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Entry version 131 (11 Dec 2019)
Sequence version 1 (01 Oct 2000)
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Protein

Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM2

Gene

RHM2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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).2 Publications

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.
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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 2860 sec(-1) with UDP-glucose as substrate.
  1. KM=116 µM for UDP-glucose1 Publication

    pH dependencei

    Optimum pH is 7.5.1 Publication

    Temperature dependencei

    Optimum temperature is 35 degrees Celsius.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Carbohydrate biosynthesis

    This protein is involved in Carbohydrate biosynthesis.Curated
    View all proteins of this organism that are known to be involved in Carbohydrate biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei134SubstrateBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei135Proton donorBy similarity1
    Active sitei136Proton acceptorBy similarity1
    Active sitei161Proton acceptorBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi15 – 21NADSequence analysis7
    Nucleotide bindingi389 – 395NADP1 Publication7

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionIsomerase, Lyase, Multifunctional enzyme, Oxidoreductase
    LigandNAD, NADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:AT1G53500-MONOMER

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM21 Publication
    Alternative name(s):
    NDP-rhamnose synthase
    Protein MUCILAGE-MODIFIED 4
    Protein RHAMNOSE BIOSYNTHESIS 2
    Rhamnose biosynthetic enzyme 2
    Short name:
    AtRHM2
    UDP-L-rhamnose synthase MUM4
    Including the following 2 domains:
    UDP-glucose 4,6-dehydratase1 Publication (EC:4.2.1.761 Publication)
    UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose 4-keto-reductase1 Publication (EC:1.1.1.-1 Publication, EC:5.1.3.-1 Publication)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:RHM21 Publication
    Synonyms:MUM41 Publication
    Ordered Locus Names:At1g53500
    ORF Names:F22G10.13, T3F20.18
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiArabidopsis thaliana (Mouse-ear cress)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri3702 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000006548 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

    Organism-specific databases

    Arabidopsis Information Portal

    More...
    Araporti
    AT1G53500

    The Arabidopsis Information Resource

    More...
    TAIRi
    locus:2024902 AT1G53500

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi18G → A: Abolishes dehydratase activity. 1 Publication1
    Mutagenesisi36K → A: Reduces dehydratase activity. 1 Publication1
    Mutagenesisi96D → N in mum4-1; no extruded mucilage and seed coat defects. Abolishes dehydratase activity. 2 Publications1
    Mutagenesisi165K → A: Abolishes dehydratase activity. 1 Publication1
    Mutagenesisi193G → R in mum4-2; no extruded mucilage and seed coat defects. Abolishes dehydratase activity. 2 Publications1
    Mutagenesisi392G → A: No effect on dehydratase activity. 1 Publication1
    Mutagenesisi413K → A: No effect on dehydratase activity. 1 Publication1
    Mutagenesisi518K → A: No effect on dehydratase activity. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001832531 – 667Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM2Add BLAST667

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    Q9LPG6

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9LPG6

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q9LPG6

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Expressed in roots, stems, leaves, seedlings, inflorescence tips, and siliques.1 Publication

    <p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

    Up-regulated at the time of mucilage production during seed coat differentiation.1 Publication

    Gene expression databases

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q9LPG6 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q9LPG6 AT

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    27010, 3 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    3702.AT1G53500.1

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q9LPG6

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The dehydratase activity is contained in the N-terminal region while the epimerase and reductase activities are in the C-terminal region.1 Publication

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    In the C-terminal section; belongs to the dTDP-4-dehydrorhamnose reductase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0747 Eukaryota
    COG1088 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000167988

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9LPG6

    KEGG Orthology (KO)

    More...
    KOi
    K12450

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    ERTTWED

    Database of Orthologous Groups

    More...
    OrthoDBi
    848823at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q9LPG6

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd05246 dTDP_GD_SDR_e, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR005888 dTDP_Gluc_deHydtase
    IPR016040 NAD(P)-bd_dom
    IPR036291 NAD(P)-bd_dom_sf
    IPR029903 RmlD-like-bd

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF16363 GDP_Man_Dehyd, 1 hit
    PF04321 RmlD_sub_bind, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735 SSF51735, 2 hits

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01181 dTDP_gluc_dehyt, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    Q9LPG6-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MDDTTYKPKN ILITGAAGFI ASHVANRLIR NYPDYKIVVL DKLDYCSDLK
    60 70 80 90 100
    NLDPSFSSPN FKFVKGDIAS DDLVNYLLIT ENIDTIMHFA AQTHVDNSFG
    110 120 130 140 150
    NSFEFTKNNI YGTHVLLEAC KVTGQIRRFI HVSTDEVYGE TDEDAAVGNH
    160 170 180 190 200
    EASQLLPTNP YSATKAGAEM LVMAYGRSYG LPVITTRGNN VYGPNQFPEK
    210 220 230 240 250
    MIPKFILLAM SGKPLPIHGD GSNVRSYLYC EDVAEAFEVV LHKGEIGHVY
    260 270 280 290 300
    NVGTKRERRV IDVARDICKL FGKDPESSIQ FVENRPFNDQ RYFLDDQKLK
    310 320 330 340 350
    KLGWQERTNW EDGLKKTMDW YTQNPEWWGD VSGALLPHPR MLMMPGGRLS
    360 370 380 390 400
    DGSSEKKDVS SNTVQTFTVV TPKNGDSGDK ASLKFLIYGK TGWLGGLLGK
    410 420 430 440 450
    LCEKQGITYE YGKGRLEDRA SLVADIRSIK PTHVFNAAGL TGRPNVDWCE
    460 470 480 490 500
    SHKPETIRVN VAGTLTLADV CRENDLLMMN FATGCIFEYD ATHPEGSGIG
    510 520 530 540 550
    FKEEDKPNFF GSFYSKTKAM VEELLREFDN VCTLRVRMPI SSDLNNPRNF
    560 570 580 590 600
    ITKISRYNKV VDIPNSMTVL DELLPISIEM AKRNLRGIWN FTNPGVVSHN
    610 620 630 640 650
    EILEMYKNYI EPGFKWSNFT VEEQAKVIVA ARSNNEMDGS KLSKEFPEML
    660
    SIKESLLKYV FEPNKRT
    Length:667
    Mass (Da):75,226
    Last modified:October 1, 2000 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9F45A7B043BD2044
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AJ565874 mRNA Translation: CAD92667.1
    AY328518 mRNA Translation: AAP93963.1
    AC018748 Genomic DNA Translation: AAF78439.1
    AC024260 Genomic DNA Translation: AAG51981.1
    CP002684 Genomic DNA Translation: AEE32949.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    B96575

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_564633.2, NM_104228.3

    Genome annotation databases

    Ensembl plant genome annotation project

    More...
    EnsemblPlantsi
    AT1G53500.1; AT1G53500.1; AT1G53500

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    841785

    Gramene; a comparative resource for plants

    More...
    Gramenei
    AT1G53500.1; AT1G53500.1; AT1G53500

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ath:AT1G53500

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ565874 mRNA Translation: CAD92667.1
    AY328518 mRNA Translation: AAP93963.1
    AC018748 Genomic DNA Translation: AAF78439.1
    AC024260 Genomic DNA Translation: AAG51981.1
    CP002684 Genomic DNA Translation: AEE32949.1
    PIRiB96575
    RefSeqiNP_564633.2, NM_104228.3

    3D structure databases

    SMRiQ9LPG6
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi27010, 3 interactors
    STRINGi3702.AT1G53500.1

    PTM databases

    iPTMnetiQ9LPG6

    Proteomic databases

    PaxDbiQ9LPG6
    PRIDEiQ9LPG6

    Genome annotation databases

    EnsemblPlantsiAT1G53500.1; AT1G53500.1; AT1G53500
    GeneIDi841785
    GrameneiAT1G53500.1; AT1G53500.1; AT1G53500
    KEGGiath:AT1G53500

    Organism-specific databases

    AraportiAT1G53500
    TAIRilocus:2024902 AT1G53500

    Phylogenomic databases

    eggNOGiKOG0747 Eukaryota
    COG1088 LUCA
    HOGENOMiHOG000167988
    InParanoidiQ9LPG6
    KOiK12450
    OMAiERTTWED
    OrthoDBi848823at2759
    PhylomeDBiQ9LPG6

    Enzyme and pathway databases

    BioCyciMetaCyc:AT1G53500-MONOMER

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:Q9LPG6

    Gene expression databases

    ExpressionAtlasiQ9LPG6 baseline and differential
    GenevisibleiQ9LPG6 AT

    Family and domain databases

    CDDicd05246 dTDP_GD_SDR_e, 1 hit
    InterProiView protein in InterPro
    IPR005888 dTDP_Gluc_deHydtase
    IPR016040 NAD(P)-bd_dom
    IPR036291 NAD(P)-bd_dom_sf
    IPR029903 RmlD-like-bd
    PfamiView protein in Pfam
    PF16363 GDP_Man_Dehyd, 1 hit
    PF04321 RmlD_sub_bind, 1 hit
    SUPFAMiSSF51735 SSF51735, 2 hits
    TIGRFAMsiTIGR01181 dTDP_gluc_dehyt, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRHM2_ARATH
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9LPG6
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: October 1, 2000
    Last modified: December 11, 2019
    This is version 131 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
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