GRDH2_ARATH
ID GRDH2_ARATH Reviewed; 289 AA.
AC Q9MA93; Q944H4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Glucose and ribitol dehydrogenase homolog 2;
DE EC=1.1.1.-;
GN OrderedLocusNames=At3g05260; ORFNames=T12H1.23;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
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: May act as a short alcohol-polyol-sugar dehydrogenase
CC possibly related to carbohydrate metabolism and the acquisition of
CC desiccation tolerance. May also be involved in signal transduction (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AC009177; AAF27032.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74212.1; -; Genomic_DNA.
DR EMBL; AF428435; AAL16204.1; -; mRNA.
DR RefSeq; NP_187177.1; NM_111399.5.
DR AlphaFoldDB; Q9MA93; -.
DR SMR; Q9MA93; -.
DR STRING; 3702.AT3G05260.1; -.
DR PaxDb; Q9MA93; -.
DR PRIDE; Q9MA93; -.
DR ProteomicsDB; 222353; -.
DR EnsemblPlants; AT3G05260.1; AT3G05260.1; AT3G05260.
DR GeneID; 819690; -.
DR Gramene; AT3G05260.1; AT3G05260.1; AT3G05260.
DR KEGG; ath:AT3G05260; -.
DR Araport; AT3G05260; -.
DR TAIR; locus:2096284; AT3G05260.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_4_1_1; -.
DR InParanoid; Q9MA93; -.
DR OMA; FSMFHMT; -.
DR OrthoDB; 1194344at2759; -.
DR PhylomeDB; Q9MA93; -.
DR BioCyc; ARA:AT3G05260-MON; -.
DR PRO; PR:Q9MA93; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9MA93; baseline and differential.
DR Genevisible; Q9MA93; AT.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 2: Evidence at transcript level;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..289
FT /note="Glucose and ribitol dehydrogenase homolog 2"
FT /id="PRO_0000239258"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 43..67
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 2
FT /note="A -> P (in Ref. 3; AAL16204)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 31452 MW; E45A19AAD784063F CRC64;
MASGFPPQKQ ETQPGIQHVM EPTPEFSSSN YKPSNKLHGK VALVTGGDSG IGKAVCHCYA
LEGASVAFTY VKGREDKDAE ETLRLLHEVK TREAKEPIMI ATDLGFEENC KRVVEEVVNS
FGRIDVLVNC AAEQHEVSIE DIDEARLERV FRTNIFSQFF LVKYALKHMK EGSSIINTTS
VVAYAGNSSL LEYTATKGAI VSFTRGLALQ LAPKGIRVNG VAPGPVWTPL IPASFSEEAI
KQFGSETPMK RAAQPVEVAP SYVFLACNHC SSYYTGQILH PNGGLIVNA
