Q6GDU9 (PGCA_STAAR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoglucomutase
Short name=PGM
EC=5.4.2.2

Alternative name(s):
Alpha-phosphoglucomutase
Glucose phosphomutase

Gene names

Name:	pgcA
Ordered Locus Names:	SAR2576

Organism

Staphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP]

Taxonomic identifier

282458 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	552 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the interconversion between glucose-6-phosphate and alpha-glucose-1-phosphate. This is the first step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant glycolipid found in the S.aureus membrane, which is also used as a membrane anchor for lipoteichoic acid (LTA) By similarity.
Catalytic activity	Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphoglucomutase 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 – 552	552	Phosphoglucomutase		PRO_0000308342
Sites
	Active site	143	1	Phosphoserine intermediate By similarity
	Metal binding	143	1	Magnesium; via phosphate group By similarity
	Metal binding	295	1	Magnesium By similarity
	Metal binding	297	1	Magnesium By similarity
	Metal binding	299	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6GDU9 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 32F513862499BB0F	FASTA	552	62,472
	10 20 30 40 50 60 MKGCLATMDK ELWIKRANDS LVKHFYEQQS DIEQREGFES KLTFGTAGIR GKFGLGEGRL 70 80 90 100 110 120 NKFTIEKLAL GLARYLNAQT NNPTIVIHYD IRHLSTEFAQ IIANVLANHQ IIVYLPDTYK 130 140 150 160 170 180 TTPELSFAVR NLNTTAGIMI TASHNPKDYN GIKVYSSDGA QLSTDASELV SRYIEEVGDP 190 200 210 220 230 240 LQIDIPISKQ NTSYIKPFPK SVTDDYMKHI QNMIGYIPKS DLQVVFTSLH GTSVPIVPEL 250 260 270 280 290 300 LKSLNFNQFN LVEAQCKPDP NFSSVQSANP EDHRAFDQAV ELANKSHADL LISTDPDADR 310 320 330 340 350 360 LGIAERDAHG HITYFNGNQI GALLLNYRIQ QTSQLRHRLM IQSIVSSELT KSLARYNNVE 370 380 390 400 410 420 YKEVLTGFKF IAQEIRQLDD HQNMIFAFEE SYGFLSEPFV RDKDAVQIVP LIIKYASELK 430 440 450 460 470 480 LYGKTLKDEL EQIYQTVGRH EDTLFSHTLE GLEGKKKIES IMTHFRSNPP QEIQGLKVKA 490 500 510 520 530 540 IEDYLTSEVY QLDKDTTSQI DSPKSNVIRV LFDEGFIALR PSGTEPKIKL YVSLKCPDFD 550 DVAQKINAMI FS

References

[1]

"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. , Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MRSA252.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571856 Genomic DNA. Translation: CAG41556.1.
RefSeq	YP_041924.1. NC_002952.2.
3D structure databases
ProteinModelPortal	Q6GDU9.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6GDU9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000022003; EBSTAP00000021339; EBSTAG00000022002.
GeneID	2859220.
GenomeReviews	Gene locus SAR2576 in contig BX571856_GR.
KEGG	sar:SAR2576.
PATRIC	19548848. VBIStaAur71814_2602.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1109.
GeneTree	EBGT00050000024615.
HOGENOM	HBG571743.
OMA	IGEDVDM.
ProtClustDB	CLSK886017.
Enzyme and pathway databases
BioCyc	SAUR282458:SAR2576-MONOMER.
Family and domain databases
InterPro	IPR005844. A-D-PHexomutase_a/b/a-I. IPR016055. A-D-PHexomutase_a/b/a-I/II/III. IPR005845. A-D-PHexomutase_a/b/a-II. IPR005846. A-D-PHexomutase_a/b/a-III. IPR005843. A-D-PHexomutase_C. IPR016066. A-D-PHexomutase_CS. IPR005841. Alpha-D-phosphohexomutase_SF. [Graphical view]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KO	K01840.
Pfam	PF02878. PGM_PMM_I. 1 hit. PF02879. PGM_PMM_II. 1 hit. PF02880. PGM_PMM_III. 1 hit. PF00408. PGM_PMM_IV. 1 hit. [Graphical view]
PRINTS	PR00509. PGMPMM.
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PGCA_STAAR

Accession

Primary (citable) accession number: Q6GDU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
Last sequence update:	July 19, 2004
Last modified:	January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program