RHM2_ARATH
ID RHM2_ARATH Reviewed; 667 AA.
AC Q9LPG6;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
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 RHM2 {ECO:0000305|PubMed:17190829};
DE AltName: Full=NDP-rhamnose synthase;
DE AltName: Full=Protein MUCILAGE-MODIFIED 4;
DE AltName: Full=Protein RHAMNOSE BIOSYNTHESIS 2;
DE AltName: Full=Rhamnose biosynthetic enzyme 2;
DE Short=AtRHM2;
DE AltName: Full=UDP-L-rhamnose synthase MUM4;
DE Includes:
DE RecName: Full=UDP-glucose 4,6-dehydratase {ECO:0000303|PubMed:17190829};
DE EC=4.2.1.76 {ECO:0000269|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:0000303|PubMed:17190829};
DE EC=1.1.1.- {ECO:0000269|PubMed:17190829};
DE EC=5.1.3.- {ECO:0000269|PubMed:17190829};
GN Name=RHM2 {ECO:0000303|PubMed:15134748};
GN Synonyms=MUM4 {ECO:0000303|PubMed:14701918}; OrderedLocusNames=At1g53500;
GN ORFNames=F22G10.13, T3F20.18;
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 [MRNA], MUTAGENESIS OF ASP-96 AND GLY-193, FUNCTION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Col-2, and cv. Landsberg erecta;
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP DOMAIN, AND MUTAGENESIS OF GLY-18; LYS-36; ASP-96; LYS-165; GLY-193;
RP GLY-392; LYS-413 AND LYS-518.
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 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 (PubMed:17190829). Required for the normal seed coat epidermal
CC development (PubMed:14671019). {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:0000269|PubMed:17190829};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000305|PubMed:17190829};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000305|PubMed:17190829};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=116 uM for UDP-glucose {ECO:0000269|PubMed:17190829};
CC Note=kcat is 2860 sec(-1) with UDP-glucose as substrate.;
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:17190829};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:17190829};
CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, seedlings,
CC inflorescence tips, and siliques. {ECO:0000269|PubMed:14671019}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated at the time of mucilage production
CC during seed coat differentiation. {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:0000269|PubMed:17190829}.
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 -!- MISCELLANEOUS: RHM2 appears to be more highly expressed in cv.
CC Landsberg erecta than in cv. Col-2. Transcriptions factors AP2, TTG1,
CC and GL2 are required for maximum levels of RHM2 expression at the time
CC of mucilage production.
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; AJ565874; CAD92667.1; -; mRNA.
DR EMBL; AY328518; AAP93963.1; -; mRNA.
DR EMBL; AC018748; AAF78439.1; -; Genomic_DNA.
DR EMBL; AC024260; AAG51981.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32949.1; -; Genomic_DNA.
DR PIR; B96575; B96575.
DR RefSeq; NP_564633.2; NM_104228.3.
DR AlphaFoldDB; Q9LPG6; -.
DR SMR; Q9LPG6; -.
DR BioGRID; 27010; 3.
DR STRING; 3702.AT1G53500.1; -.
DR iPTMnet; Q9LPG6; -.
DR PaxDb; Q9LPG6; -.
DR PRIDE; Q9LPG6; -.
DR ProteomicsDB; 236173; -.
DR EnsemblPlants; AT1G53500.1; AT1G53500.1; AT1G53500.
DR GeneID; 841785; -.
DR Gramene; AT1G53500.1; AT1G53500.1; AT1G53500.
DR KEGG; ath:AT1G53500; -.
DR Araport; AT1G53500; -.
DR TAIR; locus:2024902; AT1G53500.
DR eggNOG; KOG0747; Eukaryota.
DR HOGENOM; CLU_026813_1_0_1; -.
DR InParanoid; Q9LPG6; -.
DR OMA; ERTTWED; -.
DR OrthoDB; 848823at2759; -.
DR PhylomeDB; Q9LPG6; -.
DR BioCyc; ARA:AT1G53500-MON; -.
DR BioCyc; MetaCyc:AT1G53500-MON; -.
DR PRO; PR:Q9LPG6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPG6; baseline and differential.
DR Genevisible; Q9LPG6; AT.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:InterPro.
DR GO; GO:0010489; F:UDP-4-keto-6-deoxy-glucose-3,5-epimerase activity; TAS:TAIR.
DR GO; GO:0010490; F:UDP-4-keto-rhamnose-4-keto-reductase activity; TAS:TAIR.
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; IBA:GO_Central.
DR GO; GO:0051555; P:flavonol biosynthetic process; IBA:GO_Central.
DR GO; GO:0010192; P:mucilage biosynthetic process; IMP:TAIR.
DR GO; GO:0010214; P:seed coat development; IMP:TAIR.
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 Isomerase; Lyase; Multifunctional enzyme; NAD; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..667
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 RHM2"
FT /id="PRO_0000183253"
FT ACT_SITE 135
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 15..21
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 389..395
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000305|PubMed:17190829"
FT MUTAGEN 18
FT /note="G->A: Abolishes dehydratase activity."
FT /evidence="ECO:0000269|PubMed:17190829"
FT MUTAGEN 36
FT /note="K->A: Reduces dehydratase activity."
FT /evidence="ECO:0000269|PubMed:17190829"
FT MUTAGEN 96
FT /note="D->N: In mum4-1; no extruded mucilage and seed coat
FT defects. Abolishes dehydratase activity."
FT /evidence="ECO:0000269|PubMed:14671019,
FT ECO:0000269|PubMed:17190829"
FT MUTAGEN 165
FT /note="K->A: Abolishes dehydratase activity."
FT /evidence="ECO:0000269|PubMed:17190829"
FT MUTAGEN 193
FT /note="G->R: In mum4-2; no extruded mucilage and seed coat
FT defects. Abolishes dehydratase activity."
FT /evidence="ECO:0000269|PubMed:14671019,
FT ECO:0000269|PubMed:17190829"
FT MUTAGEN 392
FT /note="G->A: No effect on dehydratase activity."
FT /evidence="ECO:0000269|PubMed:17190829"
FT MUTAGEN 413
FT /note="K->A: No effect on dehydratase activity."
FT /evidence="ECO:0000269|PubMed:17190829"
FT MUTAGEN 518
FT /note="K->A: No effect on dehydratase activity."
FT /evidence="ECO:0000269|PubMed:17190829"
SQ 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
