PGM1_RABIT
ID PGM1_RABIT Reviewed; 562 AA.
AC P00949; P38651;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Phosphoglucomutase-1;
DE Short=PGM 1;
DE EC=5.4.2.2 {ECO:0000269|PubMed:1328221};
DE AltName: Full=Glucose phosphomutase 1;
GN Name=PGM1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=6223925; DOI=10.1016/s0021-9258(17)44646-1;
RA Ray W.J. Jr., Hermodson M.A., Puvathingal J.M., Mahoney W.C.;
RT "The complete amino acid sequence of rabbit muscle phosphoglucomutase.";
RL J. Biol. Chem. 258:9166-9174(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1530890; DOI=10.1073/pnas.89.1.411;
RA Whitehouse D.B., Putt W., Lovegrove J.U., Morrison K.E., Hollyoake M.,
RA Fox M.F., Hopkinson D.A., Edwards Y.H.;
RT "Phosphoglucomutase 1: complete human and rabbit mRNA sequences and direct
RT mapping of this highly polymorphic marker on human chromosome 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:411-415(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND CATALYTIC
RP ACTIVITY.
RC TISSUE=Skeletal muscle;
RX PubMed=1328221; DOI=10.1016/s0021-9258(19)36800-0;
RA Lee Y.S., Marks A.R., Gureckas N., Lacro R., Nadal-Ginard B., Kim D.H.;
RT "Purification, characterization, and molecular cloning of a 60-kDa
RT phosphoprotein in rabbit skeletal sarcoplasmic reticulum which is an
RT isoform of phosphoglucomutase.";
RL J. Biol. Chem. 267:21080-21088(1992).
RN [4]
RP ACTIVE SITE.
RX PubMed=5669853; DOI=10.1042/bj1090093;
RA Milstein C.P., Milstein C.;
RT "A tryptic peptide containing a unique serine phosphate residue in rabbit
RT phosphoglucomutase.";
RL Biochem. J. 109:93-99(1968).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=1532581; DOI=10.1016/s0021-9258(18)42699-3;
RA Dai J.-B., Liu Y., Ray W.J. Jr., Konno M.;
RT "The crystal structure of muscle phosphoglucomutase refined at 2.7-A
RT resolution.";
RL J. Biol. Chem. 267:6322-6337(1992).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=15299904; DOI=10.1107/s0907444997000887;
RA Ray W.J. Jr., Baranidharan S., Liu Y.;
RT "Enhanced diffractivity of phosphoglucomutase crystals. Use of an
RT alternative cryocrystallographic procedure.";
RL Acta Crystallogr. D 53:385-391(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, SUBUNIT,
RP ACTIVITY REGULATION, AND PHOSPHORYLATION AT SER-117.
RX PubMed=15299905; DOI=10.1107/s0907444997000875;
RA Liu Y., Ray W.J. Jr., Baranidharan S.;
RT "Structure of rabbit muscle phosphoglucomutase refined at 2.4-A
RT resolution.";
RL Acta Crystallogr. D 53:392-405(1997).
RN [8] {ECO:0007744|PDB:1C47}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ALPHA-D-GLUCOSE
RP 1,6-BISPHOSPHATE.
RA Baranidharan S., Ray W.J. Jr., Liu Y.;
RT "Binding driven structural changes in crystaline phosphoglucomutase
RT associated with chemical reaction.";
RL Submitted (AUG-1999) to the PDB data bank.
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
RA Baranidharan S., Ray W.J. Jr.;
RT "Structural relationships at the active site of Phos in analog complexes.";
RL Submitted (AUG-1999) to the PDB data bank.
CC -!- FUNCTION: This enzyme participates in both the breakdown and synthesis
CC of glucose.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000269|PubMed:1328221};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15299905};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:15299905};
CC -!- ACTIVITY REGULATION: Glucose-1,6-bisphosphate enhances phosphorylation
CC of the active site Ser-117, and thereby increases enzyme activity.
CC {ECO:0000305|PubMed:15299905}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:6223925}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Sarcoplasmic reticulum
CC {ECO:0000269|PubMed:1328221}. Note=Localizes to the junctional skeletal
CC sarcoplasmic reticulum, probably by association with phospholipids
CC and/or other proteins. {ECO:0000269|PubMed:1328221}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P00949-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P00949-2; Sequence=VSP_004690, VSP_004691, VSP_004692,
CC VSP_004693;
CC -!- PTM: Isoform 2 is the major calmodulin-dependent phosphoprotein in
CC junctional skeletal sarcoplasmic reticulum vesicles.
CC {ECO:0000269|PubMed:1328221}.
CC -!- PTM: Phosphorylation at Thr-467 by PAK1 significantly enhances
CC enzymatic activity. {ECO:0000250|UniProtKB:P36871}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/PGM/";
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DR EMBL; M97664; AAA31454.1; -; mRNA.
DR EMBL; M97663; AAA31453.1; -; mRNA.
DR PIR; A45077; PMRBI.
DR PIR; B41801; PMRB.
DR RefSeq; NP_001075785.1; NM_001082316.1. [P00949-2]
DR PDB; 1C47; X-ray; 2.70 A; A/B=2-562.
DR PDB; 1C4G; X-ray; 2.70 A; A/B=2-562.
DR PDB; 1JDY; X-ray; 2.70 A; A/B=2-562.
DR PDB; 1LXT; X-ray; 2.70 A; A/B=2-562.
DR PDB; 1VKL; X-ray; 2.70 A; A/B=2-562.
DR PDB; 3PMG; X-ray; 2.40 A; A/B=2-562.
DR PDBsum; 1C47; -.
DR PDBsum; 1C4G; -.
DR PDBsum; 1JDY; -.
DR PDBsum; 1LXT; -.
DR PDBsum; 1VKL; -.
DR PDBsum; 3PMG; -.
DR AlphaFoldDB; P00949; -.
DR PCDDB; P00949; -.
DR SMR; P00949; -.
DR STRING; 9986.ENSOCUP00000025628; -.
DR PRIDE; P00949; -.
DR GeneID; 100009155; -.
DR KEGG; ocu:100009155; -.
DR CTD; 5236; -.
DR eggNOG; KOG0027; Eukaryota.
DR eggNOG; KOG0625; Eukaryota.
DR InParanoid; P00949; -.
DR OrthoDB; 555015at2759; -.
DR EvolutionaryTrace; P00949; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004614; F:phosphoglucomutase activity; IDA:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IDA:UniProtKB.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573; PTHR22573; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Carbohydrate metabolism;
KW Cytoplasm; Direct protein sequencing; Glucose metabolism; Isomerase;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome;
KW Sarcoplasmic reticulum.
FT CHAIN 1..562
FT /note="Phosphoglucomutase-1"
FT /id="PRO_0000147779"
FT ACT_SITE 117
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000269|PubMed:5669853"
FT BINDING 23
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1C47"
FT BINDING 117
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1C47"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000269|PubMed:15299905,
FT ECO:0007744|PDB:3PMG"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15299905,
FT ECO:0007744|PDB:3PMG"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15299905,
FT ECO:0007744|PDB:3PMG"
FT BINDING 292
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1C47"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15299905,
FT ECO:0007744|PDB:3PMG"
FT BINDING 293
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1C47"
FT BINDING 357
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1C47"
FT BINDING 376
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1C47"
FT BINDING 378
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1C47"
FT BINDING 389
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1C47"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P36871"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P36871"
FT MOD_RES 115
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0F9"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15299905,
FT ECO:0007744|PDB:3PMG"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38652"
FT MOD_RES 185
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P36871"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38652"
FT MOD_RES 349
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0F9"
FT MOD_RES 353
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0F9"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38652"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36871"
FT MOD_RES 419
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0F9"
FT MOD_RES 467
FT /note="Phosphothreonine; by PAK1"
FT /evidence="ECO:0000250|UniProtKB:P36871"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38652"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36871"
FT MOD_RES 507
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0F9"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36871"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38652"
FT VAR_SEQ 1..13
FT /note="MVKIVTVKTKAYP -> MEEGPLPLLTIRTAPYH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1328221"
FT /id="VSP_004690"
FT VAR_SEQ 25..36
FT /note="RVKVFQSSTNYA -> KTYYFEDKPCYL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1328221"
FT /id="VSP_004691"
FT VAR_SEQ 44..56
FT /note="ISTVEPAQRQEAT -> FFSIDLKDRQGSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1328221"
FT /id="VSP_004692"
FT VAR_SEQ 65..77
FT /note="FYMKEAIQLIVRI -> YFNKSAIETILQM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1328221"
FT /id="VSP_004693"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:3PMG"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1JDY"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1C47"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:3PMG"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3PMG"
FT TURN 266..269
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 270..277
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:1C47"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 306..315
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 321..326
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 340..346
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 359..367
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:3PMG"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 391..405
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 409..420
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 422..433
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 435..450
FT /evidence="ECO:0007829|PDB:3PMG"
FT TURN 452..456
FT /evidence="ECO:0007829|PDB:1C47"
FT STRAND 458..461
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 464..473
FT /evidence="ECO:0007829|PDB:3PMG"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 490..494
FT /evidence="ECO:0007829|PDB:3PMG"
FT TURN 495..497
FT /evidence="ECO:0007829|PDB:1LXT"
FT STRAND 499..506
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 512..522
FT /evidence="ECO:0007829|PDB:3PMG"
FT TURN 525..529
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 532..547
FT /evidence="ECO:0007829|PDB:3PMG"
FT HELIX 549..553
FT /evidence="ECO:0007829|PDB:3PMG"
FT STRAND 559..562
FT /evidence="ECO:0007829|PDB:3PMG"
SQ SEQUENCE 562 AA; 61558 MW; 6D9F42284EF09002 CRC64;
MVKIVTVKTK AYPDQKPGTS GLRKRVKVFQ SSTNYAENFI QSIISTVEPA QRQEATLVVG
GDGRFYMKEA IQLIVRIAAA NGIGRLVIGQ NGILSTPAVS CIIRKIKAIG GIILTASHNP
GGPNGDFGIK FNISNGGPAP EAITDKIFQI SKTIEEYAIC PDLKVDLGVL GKQQFDLENK
FKPFTVEIVD SVEAYATMLR NIFDFNALKE LLSGPNRLKI RIDAMHGVVG PYVKKILCEE
LGAPANSAVN CVPLEDFGGH HPDPNLTYAA DLVETMKSGE HDFGAAFDGD GDRNMILGKH
GFFVNPSDSV AVIAANIFSI PYFQQTGVRG FARSMPTSGA LDRVANATKI ALYETPTGWK
FFGNLMDASK LSLCGEESFG TGSDHIREKD GLWAVLAWLS ILATRKQSVE DILKDHWHKF
GRNFFTRYDY EEVEAEGATK MMKDLEALMF DRSFVGKQFS ANDKVYTVEK ADNFEYHDPV
DGSVSKNQGL RLIFADGSRI IFRLSGTGSA GATIRLYIDS YEKDNAKINQ DPQVMLAPLI
SIALKVSQLQ ERTGRTAPTV IT
