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Protein

3-deoxy-manno-octulosonate cytidylyltransferase

Gene

kdsB

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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 (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.UniRule annotation
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

  • 3-deoxy-manno-octulosonate cytidylyltransferase activity Source: TIGR

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Enzyme and pathway databases

BioCyciVCHO:VC1875-MONOMER.
BRENDAi2.7.7.38. 6626.
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:kdsBUniRule annotation
Ordered Locus Names:VC_1875
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000000584 Componenti: Chromosome 1

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001885171 – 2523-deoxy-manno-octulosonate cytidylyltransferaseAdd BLAST252

Interactioni

Protein-protein interaction databases

STRINGi243277.VC1875.

Structurei

Secondary structure

1252
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Beta strandi14 – 16Combined sources3
Helixi19 – 21Combined sources3
Helixi29 – 39Combined sources11
Beta strandi43 – 50Combined sources8
Helixi52 – 60Combined sources9
Beta strandi64 – 67Combined sources4
Helixi75 – 85Combined sources11
Beta strandi92 – 96Combined sources5
Helixi106 – 118Combined sources13
Beta strandi122 – 130Combined sources9
Helixi133 – 136Combined sources4
Beta strandi143 – 146Combined sources4
Beta strandi150 – 158Combined sources9
Helixi164 – 168Combined sources5
Beta strandi169 – 171Combined sources3
Beta strandi178 – 188Combined sources11
Helixi191 – 197Combined sources7
Helixi202 – 207Combined sources6
Helixi212 – 216Combined sources5
Beta strandi221 – 225Combined sources5
Helixi237 – 249Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OAMX-ray1.75A/B/C/D1-252[»]
ProteinModelPortaliQ9KQX2.
SMRiQ9KQX2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9KQX2.

Family & Domainsi

Sequence similaritiesi

Belongs to the KdsB family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CET. Bacteria.
COG1212. LUCA.
KOiK00979.
OMAiNSGTERC.

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.

Q9KQX2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFTVVIPAR YQSTRLPGKP LADIGGKPMI QWVYEQAMQA GADRVIIATD
60 70 80 90 100
DERVEQAVQA FGGVVCMTSP NHQSGTERLA EVVAKMAIPA DHIVVNVQGD
110 120 130 140 150
EPLIPPAIIR QVADNLAACS APMATLAVEI EDEAEVFNPN AVKVITDKSG
160 170 180 190 200
YALYFSRATI PWDRDNFAKA DKAIVQPLLR HIGIYAYRAG FINTYLDWQP
210 220 230 240 250
SQLEKIECLE QLRVLWHGEK IHVAVALEAP PAGVDTPEDL EVVRRIVAER

AQ
Length:252
Mass (Da):27,722
Last modified:October 1, 2000 - v1
Checksum:i10C7A093209CF212
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF95023.1.
PIRiA82146.
RefSeqiNP_231509.1. NC_002505.1.
WP_000011329.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF95023; AAF95023; VC_1875.
GeneIDi2613629.
KEGGivch:VC1875.
PATRICi20082792. VBIVibCho83274_1791.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF95023.1.
PIRiA82146.
RefSeqiNP_231509.1. NC_002505.1.
WP_000011329.1. NC_002505.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OAMX-ray1.75A/B/C/D1-252[»]
ProteinModelPortaliQ9KQX2.
SMRiQ9KQX2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243277.VC1875.

Protocols and materials databases

DNASUi2613629.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF95023; AAF95023; VC_1875.
GeneIDi2613629.
KEGGivch:VC1875.
PATRICi20082792. VBIVibCho83274_1791.

Phylogenomic databases

eggNOGiENOG4105CET. Bacteria.
COG1212. LUCA.
KOiK00979.
OMAiNSGTERC.

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00358; UER00476.
BioCyciVCHO:VC1875-MONOMER.
BRENDAi2.7.7.38. 6626.

Miscellaneous databases

EvolutionaryTraceiQ9KQX2.

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 nameiKDSB_VIBCH
AccessioniPrimary (citable) accession number: Q9KQX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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

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.