RHM3_ARATH
ID RHM3_ARATH Reviewed; 664 AA.
AC Q9LH76;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM3 {ECO:0000305|PubMed:17190829};
DE AltName: Full=Probable rhamnose biosynthetic enzyme 3;
DE Short=AtRHM3;
DE Includes:
DE RecName: Full=UDP-glucose 4,6-dehydratase {ECO:0000305|PubMed:17190829};
DE EC=4.2.1.76 {ECO:0000305|PubMed:17190829};
DE Includes:
DE RecName: Full=UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose 4-keto-reductase {ECO:0000305|PubMed:17190829};
DE EC=1.1.1.- {ECO:0000305|PubMed:17190829};
DE EC=5.1.3.- {ECO:0000305|PubMed:17190829};
GN Name=RHM3 {ECO:0000303|PubMed:15134748}; OrderedLocusNames=At3g14790;
GN ORFNames=T21E2_4;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14671019; DOI=10.1104/pp.103.034314;
RA Usadel B., Kuschinsky A.M., Rosso M.G., Eckermann N., Pauly M.;
RT "RHM2 is involved in mucilage pectin synthesis and is required for the
RT development of the seed coat in Arabidopsis.";
RL Plant Physiol. 134:286-295(2004).
RN [5]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Col-2;
RX PubMed=14701918; DOI=10.1104/pp.103.035519;
RA Western T.L., Young D.S., Dean G.H., Tan W.L., Samuels A.L., Haughn G.W.;
RT "MUCILAGE-MODIFIED4 encodes a putative pectin biosynthetic enzyme
RT developmentally regulated by APETALA2, TRANSPARENT TESTA GLABRA1, and
RT GLABRA2 in the Arabidopsis seed coat.";
RL Plant Physiol. 134:296-306(2004).
RN [6]
RP IDENTIFICATION.
RX PubMed=11554483; DOI=10.1023/a:1010671129803;
RA Reiter W.-D., Vanzin G.F.;
RT "Molecular genetics of nucleotide sugar interconversion pathways in
RT plants.";
RL Plant Mol. Biol. 47:95-113(2001).
RN [7]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=15134748; DOI=10.1016/j.pbi.2004.03.004;
RA Seifert G.J.;
RT "Nucleotide sugar interconversions and cell wall biosynthesis: how to bring
RT the inside to the outside.";
RL Curr. Opin. Plant Biol. 7:277-284(2004).
RN [8]
RP FUNCTION.
RX PubMed=17190829; DOI=10.1074/jbc.m610196200;
RA Oka T., Nemoto T., Jigami Y.;
RT "Functional analysis of Arabidopsis thaliana RHM2/MUM4, a multidomain
RT protein involved in UDP-D-glucose to UDP-L-rhamnose conversion.";
RL J. Biol. Chem. 282:5389-5403(2007).
CC -!- FUNCTION: Trifunctional enzyme involved in UDP-beta-L-rhamnose
CC biosynthesis, a precursor of the primary cell wall components
CC rhamnogalacturonan I (RG-I) and rhamnogalacturonan II (RG-II)
CC (PubMed:17190829). Catalyzes the dehydration of UDP-glucose to form
CC UDP-4-dehydro-6-deoxy-D-glucose followed by the epimerization of the
CC C3' and C5' positions of UDP-4-dehydro-6-deoxy-D-glucose to form UDP-4-
CC keto-beta-L-rhamnose and the reduction of UDP-4-keto-beta-L-rhamnose to
CC yield UDP-beta-L-rhamnose (By similarity).
CC {ECO:0000250|UniProtKB:Q9LPG6, ECO:0000269|PubMed:14671019,
CC ECO:0000269|PubMed:17190829}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-glucose = H2O + UDP-4-dehydro-6-deoxy-alpha-D-
CC glucose; Xref=Rhea:RHEA:21500, ChEBI:CHEBI:15377, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:85329; EC=4.2.1.76;
CC Evidence={ECO:0000250|UniProtKB:Q9LPG6};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:Q9LPG6};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:Q9LPG6};
CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, seedlings, and siliques.
CC Lower expression in inflorescence tips, and leaves.
CC {ECO:0000269|PubMed:14671019, ECO:0000269|PubMed:14701918}.
CC -!- DOMAIN: The dehydratase activity is contained in the N-terminal region
CC while the epimerase and reductase activities are in the C-terminal
CC region. {ECO:0000250|UniProtKB:Q9LPG6}.
CC -!- MISCELLANEOUS: In bacteria, TDP-L-rhamnose is formed by the successive
CC action of three different enzymes on TDP-D-glucose. In plants, on the
CC other hand, a single polypeptide probably catalyzes all three reactions
CC that lead to the conversion of UDP-D-glucose to UDP-L-rhamnose.
CC -!- SIMILARITY: In the N-terminal section; belongs to the NAD(P)-dependent
CC epimerase/dehydratase family. dTDP-glucose dehydratase subfamily.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the dTDP-4-
CC dehydrorhamnose reductase family. {ECO:0000305}.
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DR EMBL; AP002061; BAB02645.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75567.1; -; Genomic_DNA.
DR EMBL; AY078958; AAL84958.1; -; mRNA.
DR EMBL; AY142060; AAM98324.1; -; mRNA.
DR RefSeq; NP_188097.1; NM_112340.4.
DR AlphaFoldDB; Q9LH76; -.
DR SMR; Q9LH76; -.
DR BioGRID; 6041; 3.
DR IntAct; Q9LH76; 2.
DR STRING; 3702.AT3G14790.1; -.
DR iPTMnet; Q9LH76; -.
DR PaxDb; Q9LH76; -.
DR PRIDE; Q9LH76; -.
DR ProteomicsDB; 236950; -.
DR EnsemblPlants; AT3G14790.1; AT3G14790.1; AT3G14790.
DR GeneID; 820707; -.
DR Gramene; AT3G14790.1; AT3G14790.1; AT3G14790.
DR KEGG; ath:AT3G14790; -.
DR Araport; AT3G14790; -.
DR TAIR; locus:2099372; AT3G14790.
DR eggNOG; KOG0747; Eukaryota.
DR HOGENOM; CLU_026813_1_0_1; -.
DR InParanoid; Q9LH76; -.
DR OMA; GSKGWIG; -.
DR PhylomeDB; Q9LH76; -.
DR BioCyc; ARA:AT3G14790-MON; -.
DR BioCyc; MetaCyc:AT3G14790-MON; -.
DR PRO; PR:Q9LH76; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LH76; baseline and differential.
DR Genevisible; Q9LH76; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0050377; F:UDP-glucose 4,6-dehydratase activity; IBA:GO_Central.
DR GO; GO:0010280; F:UDP-L-rhamnose synthase activity; IDA:TAIR.
DR GO; GO:0010315; P:auxin export across the plasma membrane; IBA:GO_Central.
DR GO; GO:0051555; P:flavonol biosynthetic process; IBA:GO_Central.
DR GO; GO:0010253; P:UDP-rhamnose biosynthetic process; IDA:TAIR.
DR CDD; cd05246; dTDP_GD_SDR_e; 1.
DR InterPro; IPR005888; dTDP_Gluc_deHydtase.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029903; RmlD-like-bd.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR Pfam; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
PE 2: Evidence at transcript level;
KW Isomerase; Lyase; Multifunctional enzyme; NAD; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..664
FT /note="Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-
FT keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-
FT reductase RHM3"
FT /id="PRO_0000183254"
FT ACT_SITE 133
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 13..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 386..392
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LPG6"
SQ SEQUENCE 664 AA; 74914 MW; 211FB4C037BB6842 CRC64;
MATYKPKNIL ITGAAGFIAS HVANRLVRSY PDYKIVVLDK LDYCSNLKNL NPSKSSPNFK
FVKGDIASAD LVNYLLITEE IDTIMHFAAQ THVDNSFGNS FEFTKNNIYG THVLLEACKV
TGQIRRFIHV STDEVYGETD EDASVGNHEA SQLLPTNPYS ATKAGAEMLV MAYGRSYGLP
VITTRGNNVY GPNQFPEKLI PKFILLAMNG KPLPIHGDGS NVRSYLYCED VAEAFEVVLH
KGEVNHVYNI GTTRERRVID VANDISKLFG IDPDSTIQYV ENRPFNDQRY FLDDQKLKKL
GWCERTNWEE GLRKTMEWYT ENPEWWGDVS GALLPHPRML MMPGDRHSDG SDEHKNADGN
QTFTVVTPTK AGCSGDKRSL KFLIYGKTGW LGGLLGKLCE KQGIPYEYGK GRLEDRASLI
ADIRSIKPSH VFNAAGLTGR PNVDWCESHK TETIRVNVAG TLTLADVCRE NDLLMMNFAT
GCIFEYDAAH PEGSGIGFKE EDKPNFTGSF YSKTKAMVEE LLREFDNVCT LRVRMPISSD
LNNPRNFITK ISRYNKVVNI PNSMTILDEL LPISIEMAKR NLRGIWNFTN PGVVSHNEIL
EMYKSYIEPD FKWSNFNLEE QAKVIVAPRS NNEMDGAKLS KEFPEMLSIK DSLIKYVFEP
NKRT
