Reviewed, UniProtKB/Swiss-Prot P18159 (PGCA_BACSU)

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
Synonyms:	gtaC, gtaE, yhxB
Ordered Locus Names:	BSU09310

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	581 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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 B.subtilis membrane, which is also used as a membrane anchor for lipoteichoic acid (LTA). Has a role in the biosynthesis of all phosphate-containing envelope polymers, since glucose-1-phosphate is the precursor of UDP-glucose, which serves as a glucosyl donor not only for the biosynthesis of LTA but also for wall teichoic acids (WTAs). Is required for biofilm formation. This is likely due to another role of UDP-glucose, which might also act as a metabolic signal regulating biofilm formation or may be involved in some unknown biosynthetic pathway essential for biofilm formation, e.g. the synthesis of an exopolysaccharide. Ref.1 Ref.6
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. Ref.1
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: UniProtKB-KW 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 – 581	581	Phosphoglucomutase		PRO_0000148020
Sites
	Active site	146	1	Phosphoserine intermediate By similarity
	Metal binding	146	1	Magnesium; via phosphate group By similarity
	Metal binding	303	1	Magnesium By similarity
	Metal binding	305	1	Magnesium By similarity
	Metal binding	307	1	Magnesium By similarity
Experimental info
	Mutagenesis	162	1	G → D: Very low enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology. Ref.1
	Mutagenesis	240	1	T → I: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology. Ref.1
	Mutagenesis	407	1	G → D: Loss of enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology. Ref.1
	Mutagenesis	418	1	D → N: Impaired enzymatic activity. Great decrease in biofilm formation. Deformed cell morphology. Ref.1
	Sequence conflict	141	1	I → V in CAA74431. Ref.2
	Sequence conflict	189 – 207	19	DEENK…IGEDI → VRY in CAA74431. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P18159-1 [UniParc]. Last modified October 23, 2007. Version 3. Checksum: E8F2823808BFCDF0	FASTA	581	64,663
	10 20 30 40 50 60 MTWRKSYERW KQTEHLDLEL KERLIELEGD EQALEDCFYK DLEFGTGGMR GEIGAGTNRM 70 80 90 100 110 120 NIYTVRKASA GFAAYISKQG EEAKKRGVVI AYDSRHKSPE FAMEAAKTLA TQGIQTYVFD 130 140 150 160 170 180 ELRPTPELSF AVRQLNAYGG IVVTASHNPP EYNGYKVYGD DGGQLPPKEA DIVIEQVNAI 190 200 210 220 230 240 ENELTITVDE ENKLKEKGLI KIIGEDIDKV YTEKLTSISV HPELSEEVDV KVVFTPLHGT 250 260 270 280 290 300 ANKPVRRGLE ALGYKNVTVV KEQELPDSNF STVTSPNPEE HAAFEYAIKL GEEQNADILI 310 320 330 340 350 360 ATDPDADRLG IAVKNDQGKY TVLTGNQTGA LLLHYLLSEK KKQGILPDNG VVLKTIVTSE 370 380 390 400 410 420 IGRAVASSFG LDTIDTLTGF KFIGEKIKEY EASGQYTFQF GYEESYGYLI GDFARDKDAI 430 440 450 460 470 480 QAALLAVEVC AFYKKQGMSL YEALINLFNE YGFYREGLKS LTLKGKQGAE QIEAILASFR 490 500 510 520 530 540 QNPPQKMAGK QVVTAEDYAV SKRTLLTESK EEAIDLPKSN VLKYFLEDGS WFCLRPSGTE 550 560 570 580 PKVKFYFAVK GSSLEDSEKR LAVLSEDVMK TVDEIVESTA K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bacillus subtilis alpha-phosphoglucomutase is required for normal cell morphology and biofilm formation." Lazarevic V., Soldo B., Medico N., Pooley H.M., Bron S., Karamata D. Appl. Environ. Microbiol. 71:39-45(2005) [PubMed: 15640167] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ROLE IN LTA AND WTAS BIOSYNTHESIS, PATHWAY, ROLE IN BIOFILM FORMATION, MUTAGENESIS OF GLY-162; THR-240; GLY-407 AND ASP-418. Strain: 168.
[2]	"The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus subtilis chromosome contains several dysfunctional genes, the glyB marker, many genes encoding transporter proteins, and the ubiquitous hit gene." Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., Venema G., Bron S. Microbiology 144:859-875(1998) [PubMed: 9579061] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 141 AND 189-207.
[5]	"Glycerol catabolism in Bacillus subtilis: nucleotide sequence of the genes encoding glycerol kinase (glpK) and glycerol-3-phosphate dehydrogenase (glpD)." Holmberg C., Beijer L., Rutberg B., Rutberg L. J. Gen. Microbiol. 136:2367-2375(1990) [PubMed: 2127799] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
[6]	"Genes involved in formation of structured multicellular communities by Bacillus subtilis." Branda S.S., Gonzalez-Pastor J.E., Dervyn E., Ehrlich S.D., Losick R., Kolter R. J. Bacteriol. 186:3970-3979(2004) [PubMed: 15175311] [Abstract] Cited for: ROLE IN BIOFILM FORMATION. Strain: 168 and 3610.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ784890 Genomic DNA. Translation: CAH04980.1. Y14079 Genomic DNA. Translation: CAA74431.1. AL009126 Genomic DNA. Translation: CAB12759.2. M34393 Genomic DNA. Translation: AAA22488.1.
PIR	C69835.
RefSeq	NP_388812.2.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	936247.
GenomeReviews	Gene locus BSU09310 in contig AL009126_GR.
KEGG	bsu:BSU09310.
Organism-specific databases
SubtiList	BG10189. pgcA. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P18159.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU0931-MON.
BRENDA	5.4.2.2. 150.
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. IPR016066. A-D-PHexomutase_CS. IPR005841. A-D-PHexomutase_N. [Graphical view]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 1 hit.
Pfam	PF02878. PGM_PMM_I. 1 hit. PF02879. PGM_PMM_II. 1 hit. PF02880. PGM_PMM_III. 1 hit. [Graphical view]
PRINTS	PR00509. PGMPMM.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PGCA_BACSU

Accession

Primary (citable) accession number: P18159
Secondary accession number(s): Q68VA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	October 23, 2007
Last modified:	October 13, 2009
This is version 77 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)