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Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM1 (Protein REPRESSOR OF LRX1 1) (Rhamnose biosynthetic enzyme 1) (AtRHM1) [Includes: UDP-glucose 4,6-dehydratase (EC 4.2.1.76); UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose 4-keto-reductase (EC 1.1.1.-) (EC 5.1.3.-)]

 RHM1_ARATH              Reviewed;         669 AA.
Q9SYM5;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-APR-2018, entry version 135.
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};
AltName: Full=Protein REPRESSOR OF LRX1 1 {ECO:0000303|PubMed:18567791};
AltName: Full=Rhamnose biosynthetic enzyme 1;
Short=AtRHM1;
Includes:
RecName: Full=UDP-glucose 4,6-dehydratase {ECO:0000305|PubMed:17190829};
EC=4.2.1.76 {ECO:0000305|PubMed:17190829};
Includes:
RecName: Full=UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose 4-keto-reductase {ECO:0000305|PubMed:17190829};
EC=1.1.1.- {ECO:0000305|PubMed:17190829};
EC=5.1.3.- {ECO:0000305|PubMed:17190829};
Name=RHM1 {ECO:0000303|PubMed:15134748};
Synonyms=ROL1 {ECO:0000303|PubMed:18567791};
OrderedLocusNames=At1g78570; ORFNames=T30F21.10;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
IDENTIFICATION.
PubMed=11554483; DOI=10.1023/A:1010671129803;
Reiter W.-D., Vanzin G.F.;
"Molecular genetics of nucleotide sugar interconversion pathways in
plants.";
Plant Mol. Biol. 47:95-113(2001).
[5]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14671019; DOI=10.1104/pp.103.034314;
Usadel B., Kuschinsky A.M., Rosso M.G., Eckermann N., Pauly M.;
"RHM2 is involved in mucilage pectin synthesis and is required for the
development of the seed coat in Arabidopsis.";
Plant Physiol. 134:286-295(2004).
[6]
TISSUE SPECIFICITY.
STRAIN=cv. Col-2;
PubMed=14701918; DOI=10.1104/pp.103.035519;
Western T.L., Young D.S., Dean G.H., Tan W.L., Samuels A.L.,
Haughn G.W.;
"MUCILAGE-MODIFIED4 encodes a putative pectin biosynthetic enzyme
developmentally regulated by APETALA2, TRANSPARENT TESTA GLABRA1, and
GLABRA2 in the Arabidopsis seed coat.";
Plant Physiol. 134:296-306(2004).
[7]
REVIEW, AND NOMENCLATURE.
PubMed=15134748; DOI=10.1016/j.pbi.2004.03.004;
Seifert G.J.;
"Nucleotide sugar interconversions and cell wall biosynthesis: how to
bring the inside to the outside.";
Curr. Opin. Plant Biol. 7:277-284(2004).
[8]
TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-283.
PubMed=16766693; DOI=10.1105/tpc.105.038653;
Diet A., Link B., Seifert G.J., Schellenberg B., Wagner U., Pauly M.,
Reiter W.D., Ringli C.;
"The Arabidopsis root hair cell wall formation mutant lrx1 is
suppressed by mutations in the RHM1 gene encoding a UDP-L-rhamnose
synthase.";
Plant Cell 18:1630-1641(2006).
[9]
FUNCTION.
PubMed=17190829; DOI=10.1074/jbc.M610196200;
Oka T., Nemoto T., Jigami Y.;
"Functional analysis of Arabidopsis thaliana RHM2/MUM4, a multidomain
protein involved in UDP-D-glucose to UDP-L-rhamnose conversion.";
J. Biol. Chem. 282:5389-5403(2007).
[10]
DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-283.
PubMed=18567791; DOI=10.1105/tpc.107.053249;
Ringli C., Bigler L., Kuhn B.M., Leiber R.M., Diet A., Santelia D.,
Frey B., Pollmann S., Klein M.;
"The modified flavonol glycosylation profile in the Arabidopsis rol1
mutants results in alterations in plant growth and cell shape
formation.";
Plant Cell 20:1470-1481(2008).
[11]
FUNCTION, AND MUTAGENESIS OF ARG-283.
PubMed=18757557; DOI=10.1105/tpc.108.058040;
Yonekura-Sakakibara K., Tohge T., Matsuda F., Nakabayashi R.,
Takayama H., Niida R., Watanabe-Takahashi A., Inoue E., Saito K.;
"Comprehensive flavonol profiling and transcriptome coexpression
analysis leading to decoding gene-metabolite correlations in
Arabidopsis.";
Plant Cell 20:2160-2176(2008).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19056285; DOI=10.1016/j.plaphy.2008.10.011;
Wang J., Ji Q., Jiang L., Shen S., Fan Y., Zhang C.;
"Overexpression of a cytosol-localized rhamnose biosynthesis protein
encoded by Arabidopsis RHM1 gene increases rhamnose content in cell
wall.";
Plant Physiol. Biochem. 47:86-93(2009).
[13]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=21502189; DOI=10.1104/pp.111.175976;
Kuhn B.M., Geisler M., Bigler L., Ringli C.;
"Flavonols accumulate asymmetrically and affect auxin transport in
Arabidopsis.";
Plant Physiol. 156:585-595(2011).
-!- FUNCTION: Trifunctional enzyme involved in UDP-beta-L-rhamnose
biosynthesis, a precursor of the primary cell wall components
rhamnogalacturonan I (RG-I) and rhamnogalacturonan II (RG-II)
(PubMed:14671019, PubMed:17190829, PubMed:19056285). Plays a major
role in supplying UDP-rhamnose for flavonol biosynthesis
(PubMed:18757557). Catalyzes the dehydration of UDP-glucose to
form UDP-4-dehydro-6-deoxy-D-glucose followed by the epimerization
of the C3' and C5' positions of UDP-4-dehydro-6-deoxy-D-glucose to
form UDP-4-keto-beta-L-rhamnose and the reduction of UDP-4-keto-
beta-L-rhamnose to yield UDP-beta-L-rhamnose (By similarity).
{ECO:0000250|UniProtKB:Q9LPG6, ECO:0000269|PubMed:14671019,
ECO:0000269|PubMed:17190829, ECO:0000269|PubMed:18757557,
ECO:0000269|PubMed:19056285}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose = UDP-4-dehydro-6-deoxy-
alpha-D-glucose + H(2)O. {ECO:0000250|UniProtKB:Q9LPG6}.
-!- COFACTOR:
Name=NAD(+); Xref=ChEBI:CHEBI:57540;
Evidence={ECO:0000250|UniProtKB:Q9LPG6};
-!- COFACTOR:
Name=NADP(+); Xref=ChEBI:CHEBI:58349;
Evidence={ECO:0000250|UniProtKB:Q9LPG6};
-!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:19056285, ECO:0000269|PubMed:21502189}.
-!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, seedlings,
inflorescence tips, and siliques. Detected in the adaxial side of
cotyledons, in the emerging leaves and in trichomes. Also detected
in the root tip, more precisely in the epidermal cells in the
meristematic and elongation zone. {ECO:0000269|PubMed:14671019,
ECO:0000269|PubMed:14701918, ECO:0000269|PubMed:16766693,
ECO:0000269|PubMed:19056285, ECO:0000269|PubMed:21502189}.
-!- DOMAIN: The dehydratase activity is contained in the N-terminal
region while the epimerase and reductase activities are in the C-
terminal region. {ECO:0000250|UniProtKB:Q9LPG6}.
-!- DISRUPTION PHENOTYPE: Hyponastic growth, aberrant pavement cell
and stomatal morphology in cotyledons, and defective trichome
formation. {ECO:0000269|PubMed:18567791}.
-!- MISCELLANEOUS: The increased accumulation of auxin in rol1-2
seedlings appears to be caused by a flavonol-induced modification
of auxin transport (PubMed:18567791, PubMed:21502189). In
bacteria, TDP-L-rhamnose is formed by the successive action of
three different enzymes on TDP-D-glucose. In plants, on the other
hand, a single polypeptide probably catalyzes all three reactions
that lead to the conversion of UDP-D-glucose to UDP-L-rhamnose.
{ECO:0000269|PubMed:18567791, ECO:0000269|PubMed:21502189}.
-!- SIMILARITY: In the N-terminal section; belongs to the NAD(P)-
dependent epimerase/dehydratase family. dTDP-glucose dehydratase
subfamily. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the dTDP-4-
dehydrorhamnose reductase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AC007260; AAD30579.1; -; Genomic_DNA.
EMBL; CP002684; AEE36122.1; -; Genomic_DNA.
EMBL; AY042833; AAK68773.1; -; mRNA.
EMBL; AY081471; AAM10033.1; -; mRNA.
PIR; C96814; C96814.
RefSeq; NP_177978.1; NM_106504.4.
UniGene; At.198; -.
UniGene; At.71030; -.
ProteinModelPortal; Q9SYM5; -.
SMR; Q9SYM5; -.
BioGrid; 29412; 4.
IntAct; Q9SYM5; 2.
STRING; 3702.AT1G78570.1; -.
iPTMnet; Q9SYM5; -.
PaxDb; Q9SYM5; -.
PRIDE; Q9SYM5; -.
EnsemblPlants; AT1G78570.1; AT1G78570.1; AT1G78570.
GeneID; 844193; -.
Gramene; AT1G78570.1; AT1G78570.1; AT1G78570.
KEGG; ath:AT1G78570; -.
Araport; AT1G78570; -.
TAIR; locus:2202960; AT1G78570.
eggNOG; KOG0747; Eukaryota.
eggNOG; COG1088; LUCA.
HOGENOM; HOG000167988; -.
InParanoid; Q9SYM5; -.
KO; K12450; -.
OMA; DALVGNH; -.
OrthoDB; EOG093603H9; -.
PhylomeDB; Q9SYM5; -.
BioCyc; ARA:AT1G78570-MONOMER; -.
BioCyc; MetaCyc:AT1G78570-MONOMER; -.
PRO; PR:Q9SYM5; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9SYM5; baseline and differential.
Genevisible; Q9SYM5; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:InterPro.
GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
GO; GO:0050377; F:UDP-glucose 4,6-dehydratase activity; IDA:TAIR.
GO; GO:0010280; F:UDP-L-rhamnose synthase activity; IDA:TAIR.
GO; GO:0010315; P:auxin efflux; IMP:UniProtKB.
GO; GO:0030154; P:cell differentiation; IMP:UniProtKB.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0051555; P:flavonol biosynthetic process; IMP:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0010253; P:UDP-rhamnose biosynthetic process; IDA:TAIR.
InterPro; IPR005888; dTDP_Gluc_deHydtase.
InterPro; IPR016040; NAD(P)-bd_dom.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR029903; RmlD-like-bd.
Pfam; PF16363; GDP_Man_Dehyd; 1.
Pfam; PF04321; RmlD_sub_bind; 1.
SUPFAM; SSF51735; SSF51735; 2.
TIGRFAMs; TIGR01181; dTDP_gluc_dehyt; 1.
1: Evidence at protein level;
Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
Isomerase; Lyase; Multifunctional enzyme; NAD; NADP; Oxidoreductase;
Reference proteome.
CHAIN 1 669 Trifunctional UDP-glucose 4,6-
dehydratase/UDP-4-keto-6-deoxy-D-glucose
3,5-epimerase/UDP-4-keto-L-rhamnose-
reductase RHM1.
/FTId=PRO_0000183252.
NP_BIND 13 19 NAD. {ECO:0000255}.
NP_BIND 391 397 NADP. {ECO:0000250|UniProtKB:Q9LPG6}.
ACT_SITE 133 133 Proton donor. {ECO:0000250}.
ACT_SITE 134 134 Proton acceptor. {ECO:0000250}.
ACT_SITE 159 159 Proton acceptor. {ECO:0000250}.
BINDING 132 132 Substrate. {ECO:0000250}.
MUTAGEN 283 283 R->K: In rol1-2; Abolishes dehydratase
activity in vitro (PubMed:16766693).
Induces aberrant accumulation of
flavonols leading to alterations in plant
growth and cell shape formation
(PubMed:18567791, PubMed:18757557).
{ECO:0000269|PubMed:16766693,
ECO:0000269|PubMed:18567791,
ECO:0000269|PubMed:18757557}.
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


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