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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)DescriptionActionsGraphical viewLength
Binding sitei19Substrate1 Publication1
Binding sitei23Substrate2 Publications1
Active sitei117Phosphoserine intermediate1 Publication1
Metal bindingi117Magnesium; via phosphate group1 Publication1
Binding sitei130Substrate1 Publication1
Metal bindingi288Magnesium1 Publication1
Metal bindingi290Magnesium1 Publication1
Metal bindingi292Magnesium1 Publication1
Binding sitei357Substrate1 Publication1
Binding sitei389Substrate2 Publications1
Binding sitei515Substrate1 Publication1

GO - Molecular functioni

  • magnesium ion binding Source: UniProtKB
  • phosphoglucomutase activity Source: UniProtKB

GO - Biological processi

  • glucose metabolic process Source: UniProtKB
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)DescriptionActionsGraphical viewLength
ChainiPRO_00001477791 – 562Phosphoglucomutase-1Add BLAST562

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei16N6-acetyllysineBy similarity1
Modified residuei115PhosphothreonineBy similarity1
Modified residuei117PhosphoserineBy similarity1
Modified residuei134PhosphoserineBy similarity1
Modified residuei185PhosphothreonineBy similarity1
Modified residuei213PhosphoserineBy similarity1
Modified residuei349N6-acetyllysineBy similarity1
Modified residuei353PhosphotyrosineBy similarity1
Modified residuei369PhosphoserineBy similarity1
Modified residuei378PhosphoserineBy similarity1
Modified residuei419N6-succinyllysineBy similarity1
Modified residuei467Phosphothreonine; by PAK1By similarity1
Modified residuei485PhosphoserineBy similarity1
Modified residuei505PhosphoserineBy similarity1
Modified residuei507PhosphothreonineBy similarity1
Modified residuei509PhosphoserineBy similarity1
Modified residuei541PhosphoserineBy similarity1

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

1562
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Beta strandi21 – 25Combined sources5
Helixi26 – 31Combined sources6
Helixi35 – 45Combined sources11
Helixi49 – 51Combined sources3
Turni52 – 54Combined sources3
Beta strandi56 – 61Combined sources6
Helixi67 – 80Combined sources14
Beta strandi85 – 93Combined sources9
Helixi96 – 106Combined sources11
Beta strandi109 – 114Combined sources6
Beta strandi125 – 133Combined sources9
Beta strandi136 – 138Combined sources3
Helixi141 – 153Combined sources13
Beta strandi156 – 159Combined sources4
Beta strandi167 – 169Combined sources3
Beta strandi171 – 175Combined sources5
Beta strandi184 – 189Combined sources6
Helixi193 – 200Combined sources8
Helixi205 – 213Combined sources9
Beta strandi214 – 216Combined sources3
Beta strandi220 – 223Combined sources4
Helixi230 – 237Combined sources8
Turni238 – 241Combined sources4
Helixi245 – 247Combined sources3
Beta strandi248 – 250Combined sources3
Helixi257 – 259Combined sources3
Turni266 – 269Combined sources4
Helixi270 – 277Combined sources8
Beta strandi282 – 287Combined sources6
Beta strandi289 – 291Combined sources3
Beta strandi294 – 298Combined sources5
Helixi299 – 301Combined sources3
Helixi306 – 315Combined sources10
Helixi317 – 319Combined sources3
Helixi321 – 326Combined sources6
Beta strandi331 – 334Combined sources4
Helixi340 – 346Combined sources7
Beta strandi348 – 350Combined sources3
Beta strandi352 – 355Combined sources4
Helixi359 – 367Combined sources9
Beta strandi372 – 376Combined sources5
Turni377 – 379Combined sources3
Beta strandi380 – 383Combined sources4
Beta strandi386 – 388Combined sources3
Helixi391 – 405Combined sources15
Helixi409 – 420Combined sources12
Beta strandi422 – 433Combined sources12
Helixi435 – 450Combined sources16
Turni452 – 456Combined sources5
Beta strandi458 – 461Combined sources4
Beta strandi464 – 473Combined sources10
Turni479 – 481Combined sources3
Beta strandi490 – 494Combined sources5
Turni495 – 497Combined sources3
Beta strandi499 – 506Combined sources8
Beta strandi508 – 510Combined sources3
Beta strandi512 – 522Combined sources11
Turni525 – 529Combined sources5
Helixi532 – 547Combined sources16
Helixi549 – 553Combined sources5
Beta strandi559 – 562Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00949.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni117 – 118Substrate binding2 Publications2
Regioni292 – 293Substrate binding2 Publications2
Regioni376 – 378Substrate binding2 Publications3

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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0046901 – 13MVKIV…TKAYP → MEEGPLPLLTIRTAPYH in isoform 2. 1 PublicationAdd BLAST13
Alternative sequenceiVSP_00469125 – 36RVKVF…STNYA → KTYYFEDKPCYL in isoform 2. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_00469244 – 56ISTVE…RQEAT → FFSIDLKDRQGSS in isoform 2. 1 PublicationAdd BLAST13
Alternative sequenceiVSP_00469365 – 77FYMKE…LIVRI → YFNKSAIETILQM in isoform 2. 1 PublicationAdd BLAST13

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
PDB 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.
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...

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: November 2, 2016
This is version 143 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.