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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 RHM2 (NDP-rhamnose synthase) (Protein MUCILAGE-MODIFIED 4) (Protein RHAMNOSE BIOSYNTHESIS 2) (Rhamnose biosynthetic enzyme 2) (AtRHM2) (UDP-L-rhamnose synthase MUM4) [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.-)]

 RHM2_ARATH              Reviewed;         667 AA.
Q9LPG6;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 122.
RecName: Full=Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM2 {ECO:0000305|PubMed:17190829};
AltName: Full=NDP-rhamnose synthase;
AltName: Full=Protein MUCILAGE-MODIFIED 4;
AltName: Full=Protein RHAMNOSE BIOSYNTHESIS 2;
AltName: Full=Rhamnose biosynthetic enzyme 2;
Short=AtRHM2;
AltName: Full=UDP-L-rhamnose synthase MUM4;
Includes:
RecName: Full=UDP-glucose 4,6-dehydratase {ECO:0000303|PubMed:17190829};
EC=4.2.1.76 {ECO:0000269|PubMed:17190829};
Includes:
RecName: Full=UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose 4-keto-reductase {ECO:0000303|PubMed:17190829};
EC=1.1.1.- {ECO:0000269|PubMed:17190829};
EC=5.1.3.- {ECO:0000269|PubMed:17190829};
Name=RHM2 {ECO:0000303|PubMed:15134748};
Synonyms=MUM4 {ECO:0000303|PubMed:14701918};
OrderedLocusNames=At1g53500; ORFNames=F22G10.13, T3F20.18;
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 [MRNA], MUTAGENESIS OF ASP-96 AND GLY-193,
FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
STRAIN=cv. Col-2, and cv. Landsberg erecta;
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).
[3]
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).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
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).
[7]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
DOMAIN, AND MUTAGENESIS OF GLY-18; LYS-36; ASP-96; LYS-165; GLY-193;
GLY-392; LYS-413 AND LYS-518.
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).
-!- 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).
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 (PubMed:17190829). Required for the
normal seed coat epidermal development (PubMed:14671019).
{ECO:0000269|PubMed:14671019, ECO:0000269|PubMed:17190829}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose = UDP-4-dehydro-6-deoxy-
alpha-D-glucose + H(2)O. {ECO:0000269|PubMed:17190829}.
-!- COFACTOR:
Name=NAD(+); Xref=ChEBI:CHEBI:57540;
Evidence={ECO:0000305|PubMed:17190829};
-!- COFACTOR:
Name=NADP(+); Xref=ChEBI:CHEBI:58349;
Evidence={ECO:0000305|PubMed:17190829};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=116 uM for UDP-glucose {ECO:0000269|PubMed:17190829};
Note=kcat is 2860 sec(-1) with UDP-glucose as substrate.;
pH dependence:
Optimum pH is 7.5. {ECO:0000269|PubMed:17190829};
Temperature dependence:
Optimum temperature is 35 degrees Celsius.
{ECO:0000269|PubMed:17190829};
-!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, seedlings,
inflorescence tips, and siliques. {ECO:0000269|PubMed:14671019}.
-!- DEVELOPMENTAL STAGE: Up-regulated at the time of mucilage
production during seed coat differentiation.
{ECO:0000269|PubMed:14701918}.
-!- DOMAIN: The dehydratase activity is contained in the N-terminal
region while the epimerase and reductase activities are in the C-
terminal region. {ECO:0000269|PubMed:17190829}.
-!- MISCELLANEOUS: 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.
-!- MISCELLANEOUS: RHM2 appears to be more highly expressed in cv.
Landsberg erecta than in cv. Col-2. Transcriptions factors AP2,
TTG1, and GL2 are required for maximum levels of RHM2 expression
at the time of mucilage production.
-!- 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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EMBL; AJ565874; CAD92667.1; -; mRNA.
EMBL; AY328518; AAP93963.1; -; mRNA.
EMBL; AC018748; AAF78439.1; -; Genomic_DNA.
EMBL; AC024260; AAG51981.1; -; Genomic_DNA.
EMBL; CP002684; AEE32949.1; -; Genomic_DNA.
PIR; B96575; B96575.
RefSeq; NP_564633.2; NM_104228.3.
UniGene; At.20215; -.
ProteinModelPortal; Q9LPG6; -.
SMR; Q9LPG6; -.
BioGrid; 27010; 3.
MINT; MINT-8067929; -.
STRING; 3702.AT1G53500.1; -.
iPTMnet; Q9LPG6; -.
PaxDb; Q9LPG6; -.
PRIDE; Q9LPG6; -.
EnsemblPlants; AT1G53500.1; AT1G53500.1; AT1G53500.
GeneID; 841785; -.
Gramene; AT1G53500.1; AT1G53500.1; AT1G53500.
KEGG; ath:AT1G53500; -.
Araport; AT1G53500; -.
TAIR; locus:2024902; AT1G53500.
eggNOG; KOG0747; Eukaryota.
eggNOG; COG1088; LUCA.
HOGENOM; HOG000167988; -.
InParanoid; Q9LPG6; -.
KO; K12450; -.
OMA; ERTTWED; -.
OrthoDB; EOG093603H9; -.
PhylomeDB; Q9LPG6; -.
BioCyc; MetaCyc:AT1G53500-MONOMER; -.
PRO; PR:Q9LPG6; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9LPG6; baseline and differential.
Genevisible; Q9LPG6; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:InterPro.
GO; GO:0010489; F:UDP-4-keto-6-deoxy-glucose-3,5-epimerase activity; TAS:TAIR.
GO; GO:0010490; F:UDP-4-keto-rhamnose-4-keto-reductase activity; TAS:TAIR.
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:0010192; P:mucilage biosynthetic process; IMP:TAIR.
GO; GO:0010214; P:seed coat development; IMP:TAIR.
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;
Complete proteome; Isomerase; Lyase; Multifunctional enzyme; NAD;
NADP; Oxidoreductase; Reference proteome.
CHAIN 1 667 Trifunctional UDP-glucose 4,6-
dehydratase/UDP-4-keto-6-deoxy-D-glucose
3,5-epimerase/UDP-4-keto-L-rhamnose-
reductase RHM2.
/FTId=PRO_0000183253.
NP_BIND 15 21 NAD. {ECO:0000255}.
NP_BIND 389 395 NADP. {ECO:0000305|PubMed:17190829}.
ACT_SITE 135 135 Proton donor. {ECO:0000250}.
ACT_SITE 136 136 Proton acceptor. {ECO:0000250}.
ACT_SITE 161 161 Proton acceptor. {ECO:0000250}.
BINDING 134 134 Substrate. {ECO:0000250}.
MUTAGEN 18 18 G->A: Abolishes dehydratase activity.
{ECO:0000269|PubMed:17190829}.
MUTAGEN 36 36 K->A: Reduces dehydratase activity.
{ECO:0000269|PubMed:17190829}.
MUTAGEN 96 96 D->N: In mum4-1; no extruded mucilage and
seed coat defects. Abolishes dehydratase
activity. {ECO:0000269|PubMed:14671019,
ECO:0000269|PubMed:17190829}.
MUTAGEN 165 165 K->A: Abolishes dehydratase activity.
{ECO:0000269|PubMed:17190829}.
MUTAGEN 193 193 G->R: In mum4-2; no extruded mucilage and
seed coat defects. Abolishes dehydratase
activity. {ECO:0000269|PubMed:14671019,
ECO:0000269|PubMed:17190829}.
MUTAGEN 392 392 G->A: No effect on dehydratase activity.
{ECO:0000269|PubMed:17190829}.
MUTAGEN 413 413 K->A: No effect on dehydratase activity.
{ECO:0000269|PubMed:17190829}.
MUTAGEN 518 518 K->A: No effect on dehydratase activity.
{ECO:0000269|PubMed:17190829}.
SEQUENCE 667 AA; 75226 MW; 9F45A7B043BD2044 CRC64;
MDDTTYKPKN ILITGAAGFI ASHVANRLIR NYPDYKIVVL DKLDYCSDLK NLDPSFSSPN
FKFVKGDIAS DDLVNYLLIT ENIDTIMHFA AQTHVDNSFG NSFEFTKNNI YGTHVLLEAC
KVTGQIRRFI HVSTDEVYGE TDEDAAVGNH EASQLLPTNP YSATKAGAEM LVMAYGRSYG
LPVITTRGNN VYGPNQFPEK MIPKFILLAM SGKPLPIHGD GSNVRSYLYC EDVAEAFEVV
LHKGEIGHVY NVGTKRERRV IDVARDICKL FGKDPESSIQ FVENRPFNDQ RYFLDDQKLK
KLGWQERTNW EDGLKKTMDW YTQNPEWWGD VSGALLPHPR MLMMPGGRLS DGSSEKKDVS
SNTVQTFTVV TPKNGDSGDK ASLKFLIYGK TGWLGGLLGK LCEKQGITYE YGKGRLEDRA
SLVADIRSIK PTHVFNAAGL TGRPNVDWCE SHKPETIRVN VAGTLTLADV CRENDLLMMN
FATGCIFEYD ATHPEGSGIG FKEEDKPNFF GSFYSKTKAM VEELLREFDN VCTLRVRMPI
SSDLNNPRNF ITKISRYNKV VDIPNSMTVL DELLPISIEM AKRNLRGIWN FTNPGVVSHN
EILEMYKNYI EPGFKWSNFT VEEQAKVIVA ARSNNEMDGS KLSKEFPEML SIKESLLKYV
FEPNKRT


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