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UniProtKB - P32171 (RHAB_ECOLI)

Entry version 147 (25 May 2022)
Sequence version 1 (01 Oct 1993)
Previous versions | rss
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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%5Fsection">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%5Fsection">'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 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%5Fsection">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%5Fsection">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%5Fsection">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

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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

<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%5Fand%5Fbiotech%5Fsection">'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 or proteolytic cleavage.<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%5Fsection">'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%5Fsection">'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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P32171

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		COG1070, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_039395_0_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P32171

Identification of Orthologs from Complete Genome Data

More...OMAi		MPDLFNY

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
IPR043129, ATPase_NBD
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

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53067, SSF53067, 2 hits

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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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[»]
AlphaFoldDBiP32171
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

Phylogenomic databases

eggNOGiCOG1070, Bacteria
HOGENOMiCLU_039395_0_0_6
InParanoidiP32171
OMAiMPDLFNY
PhylomeDBiP32171

Enzyme and pathway databases

UniPathwayiUPA00541;UER00602
BioCyciEcoCyc: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
IPR043129, ATPase_NBD
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
SUPFAMiSSF53067, SSF53067, 2 hits
TIGRFAMsiTIGR02627, rhamnulo_kin, 1 hit

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%5Fand%5Fisoforms">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: May 25, 2022
This is version 147 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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