DB code: M00017

CATH domain 3.40.120.10 : Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 3 Catalytic domain
3.40.120.10 : Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 3 Catalytic domain
3.40.120.10 : Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 3 Catalytic domain
3.30.310.50 : TATA-Binding Protein
E.C. 5.4.2.2
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P00949 Phosphoglucomutase-1
PGM 1
EC 5.4.2.2
Glucose phosphomutase 1
NP_001075785.1 (Protein)
NM_001082316.1 (DNA/RNA sequence)
PF02878 (PGM_PMM_I)
PF02879 (PGM_PMM_II)
PF02880 (PGM_PMM_III)
PF00408 (PGM_PMM_IV)
[Graphical View]
P47244 Phosphoglucomutase-1
PGM 1
EC 5.4.2.2
Glucose phosphomutase 1
Parafusin
Pf
pp63
XP_001429571.1 (Protein)
XM_001429534.1 (DNA/RNA sequence)
PF02878 (PGM_PMM_I)
PF02879 (PGM_PMM_II)
PF02880 (PGM_PMM_III)
PF00408 (PGM_PMM_IV)
[Graphical View]

KEGG enzyme name
phosphoglucomutase
glucose phosphomutase
phosphoglucose mutase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P00949 PGM1_RABIT Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate. Monomer. Isoform 1: Cytoplasm. Isoform 2: Sarcoplasmic reticulum. Note=Localizes to the junctional skeletal sarcoplasmic reticulum, probably by association with phospholipids and/or other proteins. Binds 1 magnesium ion per subunit.
P47244 PGM1_PARTE Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate. Cytoplasm. Binds 1 magnesium ion per subunit.

KEGG Pathways
Map code Pathways E.C.
MAP00010 Glycolysis / Gluconeogenesis
MAP00030 Pentose phosphate pathway
MAP00052 Galactose metabolism
MAP00500 Starch and sucrose metabolism
MAP00521 Streptomycin biosynthesis

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C00103 C00620 C01171 C00668 C03736 C03735 C00660
E.C.
Compound Magnesium alpha-D-Glucose 1-phosphate alpha-D-Ribose 1-phosphate alpha-D-Hexose 1-phosphate alpha-D-Glucose 6-phosphate alpha-D-Ribose 5-phosphate alpha-D-Hexose 6-phosphate D-Glucose 1,6-bisphosphate Transition from Ser to 6-OH
Type divalent metal (Ca2+, Mg2+) carbohydrate,phosphate group/phosphate ion carbohydrate,phosphate group/phosphate ion carbohydrate,phosphate group/phosphate ion carbohydrate,phosphate group/phosphate ion carbohydrate,phosphate group/phosphate ion carbohydrate,phosphate group/phosphate ion
ChEBI 18420
18420
29042
29042
16300
16300
16326
16326
17665
17665
18189
18189
PubChem 888
888
65533
65533
439236
439236
439426
439426
439284
439284
440101
440101
440100
440100
1c47A01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c47B01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c4gA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c4gB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jdyA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jdyB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lxtA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lxtB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1vklA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1vklB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2pmgA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2pmgB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3pmgA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3pmgB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfiA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfiB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfqA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfqB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c47A02 Analogue:_CD Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c47B02 Analogue:_CD Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c4gA02 Analogue:_CO Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c4gB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jdyA02 Analogue:_CD Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jdyB02 Analogue:_CD Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lxtA02 Analogue:_CD Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lxtB02 Analogue:_CD Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1vklA02 Analogue:_NI Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1vklB02 Analogue:_NI Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2pmgA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2pmgB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3pmgA02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3pmgB02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfiA02 Analogue:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfiB02 Analogue:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfqA02 Analogue:_CA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfqB02 Analogue:_CA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c47A03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:G16 Unbound
1c47B03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c4gA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:VG1
1c4gB03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jdyA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jdyB03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lxtA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lxtB03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1vklA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1vklB03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2pmgA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2pmgB03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3pmgA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3pmgB03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfiA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfiB03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfqA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfqB03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c47A04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c47B04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c4gA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c4gB04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jdyA04 Unbound Analogue:SO4 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jdyB04 Unbound Analogue:SO4 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lxtA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lxtB04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1vklA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1vklB04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2pmgA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2pmgB04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3pmgA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3pmgB04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfiA04 Unbound Analogue:SO4 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfiB04 Unbound Analogue:SO4 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfqA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfqB04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [14], [16], [17]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1c47A01 ARG 22;SER 116;HIS 117;LYS 129 SER 116(Magnesium binding)
1c47B01 ARG 22;SER 116;HIS 117;LYS 129 SER 116(Magnesium binding)
1c4gA01 ARG 22;SER 116;HIS 117;LYS 129 SER 116(Magnesium binding)
1c4gB01 ARG 22;SER 116;HIS 117;LYS 129 SER 116(Magnesium binding)
1jdyA01 ARG 22; ;HIS 117;LYS 129 SEP 116(Magnesium binding) SEP 116(Phosphonoserine)
1jdyB01 ARG 22; ;HIS 117;LYS 129 SEP 116(Magnesium binding) SEP 116(Phosphonoserine)
1lxtA01 ARG 22;SER 116;HIS 117;LYS 129 SER 116(Magnesium binding)
1lxtB01 ARG 22;SER 116;HIS 117;LYS 129 SER 116(Magnesium binding)
1vklA01 ARG 22; ;HIS 117;LYS 129 SER 116(Magnesium binding) SEP 116(Phosphonoserine)
1vklB01 ARG 22; ;HIS 117;LYS 129 SER 116(Magnesium binding) SEP 116(Phosphonoserine)
2pmgA01 ARG 22;SER 116;HIS 117;LYS 129 SER 116(Magnesium binding)
2pmgB01 ARG 22;SER 116;HIS 117;LYS 129 SER 116(Magnesium binding)
3pmgA01 ARG 22;SER 116;HIS 117;LYS 129 SER 116(Magnesium binding) SEP 116(Phosphorylation)
3pmgB01 ARG 22;SER 116;HIS 117;LYS 129 SER 116(Magnesium binding) SEP 116(Phosphorylation)
1kfiA01 ARG 27;SER 126;HIS 127;LYS 140 SER 126(Magnesium binding) SER 126(Phosphorylation)
1kfiB01 ARG 27;SER 126;HIS 127;LYS 140 SER 126(Magnesium binding) SER 126(Phosphorylation)
1kfqA01 ARG 27;SER 126;HIS 127;LYS 140 SER 126(Magnesium binding) SER 126(Phosphorylation)
1kfqB01 ARG 27;SER 126;HIS 127;LYS 140 SER 126(Magnesium binding) SER 126(Phosphorylation)
1c47A02 ARG 292 ASP 287;ASP 289;ASP 291(Magnesium binding)
1c47B02 ARG 292 ASP 287;ASP 289;ASP 291(Magnesium binding)
1c4gA02 ARG 292 ASP 287;ASP 289;ASP 291(Magnesium binding)
1c4gB02 ARG 292 ASP 287;ASP 289;ASP 291(Magnesium binding)
1jdyA02 ARG 292 ASP 287;ASP 289;ASP 291(Magnesium binding)
1jdyB02 ARG 292 ASP 287;ASP 289;ASP 291(Magnesium binding)
1lxtA02 ARG 292 ASP 287;ASP 289;ASP 291(Magnesium binding)
1lxtB02 ARG 292 ASP 287;ASP 289;ASP 291(Magnesium binding)
1vklA02 ARG 292 ASP 287;ASP 289;ASP 291(Magnesium binding)
1vklB02 ARG 292 ASP 287;ASP 289;ASP 291(Magnesium binding)
2pmgA02 ARG 292 ASP 287;ASP 289;ASP 291(Magnesium binding)
2pmgB02 ARG 292 ASP 287;ASP 289;ASP 291(Magnesium binding)
3pmgA02 ARG 292 ASP 287;ASP 289;ASP 291(Magnesium binding)
3pmgB02 ARG 292 ASP 287;ASP 289;ASP 291(Magnesium binding)
1kfiA02 ARG 313 ASP 308;ASP 310;ASP 312(Magnesium binding)
1kfiB02 ARG 313 ASP 308;ASP 310;ASP 312(Magnesium binding)
1kfqA02 ARG 313 ASP 308;ASP 310;ASP 312(Magnesium binding)
1kfqB02 ARG 313 ASP 308;ASP 310;ASP 312(Magnesium binding)
1c47A03 LYS 388
1c47B03 LYS 388
1c4gA03 LYS 388
1c4gB03 LYS 388
1jdyA03 LYS 388
1jdyB03 LYS 388
1lxtA03 LYS 388
1lxtB03 LYS 388
1vklA03 LYS 388
1vklB03 LYS 388
2pmgA03 LYS 388
2pmgB03 LYS 388
3pmgA03 LYS 388
3pmgB03 LYS 388
1kfiA03 LYS 405
1kfiB03 LYS 405
1kfqA03 LYS 405
1kfqB03 LYS 405
1c47A04
1c47B04
1c4gA04
1c4gB04
1jdyA04
1jdyB04
1lxtA04
1lxtB04
1vklA04
1vklB04
2pmgA04
2pmgB04
3pmgA04
3pmgB04
1kfiA04
1kfiB04
1kfqA04
1kfqB04

References for Catalytic Mechanism
References Sections No. 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]
Resource
Comments ACTIVE SITE
Medline ID 68368401
PubMed ID 5669853
Journal Biochem J
Year 1968
Volume 109
Pages 93-9
Authors Milstein CP, Milstein C
Title A tryptic peptide containing a unique serine phosphate residue in rabbit phosphoglucomutase.
Related PDB
Related UniProtKB P00949
[2]
Resource
Comments
Medline ID
PubMed ID 5041899
Journal Biochemistry
Year 1972
Volume 11
Pages 2800-4
Authors Ray WJ Jr, Goodin DS, Ng L
Title Cobalt (II) and nickel (II) complexes of phosphoglucomutase.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 4830239
Journal J Biol Chem
Year 1974
Volume 249
Pages 3166-9
Authors Walinder O, Joshi JG
Title Mechanism of action of rabbit muscle phosphoglucomutase. Rate of enzyme phosphate turnover studied with a rapid mixing technique.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 6115419
Journal Philos Trans R Soc Lond B Biol Sci
Year 1981
Volume 293
Pages 205-8
Authors Wierenga RK, Lewis DG, Rossmann MG, Ray WJ Jr
Title The structure determination of rabbit phosphoglucomutase.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 2934384
Journal J Biol Chem
Year 1986
Volume 261
Pages 264-74
Authors Lin Z, Konno M, Abad-Zapatero C, Wierenga R, Murthy MR, Ray WJ Jr, Rossmann MG
Title The structure of rabbit muscle phosphoglucomutase at intermediate resolution.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 2974722
Journal Biochemistry
Year 1988
Volume 27
Pages 7328-32
Authors Kim SC, Raushel FM
Title Mechanism-based inactivation of rabbit muscle phosphoglucomutase by nojirimycin 6-phosphate.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 1712631
Journal Biochemistry
Year 1991
Volume 30
Pages 6866-75
Authors Ray WJ Jr, Bolin JT, Puvathingal JM, Minor W, Liu YW, Muchmore SW
Title Removal 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.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 1829964
Journal Biochemistry
Year 1991
Volume 30
Pages 6875-85
Authors Ray WJ Jr, Puvathingal JM, Liu YW
Title Formation of substrate and transition-state analogue complexes in crystals of phosphoglucomutase after removing the crystallization salt.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 1531025
Journal Biochemistry
Year 1992
Volume 31
Pages 498-505
Authors Percival MD, Withers SG
Title Binding energy and catalysis: deoxyfluoro sugars as probes of hydrogen bonding in phosphoglucomutase.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 1531026
Journal Biochemistry
Year 1992
Volume 31
Pages 505-12
Authors Percival MD, Withers SG
Title 19F NMR investigations of the catalytic mechanism of phosphoglucomutase using fluorinated substrates and inhibitors.
Related PDB
Related UniProtKB
[11]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)
Medline ID 92210613
PubMed ID 1532581
Journal J Biol Chem
Year 1992
Volume 267
Pages 6322-37
Authors Dai JB, Liu Y, Ray WJ Jr, Konno M
Title The crystal structure of muscle phosphoglucomutase refined at 2.7-angstrom resolution.
Related PDB 2pmg
Related UniProtKB P00949
[12]
Resource
Comments
Medline ID
PubMed ID 8418859
Journal Biochemistry
Year 1993
Volume 32
Pages 48-57
Authors Ray WJ Jr, Post CB, Liu Y, Rhyu GI
Title Structural changes at the metal ion binding site during the phosphoglucomutase reaction.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 8418857
Journal Biochemistry
Year 1993
Volume 32
Pages 38-47
Authors Ray WJ Jr, Post CB, Puvathingal JM
Title Reaction of the isosteric methylenephosphonate analog of alpha-D-glucose 1-phosphate with phosphoglucomutase. Induced-fit specificity revisited.
Related PDB
Related UniProtKB
[14]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)
Medline ID
PubMed ID 15299905
Journal Acta Crystallogr D Biol Crystallogr
Year 1997
Volume 53
Pages 392-405
Authors Liu Y, Ray WJ Jr, Baranidharan S
Title Structure of rabbit muscle phosphoglucomutase refined at 2.4-A
Related PDB 1lxt
Related UniProtKB P00949
[15]
Resource
Comments
Medline ID
PubMed ID 10506283
Journal Protein Eng
Year 1999
Volume 12
Pages 737-46
Authors Levin S, Almo SC, Satir BH
Title Functional diversity of the phosphoglucomutase superfamily: structural implications.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 11779235
Journal J Mol Biol
Year 2002
Volume 315
Pages 141-53
Authors Muller S, Diederichs K, Breed J, Kissmehl R, Hauser K, Plattner H, Welte W
Title Crystal structure analysis of the exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutase), from Paramecium reveals significant conformational variability.
Related PDB 1kfi 1kfq
Related UniProtKB P47244
[17]
Resource
Comments
Medline ID
PubMed ID 11839312
Journal Structure (Camb)
Year 2002
Volume 10
Pages 269-79
Authors Regni C, Tipton PA, Beamer LJ
Title Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 12924943
Journal Biochemistry
Year 2003
Volume 42
Pages 9946-51
Authors Naught LE, Regni C, Beamer LJ, Tipton PA
Title Roles of active site residues in Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 14725765
Journal Structure (Camb)
Year 2004
Volume 12
Pages 55-63
Authors Regni C, Naught L, Tipton PA, Beamer LJ
Title Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa.
Related PDB
Related UniProtKB

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:

Created Updated
2005-06-10 2009-02-26