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UniProtKB - P42216 (KPSU5_ECOLX)

Entry version 124 (07 Oct 2020)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
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Protein

3-deoxy-manno-octulosonate cytidylyltransferase

Gene

kpsU

Organism
Escherichia coli
Status
Reviewed-Annotation score:

Annotation score:3 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

Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.UniRule annotation

<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 <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: CMP-3-deoxy-D-manno-octulosonate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB_1), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kpsU), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kpsU), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB_2), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kpsU), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kpsU), 3-deoxy-manno-octulosonate cytidylyltransferase (kpsU), 3-deoxy-manno-octulosonate cytidylyltransferase (kpsU), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kpsU), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kpsU), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kpsU), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kpsU), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kpsU), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kpsU), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB)
This subpathway is part of the pathway CMP-3-deoxy-D-manno-octulosonate biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP, the pathway CMP-3-deoxy-D-manno-octulosonate biosynthesis and in Nucleotide-sugar biosynthesis.

Pathwayi: lipopolysaccharide biosynthesis

This protein is involved in the pathway lipopolysaccharide biosynthesis, which is part of Bacterial outer membrane biogenesis.
View all proteins of this organism that are known to be involved in the pathway lipopolysaccharide biosynthesis and in Bacterial outer membrane biogenesis.

<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

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 functionNucleotidyltransferase, Transferase
Biological processLipopolysaccharide biosynthesis

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.7.38, 2026

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

More...UniPathwayi		UPA00030
UPA00358;UER00476

<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:
3-deoxy-manno-octulosonate cytidylyltransferaseUniRule annotation (EC:2.7.7.38UniRule annotation)
Alternative name(s):
CMP-2-keto-3-deoxyoctulosonic acid synthaseUniRule annotation
Short name:
CKSUniRule annotation
Short name:
CMP-KDO synthaseUniRule 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:kpsU
<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
<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 identifieri562 [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 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

Complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cytoplasm

<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

Chemistry databases

Drug and drug target database

More...DrugBanki		DB04482, Cmp-2-Keto-3-Deoxy-Octulosonic Acid
DB04555, Cytidine-5'-Diphosphate
DB03403, Cytidine-5'-Monophosphate
DB02431, Cytidine-5'-Triphosphate
DB03721, N-acetyl-alpha-neuraminic acid

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved
<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_00001885232 – 2463-deoxy-manno-octulosonate cytidylyltransferaseAdd BLAST245

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P42216

<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

Homodimer.

<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

1246
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		P42216

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		P42216

<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 information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the KdsB family.UniRule annotation

Phylogenomic databases

Database of Orthologous Groups

More...OrthoDBi		1345588at2

Family and domain databases

Conserved Domains Database

More...CDDi		cd02517, CMP-KDO-Synthetase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.90.550.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00057, KdsB, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003329, Cytidylyl_trans
IPR004528, KdsB
IPR029044, Nucleotide-diphossugar_trans

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02348, CTP_transf_3, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53448, SSF53448, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00466, kdsB, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P42216-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKAVIVIPA RYGSSRLPGK PLLDIVGKPM IQHVYERALQ VAGVAEVWVA 
        60         70         80         90        100
TDDPRVEQAV QAFGGKAIMT RNDHESGTDR LVEVMHKVEA DIYINLQGDE 
       110        120        130        140        150
PMIRPRDVET LLQGMRDDPA LPVATLCHAI SAAEAAEPST VKVVVNTRQD 
       160        170        180        190        200
ALYFSRSPIP YPRNAEKARY LKHVGIYAYR RDVLQNYSQL PESMPEQAES 
       210        220        230        240 
LEQLRLMNAG INIRTFEVAA TGPGVDTPAC LEKVRALMAQ ELAENA
Length:246
Mass (Da):27,159
Last modified:January 23, 2007 - v3
<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:i3D8946D30799E6BB
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
X74567 Genomic DNA Translation: CAA52657.1
S76943 Genomic DNA Translation: AAB33584.1

Protein sequence database of the Protein Information Resource

More...PIRi		C48492

NCBI Reference Sequences

More...RefSeqi		WP_000030749.1, NZ_WWEL01000034.1

<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
X74567 Genomic DNA Translation: CAA52657.1
S76943 Genomic DNA Translation: AAB33584.1
PIRiC48492
RefSeqiWP_000030749.1, NZ_WWEL01000034.1

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
1GQ9X-ray2.60A/B2-246[»]
1GQCX-ray2.60A/B2-246[»]
1H6JX-ray2.32A/B2-246[»]
1H7EX-ray1.83A/B2-246[»]
1H7FX-ray2.12A/B2-246[»]
1H7GX-ray2.13A/B2-246[»]
1H7HX-ray2.30A/B2-246[»]
1H7TX-ray2.48A/B2-246[»]
SMRiP42216
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

DrugBankiDB04482, Cmp-2-Keto-3-Deoxy-Octulosonic Acid
DB04555, Cytidine-5'-Diphosphate
DB03403, Cytidine-5'-Monophosphate
DB02431, Cytidine-5'-Triphosphate
DB03721, N-acetyl-alpha-neuraminic acid

Proteomic databases

PRIDEiP42216

Phylogenomic databases

OrthoDBi1345588at2

Enzyme and pathway databases

UniPathwayiUPA00030
UPA00358;UER00476
BRENDAi2.7.7.38, 2026

Miscellaneous databases

EvolutionaryTraceiP42216

Family and domain databases

CDDicd02517, CMP-KDO-Synthetase, 1 hit
Gene3Di3.90.550.10, 1 hit
HAMAPiMF_00057, KdsB, 1 hit
InterProiView protein in InterPro
IPR003329, Cytidylyl_trans
IPR004528, KdsB
IPR029044, Nucleotide-diphossugar_trans
PfamiView protein in Pfam
PF02348, CTP_transf_3, 1 hit
SUPFAMiSSF53448, SSF53448, 1 hit
TIGRFAMsiTIGR00466, kdsB, 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 nameiKPSU5_ECOLX
<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: P42216
<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: November 1, 1995
Last sequence update: January 23, 2007
Last modified: October 7, 2020
This is version 124 of the entry and version 3 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

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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