Reviewed, UniProtKB/Swiss-Prot Q9Y725 (MPG11_CANGA)

Names and origin

Protein names

Recommended name:
    Mannose-1-phosphate guanyltransferase 1
    EC=2.7.7.13
Alternative name(s):
    ATP-mannose-1-phosphate guanylyltransferase 1
    GDP-mannose pyrophosphorylase 1

Gene names

Name:	MPG1
Synonyms:	VIG9
Ordered Locus Names:	CAGL0D01034g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint By similarity.
Catalytic activity	GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose. Ref.1
Pathway	Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the transferase hexapeptide repeat family.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Cytoplasm
Ligand	GTP-binding Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro cell cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW mannose-1-phosphate guanylyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 361	361	Mannose-1-phosphate guanyltransferase 1		PRO_0000238485
Experimental info
	Sequence conflict	55	1	C → Y in CAG58370. Ref.2
	Sequence conflict	330	1	N → D in CAG58370. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9Y725-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: E255084D2EDB2A1D	FASTA	361	39,299
	10 20 30 40 50 60 MKGLILVGGY GTRLRPLTLT VPKPLVEFGN RPMILHQIEA LANAGVTDIV LAVNCRPEVM 70 80 90 100 110 120 VETLQKYEKE YGVSITFSVE TEPLGTAGPL KLAEKVLKKD NSPFFVLNSD VICEYPFKEL 130 140 150 160 170 180 ADFHKAHGGK GTIVATKVDE PSKYGVIVHD IATPNLIDRF VEKPKEFVGN RINAGLYILN 190 200 210 220 230 240 PEVIDLIEMK PTSIETETFP ILVEQKSLYS FDLEGFWMDV GQPKDFLSGT VLYLNSVSKK 250 260 270 280 290 300 NPEKLTKGDN IVGNVMVDPS AKIAASAKVG PDVVIGPNVT IGEGVRITRS VVLSDSSIQD 310 320 330 340 350 360 HSLVKSTIVG WKSTVGKWCR LEGVTVLGDN VVVKDEVYVN GGKVLPHKSI SANVPSEAII M

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The VIG9 gene products from the human pathogenic fungi Candida albicans and Candida glabrata encode GDP-mannose pyrophosphorylase." Ohta A., Chibana H., Arisawa M., Sudoh M. Biochim. Biophys. Acta 1475:265-272(2000) [PubMed: 10913825] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB020570 Genomic DNA. Translation: BAA77382.1. CR380950 Genomic DNA. Translation: CAG58370.1.
RefSeq	XP_445459.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9Y725.
Genome annotation databases
GeneID	2886966.
GenomeReviews	Gene locus CAGL0D01034g in contig CR380950_GR.
KEGG	cgr:CAGL0D01034g.
Phylogenomic databases
HOGENOM	Q9Y725.
Enzyme and pathway databases
BRENDA	2.7.7.13. 189220.
Family and domain databases
InterPro	IPR001451. Hexapep_transf. IPR018357. Hexapep_transf_CS. IPR005835. NTP_transferase. [Graphical view]
Pfam	PF00132. Hexapep. 4 hits. PF00483. NTP_transferase. 1 hit. [Graphical view]
PROSITE	PS00101. HEXAPEP_TRANSFERASES. 3 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MPG11_CANGA

Accession

Primary (citable) accession number: Q9Y725
Secondary accession number(s): Q6FWD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	November 1, 1999
Last modified:	September 22, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)