NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=LT2;
DOI=10.1007/BF00259668; PubMed=1712067 [NCBI, ExPASy, EBI, Israel, Japan]
Stevenson G., Lee S.J., Romana L.K., Reeves P.R.;
"The cps gene cluster of Salmonella strain LT2 includes a second mannose pathway: sequence of two genes and relationship to genes in the rfb gene cluster.";
Mol. Gen. Genet. 227:173-180(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

FUNCTION: Involved in the biosynthesis of the capsular polysaccharide colanic acid.
CATALYTIC ACTIVITY: GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose.
PATHWAY: Carbohydrate biosynthesis; GDP-D-mannose biosynthesis .
SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2 family.

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

X59886; CAA42540.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE008793; AAL21009.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S16290; S16290.

RefSeq

NP_461050.2; -.

3D structure databases

ModBase

P26340.

Enzyme and pathway databases

BioCyc

STYP99287:STM2105-MON; -.

Organism-specific databases

StyGene

SG10066; manC.

Ontologies

GO:0004475;	Molecular function: mannose-1-phosphate guanylyltransferase activity (inferred from electronic annotation from EC).
GO:0009103;	Biological process: lipopolysaccharide biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR006375; Man1P_GuanlTrfase/Man6P_Isoase.
IPR001538; Man6P_isomerase-2_C.
IPR005835; NTP_transferase.
IPR014710; RmlC-like_jellyroll.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.120.10; RmlC-like_jellyroll; 1.

Pfam

PF01050; MannoseP_isomer; 1.
PF00483; NTP_transferase; 1.
Pfam graphical view of domain structure.

ProDom

PD002664; Man6P_isomerII; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01479; GMP_PMI; 1.

Genome annotation databases

GeneID

1253626; -.

GenomeReviews

AE006468_GR; STM2105.

NMPDR

fig|99287.1.peg.2030; -.

Phylogenomic databases

HOGENOM

P26340; -.

Genome annotation databases

CMR

P26340; STM2105.

Other

UniRef

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

Keywords

Capsule biogenesis/degradation; Complete proteome; Lipopolysaccharide biosynthesis; Nucleotidyltransferase; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 480`	`480`		`Mannose-1-phosphate guanylyltransferase manC.`	`PRO_0000194257`

Sequence information

Length: 480 AA [This is the length of the unprocessed precursor]

Molecular weight: 53370 Da [This is the MW of the unprocessed precursor]

CRC64: C1F09C66B04CDBD6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIMRQTKLYP VVMAGGSGSR LWPLSRVLYP KQFLCLKGDL TMLQTTICRL NGVECESPLV 

        70         80         90        100        110        120 
ICNEQHRFIV AEQLRQLNKL TENIILEPAG RNTAPAIALA ALAATRQHTD CDPLMLVLAA 

       130        140        150        160        170        180 
DHAIANEEAF RDAVRGAMPY ADAGKLVTFG IVPDLPETGY GYIRRGDVVP GATDAVAFEV 

       190        200        210        220        230        240 
AQFVEKPGLE TAQAYVASGD YYWNSGMFLF RAGRYLEELK KFRPDILAAC EQAMRGVDPD 

       250        260        270        280        290        300 
LDFIRVDEEA FLACPEESID YAVMERTADA VVMPMDAGWS DVGSWSSLWE ISAHTPEGNV 

       310        320        330        340        350        360 
HHGDVISHKT ENSYVYAESG LVTTVGVKDL VVVQTKDAVL IADRHAVQDV KKVVEKIKAD 

       370        380        390        400        410        420 
GRHEHHMHRE VYRPWGKYDS IDAGERYQVK RITVKPGEGL SVQMHHHRAE HWVVVAGTAR 

       430        440        450        460        470        480 
VTINGEVKLL GENESIYIPL GATHCLENPG KIPLDLIEVR SGSYLEEDDV VRFEDRYGRV

P26340 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