RHM1_ARATH
ID RHM1_ARATH Reviewed; 669 AA.
AC Q9SYM5;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
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 RHM1 {ECO:0000305|PubMed:17190829};
DE AltName: Full=Protein REPRESSOR OF LRX1 1 {ECO:0000303|PubMed:18567791};
DE AltName: Full=Rhamnose biosynthetic enzyme 1;
DE Short=AtRHM1;
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=RHM1 {ECO:0000303|PubMed:15134748};
GN Synonyms=ROL1 {ECO:0000303|PubMed:18567791}; OrderedLocusNames=At1g78570;
GN ORFNames=T30F21.10;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 [5]
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 [6]
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 [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 TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-283.
RX PubMed=16766693; DOI=10.1105/tpc.105.038653;
RA Diet A., Link B., Seifert G.J., Schellenberg B., Wagner U., Pauly M.,
RA Reiter W.D., Ringli C.;
RT "The Arabidopsis root hair cell wall formation mutant lrx1 is suppressed by
RT mutations in the RHM1 gene encoding a UDP-L-rhamnose synthase.";
RL Plant Cell 18:1630-1641(2006).
RN [9]
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).
RN [10]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-283.
RX PubMed=18567791; DOI=10.1105/tpc.107.053249;
RA Ringli C., Bigler L., Kuhn B.M., Leiber R.M., Diet A., Santelia D.,
RA Frey B., Pollmann S., Klein M.;
RT "The modified flavonol glycosylation profile in the Arabidopsis rol1
RT mutants results in alterations in plant growth and cell shape formation.";
RL Plant Cell 20:1470-1481(2008).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF ARG-283.
RX PubMed=18757557; DOI=10.1105/tpc.108.058040;
RA Yonekura-Sakakibara K., Tohge T., Matsuda F., Nakabayashi R., Takayama H.,
RA Niida R., Watanabe-Takahashi A., Inoue E., Saito K.;
RT "Comprehensive flavonol profiling and transcriptome coexpression analysis
RT leading to decoding gene-metabolite correlations in Arabidopsis.";
RL Plant Cell 20:2160-2176(2008).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19056285; DOI=10.1016/j.plaphy.2008.10.011;
RA Wang J., Ji Q., Jiang L., Shen S., Fan Y., Zhang C.;
RT "Overexpression of a cytosol-localized rhamnose biosynthesis protein
RT encoded by Arabidopsis RHM1 gene increases rhamnose content in cell wall.";
RL Plant Physiol. Biochem. 47:86-93(2009).
RN [13]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21502189; DOI=10.1104/pp.111.175976;
RA Kuhn B.M., Geisler M., Bigler L., Ringli C.;
RT "Flavonols accumulate asymmetrically and affect auxin transport in
RT Arabidopsis.";
RL Plant Physiol. 156:585-595(2011).
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:14671019, PubMed:17190829, PubMed:19056285). Plays a major role
CC in supplying UDP-rhamnose for flavonol biosynthesis (PubMed:18757557).
CC Catalyzes the dehydration of UDP-glucose to form UDP-4-dehydro-6-deoxy-
CC D-glucose followed by the epimerization of the C3' and C5' positions of
CC UDP-4-dehydro-6-deoxy-D-glucose to form UDP-4-keto-beta-L-rhamnose and
CC the reduction of UDP-4-keto-beta-L-rhamnose to yield UDP-beta-L-
CC rhamnose (By similarity). {ECO:0000250|UniProtKB:Q9LPG6,
CC ECO:0000269|PubMed:14671019, ECO:0000269|PubMed:17190829,
CC ECO:0000269|PubMed:18757557, ECO:0000269|PubMed:19056285}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19056285,
CC ECO:0000269|PubMed:21502189}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, seedlings,
CC inflorescence tips, and siliques. Detected in the adaxial side of
CC cotyledons, in the emerging leaves and in trichomes. Also detected in
CC the root tip, more precisely in the epidermal cells in the meristematic
CC and elongation zone. {ECO:0000269|PubMed:14671019,
CC ECO:0000269|PubMed:14701918, ECO:0000269|PubMed:16766693,
CC ECO:0000269|PubMed:19056285, ECO:0000269|PubMed:21502189}.
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 -!- DISRUPTION PHENOTYPE: Hyponastic growth, aberrant pavement cell and
CC stomatal morphology in cotyledons, and defective trichome formation.
CC {ECO:0000269|PubMed:18567791}.
CC -!- MISCELLANEOUS: The increased accumulation of auxin in rol1-2 seedlings
CC appears to be caused by a flavonol-induced modification of auxin
CC transport (PubMed:18567791, PubMed:21502189). In bacteria, TDP-L-
CC rhamnose is formed by the successive action of three different enzymes
CC on TDP-D-glucose. In plants, on the other hand, a single polypeptide
CC probably catalyzes all three reactions that lead to the conversion of
CC UDP-D-glucose to UDP-L-rhamnose. {ECO:0000269|PubMed:18567791,
CC ECO:0000269|PubMed:21502189}.
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; AC007260; AAD30579.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36122.1; -; Genomic_DNA.
DR EMBL; AY042833; AAK68773.1; -; mRNA.
DR EMBL; AY081471; AAM10033.1; -; mRNA.
DR PIR; C96814; C96814.
DR RefSeq; NP_177978.1; NM_106504.4.
DR AlphaFoldDB; Q9SYM5; -.
DR SMR; Q9SYM5; -.
DR BioGRID; 29412; 7.
DR IntAct; Q9SYM5; 2.
DR STRING; 3702.AT1G78570.1; -.
DR iPTMnet; Q9SYM5; -.
DR PaxDb; Q9SYM5; -.
DR PRIDE; Q9SYM5; -.
DR ProteomicsDB; 236182; -.
DR EnsemblPlants; AT1G78570.1; AT1G78570.1; AT1G78570.
DR GeneID; 844193; -.
DR Gramene; AT1G78570.1; AT1G78570.1; AT1G78570.
DR KEGG; ath:AT1G78570; -.
DR Araport; AT1G78570; -.
DR TAIR; locus:2202960; AT1G78570.
DR eggNOG; KOG0747; Eukaryota.
DR HOGENOM; CLU_026813_1_0_1; -.
DR InParanoid; Q9SYM5; -.
DR OMA; IRTYPHY; -.
DR OrthoDB; 848823at2759; -.
DR PhylomeDB; Q9SYM5; -.
DR BioCyc; ARA:AT1G78570-MON; -.
DR BioCyc; MetaCyc:AT1G78570-MON; -.
DR PRO; PR:Q9SYM5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYM5; baseline and differential.
DR Genevisible; Q9SYM5; AT.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; 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; IDA:TAIR.
DR GO; GO:0010280; F:UDP-L-rhamnose synthase activity; IDA:TAIR.
DR GO; GO:0010315; P:auxin export across the plasma membrane; IMP:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IMP:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0051555; P:flavonol biosynthetic process; IMP:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
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.
DR TIGRFAMs; TIGR01181; dTDP_gluc_dehyt; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Cytoplasm; Isomerase; Lyase;
KW Multifunctional enzyme; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..669
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 RHM1"
FT /id="PRO_0000183252"
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 391..397
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LPG6"
FT MUTAGEN 283
FT /note="R->K: In rol1-2; Abolishes dehydratase activity in
FT vitro (PubMed:16766693). Induces aberrant accumulation of
FT flavonols leading to alterations in plant growth and cell
FT shape formation (PubMed:18567791, PubMed:18757557)."
FT /evidence="ECO:0000269|PubMed:16766693,
FT ECO:0000269|PubMed:18567791, ECO:0000269|PubMed:18757557"
SQ SEQUENCE 669 AA; 75372 MW; FB8DF9C864F176D4 CRC64;
MASYTPKNIL ITGAAGFIAS HVANRLIRSY PDYKIVVLDK LDYCSNLKNL NPSKHSPNFK
FVKGDIASAD LVNHLLITEG IDTIMHFAAQ THVDNSFGNS FEFTKNNIYG THVLLEACKV
TGQIRRFIHV STDEVYGETD EDALVGNHEA SQLLPTNPYS ATKAGAEMLV MAYGRSYGLP
VITTRGNNVY GPNQFPEKLI PKFILLAMRG QVLPIHGDGS NVRSYLYCED VAEAFEVVLH
KGEVGHVYNI GTKKERRVND VAKDICKLFN MDPEANIKFV DNRPFNDQRY FLDDQKLKKL
GWSERTTWEE GLKKTMDWYT QNPEWWGDVS GALLPHPRML MMPGGRHFDG SEDNSLAATL
SEKPSQTHMV VPSQRSNGTP QKPSLKFLIY GKTGWIGGLL GKICDKQGIA YEYGKGRLED
RSSLLQDIQS VKPTHVFNSA GVTGRPNVDW CESHKTETIR ANVAGTLTLA DVCREHGLLM
MNFATGCIFE YDDKHPEGSG IGFKEEDTPN FTGSFYSKTK AMVEELLKEY DNVCTLRVRM
PISSDLNNPR NFITKISRYN KVVNIPNSMT VLDELLPISI EMAKRNLKGI WNFTNPGVVS
HNEILEMYRD YINPEFKWAN FTLEEQAKVI VAPRSNNEMD ASKLKKEFPE LLSIKESLIK
YAYGPNKKT
