[1]	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).
[3]	PROTEIN SEQUENCE OF 1-13, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. STRAIN=LT2; DOI=10.1093/glycob/6.6.591; PubMed=8922954 [NCBI, ExPASy, EBI, Israel, Japan] Elling L., Ritter J.E., Verseck S.; "Expression, purification and characterization of recombinant phosphomannomutase and GDP-alpha-D-mannose pyrophosphorylase from Salmonella enterica, group B, for the synthesis of GDP-alpha-D-mannose from D-mannose."; Glycobiology 6:591-597(1996).

Comments

FUNCTION: Involved in GDP-mannose biosynthesis which serves as the activated sugar nucleotide precursor for mannose residues in cell surface polysaccharides. This enzyme participates in synthesis of the LPS group B O antigen.
CATALYTIC ACTIVITY: GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=0.01 mM for mannose-1-phosphate;
K_M=0.20 mM for GTP;
V_max=1.80 µmol/min/mg enzyme toward mannose-1-phosphate;
V_max=2.40 µmol/min/mg enzyme toward GTP;
PATHWAY: Carbohydrate biosynthesis; GDP-D-mannose biosynthesis .
PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis .
SUBUNIT: Homodimer.
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

X56793; CAA40128.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE008792; AAL20988.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S15312; S15312.

RefSeq

NP_461029.1; -.

3D structure databases

ModBase

P26404.

Enzyme and pathway databases

BioCyc

STYP99287:STM2084-MON; -.

Organism-specific databases

StyGene

SG10350; rfbM.

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

1253605; -.

GenomeReviews

AE006468_GR; STM2084.

KEGG

stm:STM2084; -.

NMPDR

fig|99287.1.peg.2009; -.

Phylogenomic databases

HOGENOM

P26404; -.

Genome annotation databases

CMR

P26404; STM2084.

Other

UniRef

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

Keywords

Complete proteome; Direct protein sequencing; Lipopolysaccharide biosynthesis; Nucleotidyltransferase; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 479`	`479`		`Mannose-1-phosphate guanylyltransferase rfbM.`	`PRO_0000194261`

Sequence information

Length: 479 AA [This is the length of the unprocessed precursor]

Molecular weight: 54046 Da [This is the MW of the unprocessed precursor]

CRC64: FE9E84D5CEE1F118 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSFLPVIMAG GTGSRLWPLS REYHPKQFLS VEGKLSMLQN TIKRLASLST EEPVVICNDR 

        70         80         90        100        110        120 
HRFLVAEQLR EIDKLANNII LEPVGRNTAP AIALAAFCAL QNADNADPLL LVLAADHVIQ 

       130        140        150        160        170        180 
DEIAFTKAVR HAEEYAANGK LVTFGIVPTH AETGYGYIRR GELIGNDAYA VAEFVEKPDI 

       190        200        210        220        230        240 
DTAGDYFKSG KYYWNSGMFL FRASSYLNEL KYLSPEIYKA CEKAVGHINP DLDFIRIDKE 

       250        260        270        280        290        300 
EFMSCPSDSI DYAVMEHTQH AVVIPMSAGW SDVGSWSSLW DISNKDHQRN VLKGDIFAHA 

       310        320        330        340        350        360 
CNDNYIYSED MFISAIGVSN LVIVQTTDAL LVANKDTVQD VKKIVDYLKR NDRNEYKQHQ 

       370        380        390        400        410        420 
EVFRPWGKYN VIDSGKNYLV RCITVKPGEK FVAQMHHHRA EHWIVLSGTA RVTKGEQTYM 

       430        440        450        460        470 
VSENESTFIP PNTIHALENP GMTPLKLIEI QSGTYLGEDD IIRLEQRSGF SKEWTNERS

P26404 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