GALDH_ARATH
ID GALDH_ARATH Reviewed; 319 AA.
AC O81884; D9IZZ0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=L-galactose dehydrogenase;
DE Short=At-GalDH;
DE Short=L-GalDH;
DE EC=1.1.1.316;
GN Name=LGALDH; OrderedLocusNames=At4g33670; ORFNames=T16L1.160;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12047629; DOI=10.1046/j.1365-313x.2002.01315.x;
RA Gatzek S., Wheeler G.L., Smirnoff N.;
RT "Antisense suppression of l-galactose dehydrogenase in Arabidopsis thaliana
RT provides evidence for its role in ascorbate synthesis and reveals light
RT modulated l-galactose synthesis.";
RL Plant J. 30:541-553(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Venkatesh J., Gururani M.A., Nookaraju A., Pandey S.K., Park S.W.,
RA Kim D.H., Chul C.S., Upadhyaya C.P.;
RT "Metabolic engineering for upregulation of vitamin C biosynthesis in
RT potato.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: Catalyzes the oxidation of L-galactose to L-galactono-1,4-
CC lactone in the presence of NAD(+). Uses NAD(+) as a hydrogen acceptor
CC much more efficiently than NADP(+). {ECO:0000269|PubMed:12047629}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-galactose + NAD(+) = H(+) + L-galactono-1,4-lactone + NADH;
CC Xref=Rhea:RHEA:31559, ChEBI:CHEBI:15378, ChEBI:CHEBI:17464,
CC ChEBI:CHEBI:37619, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.316; Evidence={ECO:0000269|PubMed:12047629};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.08 mM for L-galactose (at pH 7.5) {ECO:0000269|PubMed:12047629};
CC KM=56 mM for L-fucose (at pH 7.5) {ECO:0000269|PubMed:12047629};
CC KM=20.3 uM for NAD (at pH 7.5) {ECO:0000269|PubMed:12047629};
CC KM=0.59 mM for NADP (at pH 7.5) {ECO:0000269|PubMed:12047629};
CC pH dependence:
CC Optimum pH is 8.5-9. {ECO:0000269|PubMed:12047629};
CC -!- DISRUPTION PHENOTYPE: Lower leaf ascorbate concentration with
CC accumulation of L-galactose when grown under high light conditions.
CC {ECO:0000269|PubMed:12047629}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AJ417563; CAD10386.1; -; mRNA.
DR EMBL; HM230668; ADJ21815.1; -; mRNA.
DR EMBL; AL031394; CAA20580.1; -; Genomic_DNA.
DR EMBL; AL161583; CAB80084.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86264.1; -; Genomic_DNA.
DR EMBL; AY050377; AAK91395.1; -; mRNA.
DR EMBL; AY090337; AAL90998.1; -; mRNA.
DR PIR; T04984; T04984.
DR RefSeq; NP_195093.1; NM_119525.6.
DR AlphaFoldDB; O81884; -.
DR SMR; O81884; -.
DR STRING; 3702.AT4G33670.1; -.
DR PaxDb; O81884; -.
DR PRIDE; O81884; -.
DR ProteomicsDB; 248602; -.
DR EnsemblPlants; AT4G33670.1; AT4G33670.1; AT4G33670.
DR GeneID; 829509; -.
DR Gramene; AT4G33670.1; AT4G33670.1; AT4G33670.
DR KEGG; ath:AT4G33670; -.
DR Araport; AT4G33670; -.
DR TAIR; locus:2134228; AT4G33670.
DR eggNOG; KOG1576; Eukaryota.
DR HOGENOM; CLU_023205_2_3_1; -.
DR InParanoid; O81884; -.
DR OMA; YELDYDN; -.
DR OrthoDB; 1085241at2759; -.
DR PhylomeDB; O81884; -.
DR BioCyc; ARA:AT4G33670-MON; -.
DR BioCyc; MetaCyc:AT4G33670-MON; -.
DR BRENDA; 1.1.1.316; 399.
DR PRO; PR:O81884; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81884; baseline and differential.
DR Genevisible; O81884; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0010349; F:L-galactose dehydrogenase activity; IDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IMP:TAIR.
DR CDD; cd19163; AKR_galDH; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044479; LGALDH-like.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR42686; PTHR42686; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Galactose metabolism; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..319
FT /note="L-galactose dehydrogenase"
FT /id="PRO_0000418776"
FT DOMAIN 122..269
FT /note="SIS"
FT ACT_SITE 59
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 249
FT /note="K -> E (in Ref. 2; ADJ21815)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 34532 MW; 9400717380DFA71E CRC64;
MTKIELRALG NTGLKVSAVG FGASPLGSVF GPVAEDDAVA TVREAFRLGI NFFDTSPYYG
GTLSEKMLGK GLKALQVPRS DYIVATKCGR YKEGFDFSAE RVRKSIDESL ERLQLDYVDI
LHCHDIEFGS LDQIVSETIP ALQKLKQEGK TRFIGITGLP LDIFTYVLDR VPPGTVDVIL
SYCHYGVNDS TLLDLLPYLK SKGVGVISAS PLAMGLLTEQ GPPEWHPASP ELKSASKAAV
AHCKSKGKKI TKLALQYSLA NKEISSVLVG MSSVSQVEEN VAAVTELESL GMDQETLSEV
EAILEPVKNL TWPSGIHQN
