Reviewed, UniProtKB/Swiss-Prot P00949 (PGM1_RABIT)

Names and origin

Protein names

Recommended name:
    Phosphoglucomutase-1
      Short name=PGM 1
    EC=5.4.2.2
Alternative name(s):
    Glucose phosphomutase 1

Gene names

Name:

PGM1

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	562 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This enzyme participates in both the breakdown and synthesis of glucose.
Catalytic activity	Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
Cofactor	Binds 1 magnesium ion per subunit.
Subunit structure	Monomer.
Subcellular location	Isoform 1: Cytoplasm. Isoform 2: Sarcoplasmic reticulum. Note: Localizes to the junctional skeletal sarcoplasmic reticulum, probably by association with phospholipids and/or other proteins.
Post-translational modification	Isoform 2 is the major calmodulin-dependent phosphoprotein in junctional skeletal sarcoplasmic reticulum vesicles.
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Cellular component	Cytoplasm Sarcoplasmic reticulum
Coding sequence diversity	Alternative splicing
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	sarcoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoglucomutase activity Inferred from sequence or structural similarity. Source: AgBase
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P00949-1)

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.

Isoform 2 (identifier: P00949-2)

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

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 562

561

Phosphoglucomutase-1

PRO_0000147779

Sites

Active site

117

1

Phosphoserine intermediate Ref.4

Metal binding

117

1

Magnesium; via phosphate group

Metal binding

288

1

Magnesium

Metal binding

290

1

Magnesium

Metal binding

292

1

Magnesium

Amino acid modifications

Modified residue

16

1

N6-acetyllysine By similarity

Modified residue

115

1

Phosphothreonine By similarity

Modified residue

117

1

Phosphoserine By similarity

Modified residue

353

1

Phosphotyrosine By similarity

Modified residue

419

1

N6-acetyllysine By similarity

Natural variations

Alternative sequence

1 – 13

13

MVKIV…TKAYP → MEEGPLPLLTIRTAPYH in isoform 2.

VSP_004690

Alternative sequence

25 – 36

12

RVKVF…STNYA → KTYYFEDKPCYL in isoform 2.

VSP_004691

Alternative sequence

44 – 56

13

ISTVE…RQEAT → FFSIDLKDRQGSS in isoform 2.

VSP_004692

Alternative sequence

65 – 77

13

FYMKE…LIVRI → YFNKSAIETILQM in isoform 2.

VSP_004693

Secondary structure

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562

Helix Strand Turn

Details...

Beta strand

5 – 8

4

Beta strand

21 – 25

5

Helix

26 – 31

6

Helix

35 – 45

11

Helix

49 – 51

3

Turn

52 – 54

3

Beta strand

56 – 61

6

Helix

67 – 80

14

Beta strand

85 – 93

9

Helix

96 – 106

11

Beta strand

109 – 114

6

Beta strand

125 – 133

9

Beta strand

136 – 138

3

Helix

141 – 153

13

Beta strand

156 – 159

4

Beta strand

171 – 175

5

Beta strand

184 – 189

6

Helix

193 – 200

8

Helix

205 – 213

9

Beta strand

220 – 223

4

Helix

230 – 237

8

Turn

238 – 241

4

Helix

245 – 247

3

Beta strand

248 – 250

3

Helix

257 – 259

3

Turn

266 – 269

4

Helix

270 – 277

8

Beta strand

282 – 287

6

Beta strand

294 – 298

5

Helix

299 – 301

3

Helix

306 – 315

10

Helix

317 – 319

3

Helix

321 – 326

6

Beta strand

331 – 334

4

Helix

340 – 346

7

Beta strand

348 – 350

3

Beta strand

352 – 355

4

Helix

359 – 367

9

Beta strand

372 – 376

5

Turn

377 – 379

3

Beta strand

380 – 383

4

Beta strand

386 – 388

3

Helix

391 – 405

15

Helix

409 – 420

12

Beta strand

422 – 433

12

Helix

435 – 450

16

Beta strand

458 – 461

4

Beta strand

464 – 473

10

Turn

479 – 481

3

Beta strand

490 – 494

5

Beta strand

499 – 506

8

Beta strand

508 – 510

3

Beta strand

512 – 522

11

Turn

525 – 529

5

Helix

532 – 547

16

Helix

549 – 553

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6D9F42284EF09002	FASTA	562	61,558
	10 20 30 40 50 60 MVKIVTVKTK AYPDQKPGTS GLRKRVKVFQ SSTNYAENFI QSIISTVEPA QRQEATLVVG 70 80 90 100 110 120 GDGRFYMKEA IQLIVRIAAA NGIGRLVIGQ NGILSTPAVS CIIRKIKAIG GIILTASHNP 130 140 150 160 170 180 GGPNGDFGIK FNISNGGPAP EAITDKIFQI SKTIEEYAIC PDLKVDLGVL GKQQFDLENK 190 200 210 220 230 240 FKPFTVEIVD SVEAYATMLR NIFDFNALKE LLSGPNRLKI RIDAMHGVVG PYVKKILCEE 250 260 270 280 290 300 LGAPANSAVN CVPLEDFGGH HPDPNLTYAA DLVETMKSGE HDFGAAFDGD GDRNMILGKH 310 320 330 340 350 360 GFFVNPSDSV AVIAANIFSI PYFQQTGVRG FARSMPTSGA LDRVANATKI ALYETPTGWK 370 380 390 400 410 420 FFGNLMDASK LSLCGEESFG TGSDHIREKD GLWAVLAWLS ILATRKQSVE DILKDHWHKF 430 440 450 460 470 480 GRNFFTRYDY EEVEAEGATK MMKDLEALMF DRSFVGKQFS ANDKVYTVEK ADNFEYHDPV 490 500 510 520 530 540 DGSVSKNQGL RLIFADGSRI IFRLSGTGSA GATIRLYIDS YEKDNAKINQ DPQVMLAPLI 550 560 SIALKVSQLQ ERTGRTAPTV IT
	Isoform 2. Checksum: DB76D766775F9F13	FASTA	566	62,193
	10 20 30 40 50 60 MEEGPLPLLT IRTAPYHDQK PGTSGLRKKT YYFEDKPCYL ENFIQSIFFS IDLKDRQGSS 70 80 90 100 110 120 LVVGGDGRYF NKSAIETILQ MAAANGIGRL VIGQNGILST PAVSCIIRKI KAIGGIILTA 130 140 150 160 170 180 SHNPGGPNGD FGIKFNISNG GPAPEAITDK IFQISKTIEE YAICPDLKVD LGVLGKQQFD 190 200 210 220 230 240 LENKFKPFTV EIVDSVEAYA TMLRNIFDFN ALKELLSGPN RLKIRIDAMH GVVGPYVKKI 250 260 270 280 290 300 LCEELGAPAN SAVNCVPLED FGGHHPDPNL TYAADLVETM KSGEHDFGAA FDGDGDRNMI 310 320 330 340 350 360 LGKHGFFVNP SDSVAVIAAN IFSIPYFQQT GVRGFARSMP TSGALDRVAN ATKIALYETP 370 380 390 400 410 420 TGWKFFGNLM DASKLSLCGE ESFGTGSDHI REKDGLWAVL AWLSILATRK QSVEDILKDH 430 440 450 460 470 480 WHKFGRNFFT RYDYEEVEAE GATKMMKDLE ALMFDRSFVG KQFSANDKVY TVEKADNFEY 490 500 510 520 530 540 HDPVDGSVSK NQGLRLIFAD GSRIIFRLSG TGSAGATIRL YIDSYEKDNA KINQDPQVML 550 560 APLISIALKV SQLQERTGRT APTVIT

References

[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: 6223925] [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: 1530890] [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: 1328221] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). 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: 5669853] [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: 1532581] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[6]	"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: 15299905] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBLGenBankDDBJ

M97664 mRNA. Translation: AAA31454.1.
M97663 mRNA. Translation: AAA31453.1.

PIR

PMRBI. A45077.
PMRB. B41801.

RefSeq

NP_001075785.1.

UniGene

Ocu.1953

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C47	X-ray	2.70	A/B	2-562	[»]
1C4G	X-ray	2.70	A/B	2-562	[»]
1JDY	X-ray	2.70	A/B	2-561	[»]
1LXT	X-ray	2.70	A/B	2-562	[»]
1VKL	X-ray	2.70	A/B	2-561	[»]
3PMG	X-ray	2.40	A/B	2-562	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P00949.

Genome annotation databases

Ensembl

ENSOCUT00000000288; ENSOCUP00000000253; ENSOCUG00000000287; Oryctolagus cuniculus. [Genome view]

GeneID

100009155.

Organism-specific databases

CTD

100009155.

Phylogenomic databases

HOVERGEN

P00949.

Enzyme and pathway databases

BRENDA

5.4.2.2. 255.

Family and domain databases

InterPro

IPR005844. 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. A-D-PHexomutase_N.
[Graphical view]

Gene3D

G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 2 hits.

Pfam

PF02878. 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]

PRINTS

PR00509. PGMPMM.

PROSITE

PS00710. PGM_PMM. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PGM1_RABIT

Accession

Primary (citable) accession number: P00949
Secondary accession number(s): P38651

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	October 13, 2009
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)