PGCA_BACSU
ID PGCA_BACSU Reviewed; 581 AA.
AC P18159; Q68VA2;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Phosphoglucomutase;
DE Short=PGM;
DE EC=5.4.2.2;
DE AltName: Full=Alpha-phosphoglucomutase;
DE AltName: Full=Glucose phosphomutase;
GN Name=pgcA; Synonyms=gtaC, gtaE, yhxB; OrderedLocusNames=BSU09310;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ROLE IN LTA AND WTAS
RP BIOSYNTHESIS, PATHWAY, ROLE IN BIOFILM FORMATION, AND MUTAGENESIS OF
RP GLY-162; THR-240; GLY-407 AND ASP-418.
RC STRAIN=168;
RX PubMed=15640167; DOI=10.1128/aem.71.1.39-45.2005;
RA Lazarevic V., Soldo B., Medico N., Pooley H.M., Bron S., Karamata D.;
RT "Bacillus subtilis alpha-phosphoglucomutase is required for normal cell
RT morphology and biofilm formation.";
RL Appl. Environ. Microbiol. 71:39-45(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION TO 141 AND 189-207.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
RX PubMed=2127799; DOI=10.1099/00221287-136-12-2367;
RA Holmberg C., Beijer L., Rutberg B., Rutberg L.;
RT "Glycerol catabolism in Bacillus subtilis: nucleotide sequence of the genes
RT encoding glycerol kinase (glpK) and glycerol-3-phosphate dehydrogenase
RT (glpD).";
RL J. Gen. Microbiol. 136:2367-2375(1990).
RN [6]
RP ROLE IN BIOFILM FORMATION.
RC STRAIN=168, and 3610;
RX PubMed=15175311; DOI=10.1128/jb.186.12.3970-3979.2004;
RA Branda S.S., Gonzalez-Pastor J.E., Dervyn E., Ehrlich S.D., Losick R.,
RA Kolter R.;
RT "Genes involved in formation of structured multicellular communities by
RT Bacillus subtilis.";
RL J. Bacteriol. 186:3970-3979(2004).
CC -!- FUNCTION: Catalyzes the interconversion between glucose-6-phosphate and
CC alpha-glucose-1-phosphate. This is the first step in the biosynthesis
CC of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant
CC glycolipid found in B.subtilis membrane, which is also used as a
CC membrane anchor for lipoteichoic acid (LTA). Has a role in the
CC biosynthesis of all phosphate-containing envelope polymers, since
CC glucose-1-phosphate is the precursor of UDP-glucose, which serves as a
CC glucosyl donor not only for the biosynthesis of LTA but also for wall
CC teichoic acids (WTAs). Is required for biofilm formation. This is
CC likely due to another role of UDP-glucose, which might also act as a
CC metabolic signal regulating biofilm formation or may be involved in
CC some unknown biosynthetic pathway essential for biofilm formation, e.g.
CC the synthesis of an exopolysaccharide. {ECO:0000269|PubMed:15175311,
CC ECO:0000269|PubMed:15640167}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
CC {ECO:0000269|PubMed:15640167}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; AJ784890; CAH04980.1; -; Genomic_DNA.
DR EMBL; Y14079; CAA74431.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12759.2; -; Genomic_DNA.
DR EMBL; M34393; AAA22488.1; -; Genomic_DNA.
DR PIR; C69835; C69835.
DR RefSeq; NP_388812.2; NC_000964.3.
DR RefSeq; WP_003244986.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P18159; -.
DR SMR; P18159; -.
DR IntAct; P18159; 1.
DR MINT; P18159; -.
DR STRING; 224308.BSU09310; -.
DR jPOST; P18159; -.
DR PRIDE; P18159; -.
DR EnsemblBacteria; CAB12759; CAB12759; BSU_09310.
DR GeneID; 936247; -.
DR KEGG; bsu:BSU09310; -.
DR PATRIC; fig|224308.179.peg.1004; -.
DR eggNOG; COG1109; Bacteria.
DR InParanoid; P18159; -.
DR OMA; GYDRRFM; -.
DR PhylomeDB; P18159; -.
DR BioCyc; BSUB:BSU09310-MON; -.
DR BioCyc; MetaCyc:MON-6122; -.
DR SABIO-RK; P18159; -.
DR UniPathway; UPA00894; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0008973; F:phosphopentomutase activity; IBA:GO_Central.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IBA:GO_Central.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glucose metabolism; Isomerase; Magnesium;
KW Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..581
FT /note="Phosphoglucomutase"
FT /id="PRO_0000148020"
FT ACT_SITE 146
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MUTAGEN 162
FT /note="G->D: Very low enzymatic activity. Great decrease in
FT biofilm formation. Deformed cell morphology."
FT /evidence="ECO:0000269|PubMed:15640167"
FT MUTAGEN 240
FT /note="T->I: Impaired enzymatic activity. Great decrease in
FT biofilm formation. Deformed cell morphology."
FT /evidence="ECO:0000269|PubMed:15640167"
FT MUTAGEN 407
FT /note="G->D: Loss of enzymatic activity. Great decrease in
FT biofilm formation. Deformed cell morphology."
FT /evidence="ECO:0000269|PubMed:15640167"
FT MUTAGEN 418
FT /note="D->N: Impaired enzymatic activity. Great decrease in
FT biofilm formation. Deformed cell morphology."
FT /evidence="ECO:0000269|PubMed:15640167"
FT CONFLICT 141
FT /note="I -> V (in Ref. 2; CAA74431)"
FT /evidence="ECO:0000305"
FT CONFLICT 189..207
FT /note="DEENKLKEKGLIKIIGEDI -> VRY (in Ref. 2; CAA74431)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 581 AA; 64663 MW; E8F2823808BFCDF0 CRC64;
MTWRKSYERW KQTEHLDLEL KERLIELEGD EQALEDCFYK DLEFGTGGMR GEIGAGTNRM
NIYTVRKASA GFAAYISKQG EEAKKRGVVI AYDSRHKSPE FAMEAAKTLA TQGIQTYVFD
ELRPTPELSF AVRQLNAYGG IVVTASHNPP EYNGYKVYGD DGGQLPPKEA DIVIEQVNAI
ENELTITVDE ENKLKEKGLI KIIGEDIDKV YTEKLTSISV HPELSEEVDV KVVFTPLHGT
ANKPVRRGLE ALGYKNVTVV KEQELPDSNF STVTSPNPEE HAAFEYAIKL GEEQNADILI
ATDPDADRLG IAVKNDQGKY TVLTGNQTGA LLLHYLLSEK KKQGILPDNG VVLKTIVTSE
IGRAVASSFG LDTIDTLTGF KFIGEKIKEY EASGQYTFQF GYEESYGYLI GDFARDKDAI
QAALLAVEVC AFYKKQGMSL YEALINLFNE YGFYREGLKS LTLKGKQGAE QIEAILASFR
QNPPQKMAGK QVVTAEDYAV SKRTLLTESK EEAIDLPKSN VLKYFLEDGS WFCLRPSGTE
PKVKFYFAVK GSSLEDSEKR LAVLSEDVMK TVDEIVESTA K
