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UniProtKB - P32171 (RHAB_ECOLI)

Entry version 136 (16 Oct 2019)
Sequence version 1 (01 Oct 1993)
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Protein

L-Rhamnulokinase

Gene

rhaB

Organism
Escherichia coli (strain K12)
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

Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). It could also play a role in the metabolism of some rare sugars such as L-fructose. Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate. Uridine triphosphate (UTP), cytidine 5-triphosphate (CTP), guanosine 5-triphosphate (GTP), and thymidine triphosphate (TTP) also can act as phosphoryl donors. It can also phosphorylate L-fuculose and L-xylulose.UniRule annotation3 Publications

<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

Mg2+UniRule annotation1 PublicationNote: It can also use manganese, cobalt, iron, calcium and copper ions.1 Publication

<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

  1. KM=82 µM for L-rhamnulose (at pH 8.5 and 37 degrees Celsius)1 Publication
  2. KM=110 µM for ATP (at pH 8.5 and 37 degrees Celsius)1 Publication
  3. KM=270 µM for magnesium ion (at pH 8.5 and 37 degrees Celsius)1 Publication
  4. KM=3 mM for beta-L-fructose (at pH 8)1 Publication

    pH dependencei

    Optimum pH is 8.5.1 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: L-rhamnose degradation

    This protein is involved in step 2 of the subpathway that synthesizes glycerone phosphate from L-rhamnose.UniRule annotation
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. L-rhamnose isomerase (rhaA), L-rhamnose isomerase (rhaA), L-rhamnose isomerase (rhaA), L-rhamnose isomerase (rhaA), L-rhamnose isomerase (rhaA)
    2. Rhamnulokinase (rhaB), Rhamnulokinase (rhaB), Rhamnulokinase (rhaB), Rhamnulokinase (rhaB), L-Rhamnulokinase (rhaB)
    3. Rhamnulose-1-phosphate aldolase (rhaD), Rhamnulose-1-phosphate aldolase (rhaD), Rhamnulose-1-phosphate aldolase (rhaD), Rhamnulose-1-phosphate aldolase (rhaD), Rhamnulose-1-phosphate aldolase (rhaD)
    This subpathway is part of the pathway L-rhamnose degradation, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes glycerone phosphate from L-rhamnose, the pathway L-rhamnose degradation and in Carbohydrate degradation.

    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 sitei83Substrate; via amide nitrogen and carbonyl oxygenUniRule annotation1 Publication1
    <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 sitei237Proton acceptorUniRule annotation1 Publication1
    Binding sitei259ATPUniRule annotation1 Publication1
    Binding sitei296SubstrateUniRule annotation1 Publication1
    Binding sitei304ATPUniRule annotation1 Publication1
    Binding sitei402ATP; via amide nitrogenUniRule annotation1 Publication1

    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 bindingi13 – 17ATPUniRule annotation1 Publication5

    <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

    • ATP binding Source: UniProtKB
    • rhamnulokinase activity Source: UniProtKB
    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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 functionKinase, Transferase
    Biological processRhamnose metabolism
    LigandATP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:RHAMNULOKIN-MONOMER
    ECOL316407:JW3875-MONOMER
    MetaCyc:RHAMNULOKIN-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		2.7.1.5 2026

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...    UniPathwayi    		UPA00541;UER00602

    <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:
    L-Rhamnulokinase1 PublicationUniRule annotation (EC:2.7.1.5UniRule annotation2 Publications)
    Short name:
    RhaB1 PublicationUniRule annotation
    Short name:
    RhuK1 Publication
    Alternative name(s):
    ATP:L-rhamnulose phosphotransferase1 PublicationUniRule annotation
    L-rhamnulose 1-kinase1 PublicationUniRule annotation
    Rhamnulose kinase1 PublicationUniRule annotation
    <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:rhaB1 PublicationUniRule annotation
    Ordered Locus Names:b3904, JW3875
    <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>OrganismiEscherichia coli (strain K12)
    <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 identifieri83333 [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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <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
    • UP000000318 <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
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...    EcoGenei    		EG11868 rhaB

    <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

    GO - Cellular componenti

    • cytosol Source: GO_Central
    Complete GO annotation on QuickGO ...

    <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

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Cells lacking this gene are unable to utilize rhamnose as a source of carbon.1 Publication

    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>Mutagenesisi69E → A: Same kinase activity as the wild-type; when associated with A-70 and A-73. 1 Publication1
    Mutagenesisi70E → A: Same kinase activity as the wild-type; when associated with A-69 and A-73. 1 Publication1
    Mutagenesisi73R → A: Same kinase activity as the wild-type; when associated with A-69 and A-70. 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_00000905311 – 489L-RhamnulokinaseAdd BLAST489

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi68 ↔ 222UniRule annotation1 Publication
    Disulfide bondi353 ↔ 370UniRule annotation1 Publication
    Disulfide bondi413 ↔ 417UniRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

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

    More...    PaxDbi    		P32171

    PRoteomics IDEntifications database

    More...    PRIDEi    		P32171

    <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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Induced by L-rhamnose via the RhaR-RhaS regulatory cascade. Binding of the cAMP receptor protein (CRP) is required for full expression. Also induced by L-lyxose.3 Publications

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer.

    UniRule annotation1 Publication

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...    IntActi    		P32171, 2 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b3904

    <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

    Secondary structure

    1489
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...    SMRi    		P32171

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		P32171

    <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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni236 – 238Substrate bindingUniRule annotation1 Publication3

    <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

    Belongs to the rhamnulokinase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4105DET Bacteria
    COG1070 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000250110

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P32171

    KEGG Orthology (KO)

    More...    KOi    		K00848

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P32171

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd07771 FGGY_RhuK, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_01535 Rhamnulokinase, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR018485 Carb_kinase_FGGY_C
    IPR018484 Carb_kinase_FGGY_N
    IPR013449 Rhamnulokinase

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF02782 FGGY_C, 1 hit
    PF00370 FGGY_N, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR02627 rhamnulo_kin, 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.

    P32171-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTFRNCVAVD LGASSGRVML ARYERECRSL TLREIHRFNN GLHSQNGYVT 
            60         70         80         90        100
    WDVDSLESAI RLGLNKVCEE GIRIDSIGID TWGVDFVLLD QQGQRVGLPV 
           110        120        130        140        150
    AYRDSRTNGL MAQAQQQLGK RDIYQRSGIQ FLPFNTLYQL RALTEQQPEL 
           160        170        180        190        200
    IPHIAHALLM PDYFSYRLTG KMNWEYTNAT TTQLVNINSD DWDESLLAWS 
           210        220        230        240        250
    GANKAWFGRP THPGNVIGHW ICPQGNEIPV VAVASHDTAS AVIASPLNGS 
           260        270        280        290        300
    RAAYLSSGTW SLMGFESQTP FTNDTALAAN ITNEGGAEGR YRVLKNIMGL 
           310        320        330        340        350
    WLLQRVLQEQ QINDLPALIS ATQALPACRF IINPNDDRFI NPETMCSEIQ 
           360        370        380        390        400
    AACRETAQPI PESDAELARC IFDSLALLYA DVLHELAQLR GEDFSQLHIV 
           410        420        430        440        450
    GGGCQNTLLN QLCADACGIR VIAGPVEAST LGNIGIQLMT LDELNNVDDF 
           460        470        480 
    RQVVSTTANL TTFTPNPDSE IAHYVAQIHS TRQTKELCA
    Length:489
    Mass (Da):54,069
    Last modified:October 1, 1993 - 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:iAF66259EACAC5F4E
    GO

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence CAA43001 differs from that shown. Reason: Frameshift.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti214Missing in CAA43001 (PubMed:8396120).Curated1
    Sequence conflicti388 – 389QL → HV in CAA43001 (PubMed:8396120).Curated2

    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
    		X60472 Genomic DNA Translation: CAA43001.1 Frameshift.
    L19201 Genomic DNA Translation: AAB03037.1
    U00096 Genomic DNA Translation: AAC76886.1
    AP009048 Genomic DNA Translation: BAE77405.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		S40848

    NCBI Reference Sequences

    More...    RefSeqi    		NP_418340.1, NC_000913.3
    WP_000144073.1, NZ_SSZK01000014.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC76886; AAC76886; b3904
    BAE77405; BAE77405; BAE77405

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		948399

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW3875
    eco:b3904

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.2802

    <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
    		X60472 Genomic DNA Translation: CAA43001.1 Frameshift.
    L19201 Genomic DNA Translation: AAB03037.1
    U00096 Genomic DNA Translation: AAC76886.1
    AP009048 Genomic DNA Translation: BAE77405.1
    PIRiS40848
    RefSeqiNP_418340.1, NC_000913.3
    WP_000144073.1, NZ_SSZK01000014.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...    PDBei

    Protein Data Bank RCSB

    More...    RCSB PDBi

    Protein Data Bank Japan

    More...    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2CGJX-ray2.26A1-489[»]
    2CGKX-ray2.46A/B1-489[»]
    2CGLX-ray1.88A1-489[»]
    SMRiP32171
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    IntActiP32171, 2 interactors
    STRINGi511145.b3904

    Proteomic databases

    PaxDbiP32171
    PRIDEiP32171

    Genome annotation databases

    EnsemblBacteriaiAAC76886; AAC76886; b3904
    BAE77405; BAE77405; BAE77405
    GeneIDi948399
    KEGGiecj:JW3875
    eco:b3904
    PATRICifig|1411691.4.peg.2802

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...    EchoBASEi    		EB1814
    EcoGeneiEG11868 rhaB

    Phylogenomic databases

    eggNOGiENOG4105DET Bacteria
    COG1070 LUCA
    HOGENOMiHOG000250110
    InParanoidiP32171
    KOiK00848
    PhylomeDBiP32171

    Enzyme and pathway databases

    UniPathwayiUPA00541;UER00602
    BioCyciEcoCyc:RHAMNULOKIN-MONOMER
    ECOL316407:JW3875-MONOMER
    MetaCyc:RHAMNULOKIN-MONOMER
    BRENDAi2.7.1.5 2026

    Miscellaneous databases

    EvolutionaryTraceiP32171

    Protein Ontology

    More...    PROi    		PR:P32171

    Family and domain databases

    CDDicd07771 FGGY_RhuK, 1 hit
    HAMAPiMF_01535 Rhamnulokinase, 1 hit
    InterProiView protein in InterPro
    IPR018485 Carb_kinase_FGGY_C
    IPR018484 Carb_kinase_FGGY_N
    IPR013449 Rhamnulokinase
    PfamiView protein in Pfam
    PF02782 FGGY_C, 1 hit
    PF00370 FGGY_N, 1 hit
    TIGRFAMsiTIGR02627 rhamnulo_kin, 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 nameiRHAB_ECOLI
    <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: P32171
    Secondary accession number(s): Q2M8K1
    <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: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 16, 2019
    This is version 136 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 programProkaryotic 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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