKA VGICGSDIHY LKTMKCGDFQ VKDPMVIGHE CAGIVDKVGS
EVKHLVPGDR VAVEPGISCA HCQQCKGGRY NLCPDMKFFA TPPVHGSLAN QIVHPADLCF
KLPENVSLEE GAMCEPLSVG VHACRRANVG PETTVLIVGA GPIGLVSVLA ARAFGAPRIV
IVDMDDRRLA MAKSLGADGT VKVSTKMEDL DDEVAKIKEA MGSEVDVTFD CVGFNKTMST
GLNATRPGGK VCLVGMGHGV MTVPLTPAAA REVDVVGVFR YKNTWPLCLE FLRSGKIDVK
PLITHRFGFT EKEVEEALEP VL
//
