EzCatDB: M00017
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DB codeM00017
CATH domainDomain 13.40.120.10 : Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 3Catalytic domain
Domain 23.40.120.10 : Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 3Catalytic domain
Domain 33.40.120.10 : Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 3Catalytic domain
Domain 43.30.310.50 : TATA-Binding Protein
E.C.5.4.2.2


Enzyme Name
UniProtKBKEGG

P00949P47244
Protein namePhosphoglucomutase-1Phosphoglucomutase-1phosphoglucomutase
glucose phosphomutase
phosphoglucose mutase
SynonymsPGM 1
EC 5.4.2.2
Glucose phosphomutase 1
PGM 1
EC 5.4.2.2
Glucose phosphomutase 1
Parafusin
Pf
pp63
RefSeqNP_001075785.1 (Protein)
NM_001082316.1 (DNA/RNA sequence)
XP_001429571.1 (Protein)
XM_001429534.1 (DNA/RNA sequence)
PfamPF02878 (PGM_PMM_I)
PF02879 (PGM_PMM_II)
PF02880 (PGM_PMM_III)
PF00408 (PGM_PMM_IV)
[Graphical view]
PF02878 (PGM_PMM_I)
PF02879 (PGM_PMM_II)
PF02880 (PGM_PMM_III)
PF00408 (PGM_PMM_IV)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00010Glycolysis / Gluconeogenesis
MAP00030Pentose phosphate pathway
MAP00052Galactose metabolism
MAP00500Starch and sucrose metabolism
MAP00521Streptomycin biosynthesis

UniProtKB:Accession NumberP00949P47244
Entry namePGM1_RABITPGM1_PARTE
ActivityAlpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
SubunitMonomer.
Subcellular locationIsoform 1: Cytoplasm.,Isoform 2: Sarcoplasmic reticulum. Note=Localizes to the junctional skeletal sarcoplasmic reticulum, probably by association with phospholipids and/or other proteins.Cytoplasm.
CofactorBinds 1 magnesium ion per subunit.Binds 1 magnesium ion per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00305C00103C00620C01171C00668C03736C03735C00660
CompoundMagnesiumalpha-D-Glucose 1-phosphatealpha-D-Ribose 1-phosphatealpha-D-Hexose 1-phosphatealpha-D-Glucose 6-phosphatealpha-D-Ribose 5-phosphatealpha-D-Hexose 6-phosphateD-Glucose 1,6-bisphosphateTransition from Ser to 6-OH
Typedivalent metal (Ca2+, Mg2+)carbohydrate,phosphate group/phosphate ioncarbohydrate,phosphate group/phosphate ioncarbohydrate,phosphate group/phosphate ioncarbohydrate,phosphate group/phosphate ioncarbohydrate,phosphate group/phosphate ioncarbohydrate,phosphate group/phosphate ion

ChEBI18420
29042
16300
16326
17665
18189



PubChem888
65533
439236
439426
439284
440101
440100


                 
1c47A01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1c47B01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1c4gA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1c4gB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jdyA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jdyB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lxtA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lxtB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1vklA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1vklB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2pmgA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2pmgB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3pmgA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3pmgB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kfiA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kfiB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kfqA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kfqB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1c47A02Analogue:_CDUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1c47B02Analogue:_CDUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1c4gA02Analogue:_COUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1c4gB02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jdyA02Analogue:_CDUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jdyB02Analogue:_CDUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lxtA02Analogue:_CDUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lxtB02Analogue:_CDUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1vklA02Analogue:_NIUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1vklB02Analogue:_NIUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2pmgA02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2pmgB02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3pmgA02Bound:_MGUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3pmgB02Bound:_MGUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kfiA02Analogue:_ZNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kfiB02Analogue:_ZNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kfqA02Analogue:_CAUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kfqB02Analogue:_CAUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1c47A03UnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-bound:G16Unbound
1c47B03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1c4gA03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:VG1
1c4gB03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jdyA03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jdyB03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lxtA03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lxtB03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1vklA03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1vklB03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2pmgA03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2pmgB03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3pmgA03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3pmgB03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kfiA03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kfiB03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kfqA03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kfqB03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1c47A04UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1c47B04UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1c4gA04UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1c4gB04UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jdyA04UnboundAnalogue:SO4UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jdyB04UnboundAnalogue:SO4UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lxtA04UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lxtB04UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1vklA04UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1vklB04UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2pmgA04UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2pmgB04UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3pmgA04UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3pmgB04UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kfiA04UnboundAnalogue:SO4UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kfiB04UnboundAnalogue:SO4UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kfqA04UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kfqB04UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [14], [16], [17]
pdbCatalytic residuesCofactor-binding residuesModified residues
           
1c47A01ARG 22;SER 116;HIS 117;LYS 129
SER 116(Magnesium binding)
                        
1c47B01ARG 22;SER 116;HIS 117;LYS 129
SER 116(Magnesium binding)
                        
1c4gA01ARG 22;SER 116;HIS 117;LYS 129
SER 116(Magnesium binding)
                        
1c4gB01ARG 22;SER 116;HIS 117;LYS 129
SER 116(Magnesium binding)
                        
1jdyA01ARG 22;       ;HIS 117;LYS 129
SEP 116(Magnesium binding)
SEP 116(Phosphonoserine)
1jdyB01ARG 22;       ;HIS 117;LYS 129
SEP 116(Magnesium binding)
SEP 116(Phosphonoserine)
1lxtA01ARG 22;SER 116;HIS 117;LYS 129
SER 116(Magnesium binding)
                        
1lxtB01ARG 22;SER 116;HIS 117;LYS 129
SER 116(Magnesium binding)
                        
1vklA01ARG 22;       ;HIS 117;LYS 129
SER 116(Magnesium binding)
SEP 116(Phosphonoserine)
1vklB01ARG 22;       ;HIS 117;LYS 129
SER 116(Magnesium binding)
SEP 116(Phosphonoserine)
2pmgA01ARG 22;SER 116;HIS 117;LYS 129
SER 116(Magnesium binding)
                        
2pmgB01ARG 22;SER 116;HIS 117;LYS 129
SER 116(Magnesium binding)
                        
3pmgA01ARG 22;SER 116;HIS 117;LYS 129
SER 116(Magnesium binding)
SEP 116(Phosphorylation)
3pmgB01ARG 22;SER 116;HIS 117;LYS 129
SER 116(Magnesium binding)
SEP 116(Phosphorylation)
1kfiA01ARG 27;SER 126;HIS 127;LYS 140
SER 126(Magnesium binding)
SER 126(Phosphorylation)
1kfiB01ARG 27;SER 126;HIS 127;LYS 140
SER 126(Magnesium binding)
SER 126(Phosphorylation)
1kfqA01ARG 27;SER 126;HIS 127;LYS 140
SER 126(Magnesium binding)
SER 126(Phosphorylation)
1kfqB01ARG 27;SER 126;HIS 127;LYS 140
SER 126(Magnesium binding)
SER 126(Phosphorylation)
1c47A02ARG 292
ASP 287;ASP 289;ASP 291(Magnesium binding)
 
1c47B02ARG 292
ASP 287;ASP 289;ASP 291(Magnesium binding)
 
1c4gA02ARG 292
ASP 287;ASP 289;ASP 291(Magnesium binding)
 
1c4gB02ARG 292
ASP 287;ASP 289;ASP 291(Magnesium binding)
 
1jdyA02ARG 292
ASP 287;ASP 289;ASP 291(Magnesium binding)
 
1jdyB02ARG 292
ASP 287;ASP 289;ASP 291(Magnesium binding)
 
1lxtA02ARG 292
ASP 287;ASP 289;ASP 291(Magnesium binding)
 
1lxtB02ARG 292
ASP 287;ASP 289;ASP 291(Magnesium binding)
 
1vklA02ARG 292
ASP 287;ASP 289;ASP 291(Magnesium binding)
 
1vklB02ARG 292
ASP 287;ASP 289;ASP 291(Magnesium binding)
 
2pmgA02ARG 292
ASP 287;ASP 289;ASP 291(Magnesium binding)
 
2pmgB02ARG 292
ASP 287;ASP 289;ASP 291(Magnesium binding)
 
3pmgA02ARG 292
ASP 287;ASP 289;ASP 291(Magnesium binding)
 
3pmgB02ARG 292
ASP 287;ASP 289;ASP 291(Magnesium binding)
 
1kfiA02ARG 313
ASP 308;ASP 310;ASP 312(Magnesium binding)
 
1kfiB02ARG 313
ASP 308;ASP 310;ASP 312(Magnesium binding)
 
1kfqA02ARG 313
ASP 308;ASP 310;ASP 312(Magnesium binding)
 
1kfqB02ARG 313
ASP 308;ASP 310;ASP 312(Magnesium binding)
 
1c47A03LYS 388
 
 
1c47B03LYS 388
 
 
1c4gA03LYS 388
 
 
1c4gB03LYS 388
 
 
1jdyA03LYS 388
 
 
1jdyB03LYS 388
 
 
1lxtA03LYS 388
 
 
1lxtB03LYS 388
 
 
1vklA03LYS 388
 
 
1vklB03LYS 388
 
 
2pmgA03LYS 388
 
 
2pmgB03LYS 388
 
 
3pmgA03LYS 388
 
 
3pmgB03LYS 388
 
 
1kfiA03LYS 405
 
 
1kfiB03LYS 405
 
 
1kfqA03LYS 405
 
 
1kfqB03LYS 405
 
 
1c47A04       
 
 
1c47B04       
 
 
1c4gA04       
 
 
1c4gB04       
 
 
1jdyA04       
 
 
1jdyB04       
 
 
1lxtA04       
 
 
1lxtB04       
 
 
1vklA04       
 
 
1vklB04       
 
 
2pmgA04       
 
 
2pmgB04       
 
 
3pmgA04       
 
 
3pmgB04       
 
 
1kfiA04       
 
 
1kfiB04       
 
 
1kfqA04       
 
 
1kfqB04       
 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[9]Scheme II, p.504
[10]p.511-512
[11]p.6328-6329
[12]p.52-55
[14]p.404-405
[16]p.148
[17]Fig.5, p.275-277
[18]Chart 1, p.9948-9950
[19]Fig.1, p.60-61

references
[1]
CommentsACTIVE SITE
Medline ID68368401
PubMed ID5669853
JournalBiochem J
Year1968
Volume109
Pages93-9
AuthorsMilstein CP, Milstein C
TitleA tryptic peptide containing a unique serine phosphate residue in rabbit phosphoglucomutase.
Related UniProtKBP00949
[2]
PubMed ID5041899
JournalBiochemistry
Year1972
Volume11
Pages2800-4
AuthorsRay WJ Jr, Goodin DS, Ng L
TitleCobalt (II) and nickel (II) complexes of phosphoglucomutase.
[3]
PubMed ID4830239
JournalJ Biol Chem
Year1974
Volume249
Pages3166-9
AuthorsWalinder O, Joshi JG
TitleMechanism of action of rabbit muscle phosphoglucomutase. Rate of enzyme phosphate turnover studied with a rapid mixing technique.
[4]
PubMed ID6115419
JournalPhilos Trans R Soc Lond B Biol Sci
Year1981
Volume293
Pages205-8
AuthorsWierenga RK, Lewis DG, Rossmann MG, Ray WJ Jr
TitleThe structure determination of rabbit phosphoglucomutase.
[5]
PubMed ID2934384
JournalJ Biol Chem
Year1986
Volume261
Pages264-74
AuthorsLin Z, Konno M, Abad-Zapatero C, Wierenga R, Murthy MR, Ray WJ Jr, Rossmann MG
TitleThe structure of rabbit muscle phosphoglucomutase at intermediate resolution.
[6]
PubMed ID2974722
JournalBiochemistry
Year1988
Volume27
Pages7328-32
AuthorsKim SC, Raushel FM
TitleMechanism-based inactivation of rabbit muscle phosphoglucomutase by nojirimycin 6-phosphate.
[7]
PubMed ID1712631
JournalBiochemistry
Year1991
Volume30
Pages6866-75
AuthorsRay WJ Jr, Bolin JT, Puvathingal JM, Minor W, Liu YW, Muchmore SW
TitleRemoval of salt from a salt-induced protein crystal without cross-linking. Preliminary examination of "desalted" crystals of phosphoglucomutase by X-ray crystallography at low temperature.
[8]
PubMed ID1829964
JournalBiochemistry
Year1991
Volume30
Pages6875-85
AuthorsRay WJ Jr, Puvathingal JM, Liu YW
TitleFormation of substrate and transition-state analogue complexes in crystals of phosphoglucomutase after removing the crystallization salt.
[9]
PubMed ID1531025
JournalBiochemistry
Year1992
Volume31
Pages498-505
AuthorsPercival MD, Withers SG
TitleBinding energy and catalysis: deoxyfluoro sugars as probes of hydrogen bonding in phosphoglucomutase.
[10]
PubMed ID1531026
JournalBiochemistry
Year1992
Volume31
Pages505-12
AuthorsPercival MD, Withers SG
Title19F NMR investigations of the catalytic mechanism of phosphoglucomutase using fluorinated substrates and inhibitors.
[11]
CommentsX-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)
Medline ID92210613
PubMed ID1532581
JournalJ Biol Chem
Year1992
Volume267
Pages6322-37
AuthorsDai JB, Liu Y, Ray WJ Jr, Konno M
TitleThe crystal structure of muscle phosphoglucomutase refined at 2.7-angstrom resolution.
Related PDB2pmg
Related UniProtKBP00949
[12]
PubMed ID8418859
JournalBiochemistry
Year1993
Volume32
Pages48-57
AuthorsRay WJ Jr, Post CB, Liu Y, Rhyu GI
TitleStructural changes at the metal ion binding site during the phosphoglucomutase reaction.
[13]
PubMed ID8418857
JournalBiochemistry
Year1993
Volume32
Pages38-47
AuthorsRay WJ Jr, Post CB, Puvathingal JM
TitleReaction of the isosteric methylenephosphonate analog of alpha-D-glucose 1-phosphate with phosphoglucomutase. Induced-fit specificity revisited.
[14]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)
PubMed ID15299905
JournalActa Crystallogr D Biol Crystallogr
Year1997
Volume53
Pages392-405
AuthorsLiu Y, Ray WJ Jr, Baranidharan S
TitleStructure of rabbit muscle phosphoglucomutase refined at 2.4-A
Related PDB1lxt
Related UniProtKBP00949
[15]
PubMed ID10506283
JournalProtein Eng
Year1999
Volume12
Pages737-46
AuthorsLevin S, Almo SC, Satir BH
TitleFunctional diversity of the phosphoglucomutase superfamily: structural implications.
[16]
PubMed ID11779235
JournalJ Mol Biol
Year2002
Volume315
Pages141-53
AuthorsMuller S, Diederichs K, Breed J, Kissmehl R, Hauser K, Plattner H, Welte W
TitleCrystal structure analysis of the exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutase), from Paramecium reveals significant conformational variability.
Related PDB1kfi,1kfq
Related UniProtKBP47244
[17]
PubMed ID11839312
JournalStructure (Camb)
Year2002
Volume10
Pages269-79
AuthorsRegni C, Tipton PA, Beamer LJ
TitleCrystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors.
[18]
PubMed ID12924943
JournalBiochemistry
Year2003
Volume42
Pages9946-51
AuthorsNaught LE, Regni C, Beamer LJ, Tipton PA
TitleRoles of active site residues in Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase.
[19]
PubMed ID14725765
JournalStructure (Camb)
Year2004
Volume12
Pages55-63
AuthorsRegni C, Naught L, Tipton PA, Beamer LJ
TitleStructural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa.

comments
This enzyme catalyzes two phosphoryl transfer reactions as follows:
(A) Transfer of phosphoryl group from hydroxyl group of Ser116 to 6-OH of glucose-1-phosphate, forming glucose-1,6-diphosphate:
(B) Transfer of phosphoryl group from 1-OH of a glucose-1,6-diphosphate intermediate to Ser:

createdupdated
2005-06-102009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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