IDND_VITVI
ID IDND_VITVI Reviewed; 366 AA.
AC Q1PSI9; A5ANX2; A7R1S9; F6HP72;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=L-idonate 5-dehydrogenase;
DE EC=1.1.1.366;
GN OrderedLocusNames=VIT_16s0100g00290;
GN ORFNames=GSVIVT00012394001, LOC100232980, VITISV_028585;
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL
RP STAGE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Cabernet Sauvignon;
RX PubMed=16567629; DOI=10.1073/pnas.0510864103;
RA DeBolt S., Cook D.R., Ford C.M.;
RT "L-tartaric acid synthesis from vitamin C in higher plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5608-5613(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024;
RX PubMed=17721507; DOI=10.1038/nature06148;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir;
RX PubMed=18094749; DOI=10.1371/journal.pone.0001326;
RA Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT "A high quality draft consensus sequence of the genome of a heterozygous
RT grapevine variety.";
RL PLoS ONE 2:E1326-E1326(2007).
CC -!- FUNCTION: Involved in the catabolism of ascorbate to tartrate. The
CC enzyme has no activity with NADP(+). {ECO:0000269|PubMed:16567629}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-idonate + NAD(+) = 5-dehydro-D-gluconate + H(+) + NADH;
CC Xref=Rhea:RHEA:21172, ChEBI:CHEBI:15378, ChEBI:CHEBI:17796,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58143;
CC EC=1.1.1.366; Evidence={ECO:0000269|PubMed:16567629};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.2 mM for L-idonate in the forward reaction
CC {ECO:0000269|PubMed:16567629};
CC KM=12.5 mM for 5-dehydro-D-gluconate in the reverse reaction
CC {ECO:0000269|PubMed:16567629};
CC -!- PATHWAY: Carbohydrate acid metabolism; L-idonate degradation.
CC -!- DEVELOPMENTAL STAGE: Peak of expression 4 weeks post flowering, at the
CC time when tartaric acid biosynthesis occurs.
CC {ECO:0000269|PubMed:16567629}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAN73609.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CCB56478.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ124868; ABA01327.1; -; mRNA.
DR EMBL; FN596000; CCB56478.1; ALT_SEQ; Genomic_DNA.
DR EMBL; FN597040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AM431054; CAN73609.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001267883.1; NM_001280954.1.
DR RefSeq; XP_002267662.2; XM_002267626.4.
DR RefSeq; XP_010662490.1; XM_010664188.2.
DR AlphaFoldDB; Q1PSI9; -.
DR SMR; Q1PSI9; -.
DR STRING; 29760.VIT_16s0100g00290.t01; -.
DR PRIDE; Q1PSI9; -.
DR EnsemblPlants; Vitvi16g01857_t006; Vitvi16g01857_P006; Vitvi16g01857.
DR GeneID; 100232980; -.
DR GeneID; 100257330; -.
DR Gramene; Vitvi16g01857_t006; Vitvi16g01857_P006; Vitvi16g01857.
DR KEGG; vvi:100232980; -.
DR KEGG; vvi:100257330; -.
DR eggNOG; KOG0024; Eukaryota.
DR HOGENOM; CLU_362663_0_0_1; -.
DR InParanoid; Q1PSI9; -.
DR OrthoDB; 1019156at2759; -.
DR BioCyc; MetaCyc:MON-16192; -.
DR BRENDA; 1.1.1.264; 6671.
DR BRENDA; 1.1.1.366; 6671.
DR SABIO-RK; Q1PSI9; -.
DR UniPathway; UPA00793; -.
DR Proteomes; UP000009183; Chromosome 16.
DR ExpressionAtlas; Q1PSI9; baseline and differential.
DR GO; GO:0102198; F:L-idonate 5-dehydrogenase activity (NAD-dependent); IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0046183; P:L-idonate catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05285; sorbitol_DH; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_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 Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..366
FT /note="L-idonate 5-dehydrogenase"
FT /id="PRO_0000367051"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 13
FT /note="G -> S (in Ref. 1; ABA01327)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="Y -> H (in Ref. 1; ABA01327 and 3; CAN73609)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="A -> V (in Ref. 1; ABA01327 and 3; CAN73609)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="F -> L (in Ref. 1; ABA01327)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 39466 MW; 8EABD13EA303E6C5 CRC64;
MGKGGNSEDA VSGKEHGEEN MAAWLLGIKT LKIQPYILPS LGPYDVKVRI KAVGICGSDV
HHFKTMRCAN FIVKKPMVIG HECAGIIEEV GSEVKNLVAG DRVALEPGIS CNRCSLCRNG
QYNLCREMKF FGSPPTNGSL ANQVVHPSNL CFKLPDNVSL EEGAMCEPLS VGIHACRRAN
VGPETNVLIM GSGPIGLVTM LAARAFGAPR IVLVDVDDQR LAIAKDLGAD DIIRVSTNIQ
DLDEEVAKIQ STMVTGVDVS FDCVGFNKTM STALNATRAG GKVCLVGLAQ SEMTVPLTPA
AAREVDIVGI FRYRNTWPLC LEFLRSGKID VKPLITHRFT FSQKDVEEAF ETSARGGNAI
KVMFNL
