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Protein

3-deoxy-manno-octulosonate cytidylyltransferase

Gene

kpsU

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

CTP + 3-deoxy-D-manno-octulosonate = diphosphate + CMP-3-deoxy-D-manno-octulosonate.

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.
Proteins known to be involved in this subpathway in this organism are:
  1. 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 (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 (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kdsB), 3-deoxy-manno-octulosonate cytidylyltransferase (kpsU), 3-deoxy-manno-octulosonate cytidylyltransferase (kpsU)
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Enzyme and pathway databases

BRENDAi2.7.7.38. 2026.
UniPathwayiUPA00030.
UPA00358; UER00476.

Names & Taxonomyi

Protein namesi
Recommended name:
3-deoxy-manno-octulosonate cytidylyltransferase (EC:2.7.7.38)
Alternative name(s):
CMP-2-keto-3-deoxyoctulosonic acid synthase
Short name:
CKS
Short name:
CMP-KDO synthase
Gene namesi
Name:kpsU
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 2462453-deoxy-manno-octulosonate cytidylyltransferasePRO_0000188523Add
BLAST

Proteomic databases

PRIDEiP42216.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi469008.ECD_02817.

Structurei

Secondary structure

1
246
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Beta strandi15 – 173Combined sources
Helixi20 – 223Combined sources
Beta strandi24 – 296Combined sources
Helixi30 – 3910Combined sources
Beta strandi46 – 527Combined sources
Helixi54 – 629Combined sources
Beta strandi66 – 694Combined sources
Helixi77 – 8711Combined sources
Beta strandi91 – 955Combined sources
Helixi105 – 11713Combined sources
Beta strandi123 – 1308Combined sources
Helixi132 – 1354Combined sources
Beta strandi142 – 1454Combined sources
Beta strandi150 – 1578Combined sources
Helixi165 – 1673Combined sources
Beta strandi170 – 18011Combined sources
Helixi181 – 1866Combined sources
Helixi187 – 1893Combined sources
Helixi194 – 1996Combined sources
Helixi204 – 2085Combined sources
Beta strandi213 – 2175Combined sources
Beta strandi225 – 2273Combined sources
Helixi228 – 24417Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP42216.
SMRiP42216. Positions 2-246.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42216.

Family & Domainsi

Sequence similaritiesi

Belongs to the KdsB family.Curated

Phylogenomic databases

eggNOGiENOG4105CET. Bacteria.
COG1212. LUCA.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_00057. CMP_KDO_synth.
InterProiIPR003329. Cytidylyl_trans.
IPR004528. KdsB.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR21485:SF4. PTHR21485:SF4. 1 hit.
PfamiPF02348. CTP_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR00466. kdsB. 1 hit.

Sequencei

Sequence statusi: Complete.

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
Checksum:i3D8946D30799E6BB
GO

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_LRXW01000027.1.

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_LRXW01000027.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP42216.
SMRiP42216. Positions 2-246.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi469008.ECD_02817.

Proteomic databases

PRIDEiP42216.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CET. Bacteria.
COG1212. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00358; UER00476.
BRENDAi2.7.7.38. 2026.

Miscellaneous databases

EvolutionaryTraceiP42216.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_00057. CMP_KDO_synth.
InterProiIPR003329. Cytidylyl_trans.
IPR004528. KdsB.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR21485:SF4. PTHR21485:SF4. 1 hit.
PfamiPF02348. CTP_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR00466. kdsB. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular analysis of region 1 of the Escherichia coli K5 antigen gene cluster: a region encoding proteins involved in cell surface expression of capsular polysaccharide."
    Pazzani C., Rosenow C., Boulnois G.J., Bronner D., Jann K., Roberts I.S.
    J. Bacteriol. 175:5978-5983(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K5.
  2. "Isolation from recombinant Escherichia coli and characterization of CMP-Kdo synthetase, involved in the expression of the capsular K5 polysaccharide (K-CKS)."
    Rosenow C., Roberts I.S., Jann K.
    FEMS Microbiol. Lett. 125:159-164(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The three-dimensional structure of capsule-specific CMP: 2-keto-3-deoxy-manno-octonic acid synthetase from Escherichia coli."
    Jelakovic S., Jann K., Schulz G.E.
    FEBS Lett. 391:157-161(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Entry informationi

Entry nameiKPSU5_ECOLX
AccessioniPrimary (citable) accession number: P42216
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.