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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-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

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 (kpsU), 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 (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 (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 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
Gene namesi
Name:kpsU
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001885232 – 2463-deoxy-manno-octulosonate cytidylyltransferaseAdd BLAST245

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi469008.ECD_02817.

Structurei

Secondary structure

1246
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Beta strandi15 – 17Combined sources3
Helixi20 – 22Combined sources3
Beta strandi24 – 29Combined sources6
Helixi30 – 39Combined sources10
Beta strandi46 – 52Combined sources7
Helixi54 – 62Combined sources9
Beta strandi66 – 69Combined sources4
Helixi77 – 87Combined sources11
Beta strandi91 – 95Combined sources5
Helixi105 – 117Combined sources13
Beta strandi123 – 130Combined sources8
Helixi132 – 135Combined sources4
Beta strandi142 – 145Combined sources4
Beta strandi150 – 157Combined sources8
Helixi165 – 167Combined sources3
Beta strandi170 – 180Combined sources11
Helixi181 – 186Combined sources6
Helixi187 – 189Combined sources3
Helixi194 – 199Combined sources6
Helixi204 – 208Combined sources5
Beta strandi213 – 217Combined sources5
Beta strandi225 – 227Combined sources3
Helixi228 – 244Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP42216.
SMRiP42216.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42216.

Family & Domainsi

Sequence similaritiesi

Belongs to the KdsB family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CET. Bacteria.
COG1212. LUCA.

Family and domain databases

CDDicd02517. CMP-KDO-Synthetase. 1 hit.
Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_00057. KdsB. 1 hit.
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_LZET01000077.1.

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_LZET01000077.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP42216.
SMRiP42216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi469008.ECD_02817.

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

CDDicd02517. CMP-KDO-Synthetase. 1 hit.
Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_00057. KdsB. 1 hit.
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...

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: November 30, 2016
This is version 102 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.