3-deoxy-manno-octulosonate cytidylyltransferase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P04951 (KDSB_ECOLI)

Last modified November 24, 2009. Version 101. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    3-deoxy-manno-octulosonate cytidylyltransferase
    EC=2.7.7.38
Alternative name(s):
    CMP-KDO synthetase
    CMP-2-keto-3-deoxyoctulosonic acid synthetase
      Short name=CKS

Gene names

Name:	kdsB
Ordered Locus Names:	b0918, JW0901

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria By similarity.
Catalytic activity	CTP + 3-deoxy-D-manno-octulosonate = diphosphate + CMP-3-deoxy-D-manno-octulosonate. HAMAP MF_00057
Cofactor	Magnesium. HAMAP MF_00057
Pathway	Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. HAMAP MF_00057 Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. HAMAP MF_00057
Subcellular location	Cytoplasm Potential.
Sequence similarities	Belongs to the kdsB family.

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Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Cellular component	Cytoplasm
Ligand	Magnesium
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	keto-3-deoxy-D-manno-octulosonic acid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-deoxy-manno-octulosonate cytidylyltransferase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
tufA	P0A6N1	1	EBI-544810,EBI-301077
ydhM	P67430	1	EBI-544810,EBI-544803

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed HAMAP MF_00057

Chain

2 – 248

247

3-deoxy-manno-octulosonate cytidylyltransferase HAMAP MF_00057

PRO_0000188501

Secondary structure

248

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P04951-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: AAB3CFDF4841FE7A
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FASTA

248

27,614

        10         20         30         40         50         60 
MSFVVIIPAR YASTRLPGKP LVDINGKPMI VHVLERARES GAERIIVATD HEDVARAVEA 

        70         80         90        100        110        120 
AGGEVCMTRA DHQSGTERLA EVVEKCAFSD DTVIVNVQGD EPMIPATIIR QVADNLAQRQ 

       130        140        150        160        170        180 
VGMATLAVPI HNAEEAFNPN AVKVVLDAEG YALYFSRATI PWDRDRFAEG LETVGDNFLR 

       190        200        210        220        230        240 
HLGIYGYRAG FIRRYVNWQP SPLEHIEMLE QLRVLWYGEK IHVAVAQEVP GTGVDTPEDL 


ERVRAEMR

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of CTP:CMP-3-deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase) from Escherichia coli." Goldman R.C., Bolling T.J., Kohlbrenner W.E., Kim Y., Fox J.L. J. Biol. Chem. 261:15831-15835(1986) [PubMed: 3023327] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: K12.
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

J02614 Genomic DNA. Translation: AAA83877.1.
U00096 Genomic DNA. Translation: AAC74004.1.
AP009048 Genomic DNA. Translation: BAA35664.1.

PIR

A26322.

RefSeq

AP_001548.1.
NP_415438.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VH1	X-ray	2.60	A/B/C/D	2-247	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:10066N.

IntAct

P04951. 17 interactions.

STRING

P04951.

2-D gel databases

SWISS-2DPAGE

P04951.

ECO2DBASE

C032.7. 6TH EDITION.

Genome annotation databases

GeneID

945539.

GenomeReviews

Gene locus JW0901 in contig AP009048_GR.
Gene locus b0918 in contig U00096_GR.

KEGG

ecj:JW0901.
eco:b0918.

Organism-specific databases

EchoBASE

EB0514.

EcoGene

EG10519. kdsB.

CMR

Search...

Phylogenomic databases

HOGENOM

P04951.

OMA

FSRAPLP

Enzyme and pathway databases

BioCyc

EcoCyc:CPM-KDOSYNTH-MON.
ECOL168927:B0918-MON.
MetaCyc:CPM-KDOSYNTH-MON.

Gene expression databases

Genevestigator

P04951.

Family and domain databases

HAMAP

MF_00057.
[Tree]

InterPro

IPR003329. Cytidylyl_trans.
IPR004528. KdsB.
[Graphical view]

Pfam

PF02348. CTP_transf_3. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00466. kdsB. 1 hit.

ProtoNet

Search...

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Entry information

Entry name

KDSB_ECOLI

Accession

Primary (citable) accession number: P04951

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents