NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=LT2;
DOI=10.1111/j.1365-2958.1991.tb00741.x; PubMed=1710759 [NCBI, ExPASy, EBI, Israel, Japan]
Jiang X.-M., Neal B., Santiago F., Lee S.J., Romana L.K., Reeves P.R.;
"Structure and sequence of the rfb (O antigen) gene cluster of Salmonella serovar typhimurium (strain LT2).";
Mol. Microbiol. 5:695-713(1991).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
DOI=10.1038/35101614; PubMed=11677609 [NCBI, ExPASy, EBI, Israel, Japan]
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
Nature 413:852-856(2001).

Comments

CATALYTIC ACTIVITY: CTP + alpha-D-glucose 1-phosphate = diphosphate + CDP-glucose.
PATHWAY: Nucleotide-sugar biosynthesis; CDP-3,6-dideoxy-D-mannose biosynthesis; CDP-3,6-dideoxy-D-mannose from CTP and alpha-D-glucose 1-phosphate: step 1/5 .
PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis .

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X56793; CAA40120.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE008792; AAL20996.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S15304; S15304.

RefSeq

NP_461037.1; -.

3D structure databases

PDB

1TZF; X-ray; 2.10 A; A=2-257.	[ExPASy / RCSB / EBI]
1WVC; X-ray; 2.50 A; A=2-257.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1TZF; -.
1WVC; -.

ModBase

P26396.

Enzyme and pathway databases

BioCyc

STYP99287:STM2092-MON; -.

Organism-specific databases

StyGene

SG10346; rfbF.

Ontologies

GO:0047343;	Molecular function: glucose-1-phosphate cytidylyltransferase activity (inferred from electronic annotation from EC).
GO:0009103;	Biological process: lipopolysaccharide biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013446; G1P_cyt_trans.
IPR005835; NTP_transferase.
Graphical view of domain structure.

PANTHER

PTHR22572:SF16; G1P_cyt_trans; 1.

Pfam

PF00483; NTP_transferase; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02623; G1P_cyt_trans; 1.

Genome annotation databases

GeneID

1253613; -.

GenomeReviews

AE006468_GR; STM2092.

KEGG

stm:STM2092; -.

NMPDR

fig|99287.1.peg.2017; -.

Phylogenomic databases

HOGENOM

P26396; -.

Genome annotation databases

CMR

P26396; STM2092.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Lipopolysaccharide biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 257`	`257`	`Glucose-1-phosphate cytidylyltransferase.`	`PRO_0000097293`
`STRAND`	`2 7`	`6`
`HELIX`	`23 25`	`3`
`HELIX`	`33 43`	`11`
`STRAND`	`48 53`	`6`
`HELIX`	`57 65`	`9`
`HELIX`	`67 71`	`5`
`STRAND`	`74 77`	`4`
`HELIX`	`78 80`	`3`
`STRAND`	`82 85`	`4`
`STRAND`	`94 99`	`6`
`HELIX`	`106 112`	`7`
`HELIX`	`113 116`	`4`
`TURN`	`117 119`	`3`
`STRAND`	`123 127`	`5`
`STRAND`	`130 132`	`3`
`HELIX`	`136 146`	`11`
`STRAND`	`149 155`	`7`
`STRAND`	`161 167`	`7`
`STRAND`	`170 177`	`8`
`STRAND`	`190 192`	`3`
`HELIX`	`194 199`	`6`
`TURN`	`207 209`	`3`
`HELIX`	`210 217`	`8`
`STRAND`	`221 226`	`6`
`STRAND`	`230 232`	`3`
`HELIX`	`236 247`	`12`

Sequence information

Length: 257 AA [This is the length of the unprocessed precursor]

Molecular weight: 29035 Da [This is the MW of the unprocessed precursor]

CRC64: 04DB33D51357D70E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKAVILAGGL GTRLSEETIV KPKPMVEIGG KPILWHIMKM YSVHGIKDFI ICCGYKGYVI 

        70         80         90        100        110        120 
KEYFANYFLH MSDVTFHMAE NRMEVHHKRV EPWNVTLVDT GDSSMTGGRL KRVAEYVKDD 

       130        140        150        160        170        180 
EAFLFTYGDG VADLDIKATI DFHKAHGKKA TLTATFPPGR FGALDIRAGQ VRSFQEKPKG 

       190        200        210        220        230        240 
DGAMINGGFF VLNPSVIDLI DNDATTWEQE PLMTLAQQGE LMAFEHPGFW QPMDTLRDKV 

       250 
YLEGLWEKGK APWKTWE

P26396 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools