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Phosphoglucomutase-1 (PGM 1) (EC 5.4.2.2) (Glucose phosphomutase 1)

 PGM1_RABIT              Reviewed;         562 AA.
P00949; P38651;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-FEB-2018, entry version 147.
RecName: Full=Phosphoglucomutase-1;
Short=PGM 1;
EC=5.4.2.2 {ECO:0000269|PubMed:1328221};
AltName: Full=Glucose phosphomutase 1;
Name=PGM1;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
PROTEIN SEQUENCE (ISOFORM 1).
TISSUE=Muscle;
PubMed=6223925;
Ray W.J. Jr., Hermodson M.A., Puvathingal J.M., Mahoney W.C.;
"The complete amino acid sequence of rabbit muscle
phosphoglucomutase.";
J. Biol. Chem. 258:9166-9174(1983).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1530890; DOI=10.1073/pnas.89.1.411;
Whitehouse D.B., Putt W., Lovegrove J.U., Morrison K.E., Hollyoake M.,
Fox M.F., Hopkinson D.A., Edwards Y.H.;
"Phosphoglucomutase 1: complete human and rabbit mRNA sequences and
direct mapping of this highly polymorphic marker on human chromosome
1.";
Proc. Natl. Acad. Sci. U.S.A. 89:411-415(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
CATALYTIC ACTIVITY.
TISSUE=Skeletal muscle;
PubMed=1328221;
Lee Y.S., Marks A.R., Gureckas N., Lacro R., Nadal-Ginard B.,
Kim D.H.;
"Purification, characterization, and molecular cloning of a 60-kDa
phosphoprotein in rabbit skeletal sarcoplasmic reticulum which is an
isoform of phosphoglucomutase.";
J. Biol. Chem. 267:21080-21088(1992).
[4]
ACTIVE SITE.
PubMed=5669853; DOI=10.1042/bj1090093;
Milstein C.P., Milstein C.;
"A tryptic peptide containing a unique serine phosphate residue in
rabbit phosphoglucomutase.";
Biochem. J. 109:93-99(1968).
[5]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
PubMed=1532581;
Dai J.-B., Liu Y., Ray W.J. Jr., Konno M.;
"The crystal structure of muscle phosphoglucomutase refined at 2.7-A
resolution.";
J. Biol. Chem. 267:6322-6337(1992).
[6]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
PubMed=15299904; DOI=10.1107/S0907444997000887;
Ray W.J. Jr., Baranidharan S., Liu Y.;
"Enhanced diffractivity of phosphoglucomutase crystals. Use of an
alternative cryocrystallographic procedure.";
Acta Crystallogr. D 53:385-391(1997).
[7]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, AND
SUBUNIT.
PubMed=15299905; DOI=10.1107/S0907444997000875;
Liu Y., Ray W.J. Jr., Baranidharan S.;
"Structure of rabbit muscle phosphoglucomutase refined at 2.4-A
resolution.";
Acta Crystallogr. D 53:392-405(1997).
[8]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ALPHA-D-GLUCOSE
1,6-BISPHOSPHATE.
Baranidharan S., Ray W.J. Jr., Liu Y.;
"Binding driven structural changes in crystaline phosphoglucomutase
associated with chemical reaction.";
Submitted (AUG-1999) to the PDB data bank.
[9]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOG.
Baranidharan S., Ray W.J. Jr.;
"Structural relationships at the active site of Phos in analog
complexes.";
Submitted (AUG-1999) to the PDB data bank.
-!- FUNCTION: This enzyme participates in both the breakdown and
synthesis of glucose.
-!- CATALYTIC ACTIVITY: Alpha-D-glucose 1-phosphate = alpha-D-glucose
6-phosphate. {ECO:0000269|PubMed:1328221}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:15299905};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000269|PubMed:15299905};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:6223925}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 2: Sarcoplasmic reticulum
{ECO:0000269|PubMed:1328221}. Note=Localizes to the junctional
skeletal sarcoplasmic reticulum, probably by association with
phospholipids and/or other proteins. {ECO:0000269|PubMed:1328221}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P00949-1; Sequence=Displayed;
Name=2;
IsoId=P00949-2; Sequence=VSP_004690, VSP_004691, VSP_004692,
VSP_004693;
-!- PTM: Isoform 2 is the major calmodulin-dependent phosphoprotein in
junctional skeletal sarcoplasmic reticulum vesicles.
{ECO:0000269|PubMed:1328221}.
-!- PTM: Phosphorylation at Thr-467 by PAK1 significantly enhances
enzymatic activity. {ECO:0000250|UniProtKB:P36871}.
-!- SIMILARITY: Belongs to the phosphohexose mutase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/PGM/";
-----------------------------------------------------------------------
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EMBL; M97664; AAA31454.1; -; mRNA.
EMBL; M97663; AAA31453.1; -; mRNA.
PIR; A45077; PMRBI.
PIR; B41801; PMRB.
RefSeq; NP_001075785.1; NM_001082316.1. [P00949-2]
UniGene; Ocu.1953; -.
PDB; 1C47; X-ray; 2.70 A; A/B=2-562.
PDB; 1C4G; X-ray; 2.70 A; A/B=2-562.
PDB; 1JDY; X-ray; 2.70 A; A/B=2-562.
PDB; 1LXT; X-ray; 2.70 A; A/B=2-562.
PDB; 1VKL; X-ray; 2.70 A; A/B=2-562.
PDB; 3PMG; X-ray; 2.40 A; A/B=2-562.
PDBsum; 1C47; -.
PDBsum; 1C4G; -.
PDBsum; 1JDY; -.
PDBsum; 1LXT; -.
PDBsum; 1VKL; -.
PDBsum; 3PMG; -.
ProteinModelPortal; P00949; -.
SMR; P00949; -.
PRIDE; P00949; -.
GeneID; 100009155; -.
KEGG; ocu:100009155; -.
CTD; 5236; -.
HOGENOM; HOG000009550; -.
HOVERGEN; HBG001599; -.
InParanoid; P00949; -.
KO; K01835; -.
EvolutionaryTrace; P00949; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0004614; F:phosphoglucomutase activity; IDA:UniProtKB.
GO; GO:0006006; P:glucose metabolic process; IDA:UniProtKB.
InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
InterPro; IPR005843; A-D-PHexomutase_C.
InterPro; IPR036900; A-D-PHexomutase_C_sf.
InterPro; IPR016066; A-D-PHexomutase_CS.
InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
Pfam; PF02878; PGM_PMM_I; 1.
Pfam; PF02879; PGM_PMM_II; 1.
Pfam; PF02880; PGM_PMM_III; 1.
Pfam; PF00408; PGM_PMM_IV; 1.
PRINTS; PR00509; PGMPMM.
SUPFAM; SSF53738; SSF53738; 3.
SUPFAM; SSF55957; SSF55957; 1.
PROSITE; PS00710; PGM_PMM; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Carbohydrate metabolism; Complete proteome; Cytoplasm;
Direct protein sequencing; Glucose metabolism; Isomerase; Magnesium;
Metal-binding; Phosphoprotein; Reference proteome;
Sarcoplasmic reticulum.
CHAIN 1 562 Phosphoglucomutase-1.
/FTId=PRO_0000147779.
REGION 117 118 Substrate binding. {ECO:0000269|Ref.8,
ECO:0000269|Ref.9}.
REGION 292 293 Substrate binding. {ECO:0000269|Ref.8,
ECO:0000269|Ref.9}.
REGION 376 378 Substrate binding. {ECO:0000269|Ref.8,
ECO:0000269|Ref.9}.
ACT_SITE 117 117 Phosphoserine intermediate.
{ECO:0000269|PubMed:5669853}.
METAL 117 117 Magnesium; via phosphate group.
{ECO:0000269|PubMed:15299905}.
METAL 288 288 Magnesium. {ECO:0000269|PubMed:15299905}.
METAL 290 290 Magnesium. {ECO:0000269|PubMed:15299905}.
METAL 292 292 Magnesium. {ECO:0000269|PubMed:15299905}.
BINDING 19 19 Substrate. {ECO:0000269|Ref.9}.
BINDING 23 23 Substrate. {ECO:0000269|Ref.8,
ECO:0000269|Ref.9}.
BINDING 130 130 Substrate. {ECO:0000269|Ref.9}.
BINDING 357 357 Substrate. {ECO:0000269|Ref.8}.
BINDING 389 389 Substrate. {ECO:0000269|Ref.8,
ECO:0000269|Ref.9}.
BINDING 515 515 Substrate. {ECO:0000269|Ref.9}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P36871}.
MOD_RES 16 16 N6-acetyllysine.
{ECO:0000250|UniProtKB:P36871}.
MOD_RES 115 115 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9D0F9}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000250|UniProtKB:P36871}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000250|UniProtKB:P38652}.
MOD_RES 185 185 Phosphothreonine.
{ECO:0000250|UniProtKB:P36871}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000250|UniProtKB:P38652}.
MOD_RES 349 349 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9D0F9}.
MOD_RES 353 353 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9D0F9}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000250|UniProtKB:P38652}.
MOD_RES 378 378 Phosphoserine.
{ECO:0000250|UniProtKB:P36871}.
MOD_RES 419 419 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9D0F9}.
MOD_RES 467 467 Phosphothreonine; by PAK1.
{ECO:0000250|UniProtKB:P36871}.
MOD_RES 485 485 Phosphoserine.
{ECO:0000250|UniProtKB:P38652}.
MOD_RES 505 505 Phosphoserine.
{ECO:0000250|UniProtKB:P36871}.
MOD_RES 507 507 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9D0F9}.
MOD_RES 509 509 Phosphoserine.
{ECO:0000250|UniProtKB:P36871}.
MOD_RES 541 541 Phosphoserine.
{ECO:0000250|UniProtKB:P38652}.
VAR_SEQ 1 13 MVKIVTVKTKAYP -> MEEGPLPLLTIRTAPYH (in
isoform 2). {ECO:0000303|PubMed:1328221}.
/FTId=VSP_004690.
VAR_SEQ 25 36 RVKVFQSSTNYA -> KTYYFEDKPCYL (in isoform
2). {ECO:0000303|PubMed:1328221}.
/FTId=VSP_004691.
VAR_SEQ 44 56 ISTVEPAQRQEAT -> FFSIDLKDRQGSS (in
isoform 2). {ECO:0000303|PubMed:1328221}.
/FTId=VSP_004692.
VAR_SEQ 65 77 FYMKEAIQLIVRI -> YFNKSAIETILQM (in
isoform 2). {ECO:0000303|PubMed:1328221}.
/FTId=VSP_004693.
STRAND 5 8 {ECO:0000244|PDB:3PMG}.
STRAND 21 25 {ECO:0000244|PDB:3PMG}.
HELIX 26 31 {ECO:0000244|PDB:3PMG}.
HELIX 35 45 {ECO:0000244|PDB:3PMG}.
HELIX 49 51 {ECO:0000244|PDB:3PMG}.
TURN 52 54 {ECO:0000244|PDB:3PMG}.
STRAND 56 61 {ECO:0000244|PDB:3PMG}.
HELIX 67 80 {ECO:0000244|PDB:3PMG}.
STRAND 85 93 {ECO:0000244|PDB:3PMG}.
HELIX 96 106 {ECO:0000244|PDB:3PMG}.
STRAND 109 114 {ECO:0000244|PDB:3PMG}.
STRAND 125 133 {ECO:0000244|PDB:3PMG}.
STRAND 136 138 {ECO:0000244|PDB:3PMG}.
HELIX 141 153 {ECO:0000244|PDB:3PMG}.
STRAND 156 159 {ECO:0000244|PDB:3PMG}.
STRAND 167 169 {ECO:0000244|PDB:1JDY}.
STRAND 171 175 {ECO:0000244|PDB:3PMG}.
STRAND 184 189 {ECO:0000244|PDB:3PMG}.
HELIX 193 200 {ECO:0000244|PDB:3PMG}.
HELIX 205 213 {ECO:0000244|PDB:3PMG}.
STRAND 214 216 {ECO:0000244|PDB:1C47}.
STRAND 220 223 {ECO:0000244|PDB:3PMG}.
HELIX 230 237 {ECO:0000244|PDB:3PMG}.
TURN 238 241 {ECO:0000244|PDB:3PMG}.
HELIX 245 247 {ECO:0000244|PDB:3PMG}.
STRAND 248 250 {ECO:0000244|PDB:3PMG}.
HELIX 257 259 {ECO:0000244|PDB:3PMG}.
TURN 266 269 {ECO:0000244|PDB:3PMG}.
HELIX 270 277 {ECO:0000244|PDB:3PMG}.
STRAND 282 287 {ECO:0000244|PDB:3PMG}.
STRAND 289 291 {ECO:0000244|PDB:1C47}.
STRAND 294 298 {ECO:0000244|PDB:3PMG}.
HELIX 299 301 {ECO:0000244|PDB:3PMG}.
HELIX 306 315 {ECO:0000244|PDB:3PMG}.
HELIX 317 319 {ECO:0000244|PDB:3PMG}.
HELIX 321 326 {ECO:0000244|PDB:3PMG}.
STRAND 331 334 {ECO:0000244|PDB:3PMG}.
HELIX 340 346 {ECO:0000244|PDB:3PMG}.
STRAND 348 350 {ECO:0000244|PDB:3PMG}.
STRAND 352 355 {ECO:0000244|PDB:3PMG}.
HELIX 359 367 {ECO:0000244|PDB:3PMG}.
STRAND 372 376 {ECO:0000244|PDB:3PMG}.
TURN 377 379 {ECO:0000244|PDB:3PMG}.
STRAND 380 383 {ECO:0000244|PDB:3PMG}.
STRAND 386 388 {ECO:0000244|PDB:3PMG}.
HELIX 391 405 {ECO:0000244|PDB:3PMG}.
HELIX 409 420 {ECO:0000244|PDB:3PMG}.
STRAND 422 433 {ECO:0000244|PDB:3PMG}.
HELIX 435 450 {ECO:0000244|PDB:3PMG}.
TURN 452 456 {ECO:0000244|PDB:1C47}.
STRAND 458 461 {ECO:0000244|PDB:3PMG}.
STRAND 464 473 {ECO:0000244|PDB:3PMG}.
TURN 479 481 {ECO:0000244|PDB:3PMG}.
STRAND 490 494 {ECO:0000244|PDB:3PMG}.
TURN 495 497 {ECO:0000244|PDB:1LXT}.
STRAND 499 506 {ECO:0000244|PDB:3PMG}.
STRAND 508 510 {ECO:0000244|PDB:3PMG}.
STRAND 512 522 {ECO:0000244|PDB:3PMG}.
TURN 525 529 {ECO:0000244|PDB:3PMG}.
HELIX 532 547 {ECO:0000244|PDB:3PMG}.
HELIX 549 553 {ECO:0000244|PDB:3PMG}.
STRAND 559 562 {ECO:0000244|PDB:3PMG}.
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


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