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Protein

Phosphoglucomutase-1

Gene

PGM1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This enzyme participates in both the breakdown and synthesis of glucose.

Catalytic activityi

Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei19 – 191Substrate1 Publication
Binding sitei23 – 231Substrate2 Publications
Active sitei117 – 1171Phosphoserine intermediate1 Publication
Metal bindingi117 – 1171Magnesium; via phosphate group1 Publication
Binding sitei130 – 1301Substrate1 Publication
Metal bindingi288 – 2881Magnesium1 Publication
Metal bindingi290 – 2901Magnesium1 Publication
Metal bindingi292 – 2921Magnesium1 Publication
Binding sitei357 – 3571Substrate1 Publication
Binding sitei389 – 3891Substrate2 Publications
Binding sitei515 – 5151Substrate1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglucomutase-1 (EC:5.4.2.21 Publication)
Short name:
PGM 1
Alternative name(s):
Glucose phosphomutase 1
Gene namesi
Name:PGM1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

Isoform 2 :
  • Sarcoplasmic reticulum 1 Publication

  • Note: Localizes to the junctional skeletal sarcoplasmic reticulum, probably by association with phospholipids and/or other proteins.1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 562562Phosphoglucomutase-1PRO_0000147779Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei16 – 161N6-acetyllysineBy similarity
Modified residuei115 – 1151PhosphothreonineBy similarity
Modified residuei117 – 1171PhosphoserineBy similarity
Modified residuei134 – 1341PhosphoserineBy similarity
Modified residuei185 – 1851PhosphothreonineBy similarity
Modified residuei213 – 2131PhosphoserineBy similarity
Modified residuei349 – 3491N6-acetyllysineBy similarity
Modified residuei353 – 3531PhosphotyrosineBy similarity
Modified residuei369 – 3691PhosphoserineBy similarity
Modified residuei378 – 3781PhosphoserineBy similarity
Modified residuei419 – 4191N6-succinyllysineBy similarity
Modified residuei467 – 4671Phosphothreonine; by PAK1By similarity
Modified residuei485 – 4851PhosphoserineBy similarity
Modified residuei505 – 5051PhosphoserineBy similarity
Modified residuei507 – 5071PhosphothreonineBy similarity
Modified residuei509 – 5091PhosphoserineBy similarity
Modified residuei541 – 5411PhosphoserineBy similarity

Post-translational modificationi

Isoform 2 is the major calmodulin-dependent phosphoprotein in junctional skeletal sarcoplasmic reticulum vesicles.1 Publication
Phosphorylation at Thr-467 by PAK1 significantly enhances enzymatic activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP00949.

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
562
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Beta strandi21 – 255Combined sources
Helixi26 – 316Combined sources
Helixi35 – 4511Combined sources
Helixi49 – 513Combined sources
Turni52 – 543Combined sources
Beta strandi56 – 616Combined sources
Helixi67 – 8014Combined sources
Beta strandi85 – 939Combined sources
Helixi96 – 10611Combined sources
Beta strandi109 – 1146Combined sources
Beta strandi125 – 1339Combined sources
Beta strandi136 – 1383Combined sources
Helixi141 – 15313Combined sources
Beta strandi156 – 1594Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi171 – 1755Combined sources
Beta strandi184 – 1896Combined sources
Helixi193 – 2008Combined sources
Helixi205 – 2139Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi220 – 2234Combined sources
Helixi230 – 2378Combined sources
Turni238 – 2414Combined sources
Helixi245 – 2473Combined sources
Beta strandi248 – 2503Combined sources
Helixi257 – 2593Combined sources
Turni266 – 2694Combined sources
Helixi270 – 2778Combined sources
Beta strandi282 – 2876Combined sources
Beta strandi289 – 2913Combined sources
Beta strandi294 – 2985Combined sources
Helixi299 – 3013Combined sources
Helixi306 – 31510Combined sources
Helixi317 – 3193Combined sources
Helixi321 – 3266Combined sources
Beta strandi331 – 3344Combined sources
Helixi340 – 3467Combined sources
Beta strandi348 – 3503Combined sources
Beta strandi352 – 3554Combined sources
Helixi359 – 3679Combined sources
Beta strandi372 – 3765Combined sources
Turni377 – 3793Combined sources
Beta strandi380 – 3834Combined sources
Beta strandi386 – 3883Combined sources
Helixi391 – 40515Combined sources
Helixi409 – 42012Combined sources
Beta strandi422 – 43312Combined sources
Helixi435 – 45016Combined sources
Turni452 – 4565Combined sources
Beta strandi458 – 4614Combined sources
Beta strandi464 – 47310Combined sources
Turni479 – 4813Combined sources
Beta strandi490 – 4945Combined sources
Turni495 – 4973Combined sources
Beta strandi499 – 5068Combined sources
Beta strandi508 – 5103Combined sources
Beta strandi512 – 52211Combined sources
Turni525 – 5295Combined sources
Helixi532 – 54716Combined sources
Helixi549 – 5535Combined sources
Beta strandi559 – 5624Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C47X-ray2.70A/B2-562[»]
1C4GX-ray2.70A/B2-562[»]
1JDYX-ray2.70A/B2-562[»]
1LXTX-ray2.70A/B2-562[»]
1VKLX-ray2.70A/B2-562[»]
3PMGX-ray2.40A/B2-562[»]
ProteinModelPortaliP00949.
SMRiP00949. Positions 2-562.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00949.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni117 – 1182Substrate binding2 Publications
Regioni292 – 2932Substrate binding2 Publications
Regioni376 – 3783Substrate binding2 Publications

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

HOGENOMiHOG000009550.
HOVERGENiHBG001599.
InParanoidiP00949.
KOiK01835.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. 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]
PfamiPF02878. 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]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P00949-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVKIVTVKTK AYPDQKPGTS GLRKRVKVFQ SSTNYAENFI QSIISTVEPA
60 70 80 90 100
QRQEATLVVG GDGRFYMKEA IQLIVRIAAA NGIGRLVIGQ NGILSTPAVS
110 120 130 140 150
CIIRKIKAIG GIILTASHNP GGPNGDFGIK FNISNGGPAP EAITDKIFQI
160 170 180 190 200
SKTIEEYAIC PDLKVDLGVL GKQQFDLENK FKPFTVEIVD SVEAYATMLR
210 220 230 240 250
NIFDFNALKE LLSGPNRLKI RIDAMHGVVG PYVKKILCEE LGAPANSAVN
260 270 280 290 300
CVPLEDFGGH HPDPNLTYAA DLVETMKSGE HDFGAAFDGD GDRNMILGKH
310 320 330 340 350
GFFVNPSDSV AVIAANIFSI PYFQQTGVRG FARSMPTSGA LDRVANATKI
360 370 380 390 400
ALYETPTGWK FFGNLMDASK LSLCGEESFG TGSDHIREKD GLWAVLAWLS
410 420 430 440 450
ILATRKQSVE DILKDHWHKF GRNFFTRYDY EEVEAEGATK MMKDLEALMF
460 470 480 490 500
DRSFVGKQFS ANDKVYTVEK ADNFEYHDPV DGSVSKNQGL RLIFADGSRI
510 520 530 540 550
IFRLSGTGSA GATIRLYIDS YEKDNAKINQ DPQVMLAPLI SIALKVSQLQ
560
ERTGRTAPTV IT
Length:562
Mass (Da):61,558
Last modified:January 23, 2007 - v2
Checksum:i6D9F42284EF09002
GO
Isoform 2 (identifier: P00949-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MVKIVTVKTKAYP → MEEGPLPLLTIRTAPYH
     25-36: RVKVFQSSTNYA → KTYYFEDKPCYL
     44-56: ISTVEPAQRQEAT → FFSIDLKDRQGSS
     65-77: FYMKEAIQLIVRI → YFNKSAIETILQM

Show »
Length:566
Mass (Da):62,193
Checksum:iDB76D766775F9F13
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1313MVKIV…TKAYP → MEEGPLPLLTIRTAPYH in isoform 2. 1 PublicationVSP_004690Add
BLAST
Alternative sequencei25 – 3612RVKVF…STNYA → KTYYFEDKPCYL in isoform 2. 1 PublicationVSP_004691Add
BLAST
Alternative sequencei44 – 5613ISTVE…RQEAT → FFSIDLKDRQGSS in isoform 2. 1 PublicationVSP_004692Add
BLAST
Alternative sequencei65 – 7713FYMKE…LIVRI → YFNKSAIETILQM in isoform 2. 1 PublicationVSP_004693Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97664 mRNA. Translation: AAA31454.1.
M97663 mRNA. Translation: AAA31453.1.
PIRiA45077. PMRBI.
B41801. PMRB.
RefSeqiNP_001075785.1. NM_001082316.1. [P00949-2]
UniGeneiOcu.1953.

Genome annotation databases

GeneIDi100009155.
KEGGiocu:100009155.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97664 mRNA. Translation: AAA31454.1.
M97663 mRNA. Translation: AAA31453.1.
PIRiA45077. PMRBI.
B41801. PMRB.
RefSeqiNP_001075785.1. NM_001082316.1. [P00949-2]
UniGeneiOcu.1953.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C47X-ray2.70A/B2-562[»]
1C4GX-ray2.70A/B2-562[»]
1JDYX-ray2.70A/B2-562[»]
1LXTX-ray2.70A/B2-562[»]
1VKLX-ray2.70A/B2-562[»]
3PMGX-ray2.40A/B2-562[»]
ProteinModelPortaliP00949.
SMRiP00949. Positions 2-562.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP00949.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009155.
KEGGiocu:100009155.

Organism-specific databases

CTDi5236.

Phylogenomic databases

HOGENOMiHOG000009550.
HOVERGENiHBG001599.
InParanoidiP00949.
KOiK01835.

Miscellaneous databases

EvolutionaryTraceiP00949.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. 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]
PfamiPF02878. 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]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The complete amino acid sequence of rabbit muscle phosphoglucomutase."
    Ray W.J. Jr., Hermodson M.A., Puvathingal J.M., Mahoney W.C.
    J. Biol. Chem. 258:9166-9174(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (ISOFORM 1).
    Tissue: Muscle.
  2. "Phosphoglucomutase 1: complete human and rabbit mRNA sequences and direct mapping of this highly polymorphic marker on human chromosome 1."
    Whitehouse D.B., Putt W., Lovegrove J.U., Morrison K.E., Hollyoake M., Fox M.F., Hopkinson D.A., Edwards Y.H.
    Proc. Natl. Acad. Sci. U.S.A. 89:411-415(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Purification, characterization, and molecular cloning of a 60-kDa phosphoprotein in rabbit skeletal sarcoplasmic reticulum which is an isoform of phosphoglucomutase."
    Lee Y.S., Marks A.R., Gureckas N., Lacro R., Nadal-Ginard B., Kim D.H.
    J. Biol. Chem. 267:21080-21088(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
    Tissue: Skeletal muscle.
  4. "A tryptic peptide containing a unique serine phosphate residue in rabbit phosphoglucomutase."
    Milstein C.P., Milstein C.
    Biochem. J. 109:93-99(1968) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE.
  5. "The crystal structure of muscle phosphoglucomutase refined at 2.7-A resolution."
    Dai J.-B., Liu Y., Ray W.J. Jr., Konno M.
    J. Biol. Chem. 267:6322-6337(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  6. "Enhanced diffractivity of phosphoglucomutase crystals. Use of an alternative cryocrystallographic procedure."
    Ray W.J. Jr., Baranidharan S., Liu Y.
    Acta Crystallogr. D 53:385-391(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  7. "Structure of rabbit muscle phosphoglucomutase refined at 2.4-A resolution."
    Liu Y., Ray W.J. Jr., Baranidharan S.
    Acta Crystallogr. D 53:392-405(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, SUBUNIT.
  8. "Binding driven structural changes in crystaline phosphoglucomutase associated with chemical reaction."
    Baranidharan S., Ray W.J. Jr., Liu Y.
    Submitted (AUG-1999) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ALPHA-D-GLUCOSE 1,6-BISPHOSPHATE.
  9. "Structural relationships at the active site of Phos in analog complexes."
    Baranidharan S., Ray W.J. Jr.
    Submitted (AUG-1999) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.

Entry informationi

Entry nameiPGM1_RABIT
AccessioniPrimary (citable) accession number: P00949
Secondary accession number(s): P38651
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.