PGM1_PARTE
ID PGM1_PARTE Reviewed; 572 AA.
AC P47244; O02605; Q52S71;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 4.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Phosphoglucomutase-1;
DE Short=PGM 1;
DE EC=5.4.2.2;
DE AltName: Full=Glucose phosphomutase 1;
DE AltName: Full=Parafusin;
DE Short=Pf;
DE AltName: Full=pp63;
GN Name=pp63-1; ORFNames=GSPATT00032405001;
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Stock 51;
RX PubMed=7937900; DOI=10.1073/pnas.91.21.9832;
RA Subramanian S.V., Wyroba E., Andersen A.P., Satir B.H.;
RT "Cloning and sequencing of parafusin, a calcium-dependent exocytosis-
RT related phosphoglycoprotein.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9832-9836(1994).
RN [2]
RP SEQUENCE REVISION TO 57-58.
RA Satir B.H.;
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=Stock 51;
RX PubMed=9173895; DOI=10.1042/bj3230289;
RA Hauser K., Kissmehl R., Linder J., Schultz J.E., Lottspeich F.,
RA Plattner H.;
RT "Identification of isoforms of the exocytosis-sensitive phosphoprotein
RT PP63/parafusin in Paramecium tetraurelia and demonstration of
RT phosphoglucomutase activity.";
RL Biochem. J. 323:289-296(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Stock 51;
RA Satir B.H.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2;
RX PubMed=17086204; DOI=10.1038/nature05230;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
RN [6]
RP CHARACTERIZATION.
RX PubMed=1333606; DOI=10.1073/pnas.89.23.11297;
RA Subramanian S.V., Satir B.H.;
RT "Carbohydrate cycling in signal transduction: parafusin, a
RT phosphoglycoprotein and possible Ca(2+)-dependent transducer molecule in
RT exocytosis in Paramecium.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11297-11301(1992).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=11779235; DOI=10.1006/jmbi.2001.5168;
RA Mueller S., Diederichs K., Breed J., Kissmehl R., Hauser K., Plattner H.,
RA Welte W.;
RT "Crystal structure analysis of the exocytosis-sensitive phosphoprotein,
RT pp63/parafusin (phosphoglucomutase), from Paramecium reveals significant
RT conformational variability.";
RL J. Mol. Biol. 315:141-153(2002).
CC -!- FUNCTION: May be involved in membrane fusion in exocytosis.
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:9173895};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylated via a calcium-dependent protein kinase. Very
CC rapidly (within 80 ms) dephosphorylated during triggered trichocyst
CC exocytosis.
CC -!- PTM: O-glycosylated with a short chain of mannose residues.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; L12471; AAB05649.2; -; mRNA.
DR EMBL; Y09969; CAA71088.1; -; mRNA.
DR EMBL; AY970820; AAX93766.1; -; Genomic_DNA.
DR EMBL; CT868018; CAK62173.1; -; Genomic_DNA.
DR RefSeq; XP_001429571.1; XM_001429534.1.
DR PDB; 1KFI; X-ray; 2.40 A; A/B=1-572.
DR PDB; 1KFQ; X-ray; 2.40 A; A/B=1-572.
DR PDBsum; 1KFI; -.
DR PDBsum; 1KFQ; -.
DR AlphaFoldDB; P47244; -.
DR SMR; P47244; -.
DR STRING; 5888.CAK62173; -.
DR EnsemblProtists; CAK62173; CAK62173; GSPATT00032405001.
DR GeneID; 5015355; -.
DR KEGG; ptm:GSPATT00032405001; -.
DR eggNOG; KOG0625; Eukaryota.
DR HOGENOM; CLU_009330_0_1_1; -.
DR InParanoid; P47244; -.
DR OMA; DIYKIYA; -.
DR EvolutionaryTrace; P47244; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
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; IPR005843; A-D-PHexomutase_C.
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 Pfam; PF00408; PGM_PMM_IV; 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; Cytoplasm; Direct protein sequencing; Glycoprotein;
KW Isomerase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..572
FT /note="Phosphoglucomutase-1"
FT /id="PRO_0000147813"
FT ACT_SITE 126
FT /note="Phosphoserine intermediate"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 126..127
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 312..313
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 373
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 392..394
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 527
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT CONFLICT 1..6
FT /note="MQQVIP -> MVLFLLPLRLGHNLWRIE (in Ref. 1; AAB05649
FT and 3; AAX93766)"
FT /evidence="ECO:0000305"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 38..49
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:1KFI"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 242..250
FT /evidence="ECO:0007829|PDB:1KFI"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:1KFI"
FT TURN 279..282
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 283..288
FT /evidence="ECO:0007829|PDB:1KFI"
FT TURN 289..292
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 356..364
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 378..383
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:1KFI"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 407..421
FT /evidence="ECO:0007829|PDB:1KFI"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:1KFQ"
FT HELIX 431..442
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 444..455
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 457..468
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 471..475
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 482..485
FT /evidence="ECO:0007829|PDB:1KFI"
FT TURN 491..493
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 502..505
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 511..516
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 521..536
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 542..557
FT /evidence="ECO:0007829|PDB:1KFI"
FT HELIX 559..563
FT /evidence="ECO:0007829|PDB:1KFI"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:1KFI"
SQ SEQUENCE 572 AA; 63806 MW; AB0C31BEF01A930A CRC64;
MQQVIPAPRV QVTQPYAGQK PGTSGLRKKV SEATQPNYLE NFVQSIFNTL RKDELKPKNV
LFVGGDGRYF NRQAIFSIIR LAYANDISEV HVGQAGLMST PASSHYIRKV NEEVGNCIGG
IILTASHNPG GKEHGDFGIK FNVRTGAPAP EDFTDQIYTH TTKIKEYLTV DYEFEKHINL
DQIGVYKFEG TRLEKSHFEV KVVDTVQDYT QLMQKLFDFD LLKGLFSNKD FSFRFDGMHG
VAGPYAKHIF GTLLGCSKES LLNCDPSEDF GGGHPDPNLT YAHDLVELLD IHKKKDVGTV
PQFGAACDGD ADRNMILGRQ FFVTPSDSLA VIAANANLIF KNGLLGAARS MPTSGALDKV
AAKNGIKLFE TPTGWKFFGN LMDAGLINLC GEESFGTGSN HIREKDGIWA VLAWLTILAH
KNKNTDHFVT VEEIVTQYWQ QFGRNYYSRY DYEQVDSAGA NKMMEHLKTK FQYFEQLKQG
NKADIYDYVD PVDQSVSKNQ GVRFVFGDGS RIIFRLSGTG SVGATIRIYF EQFEQQQIQH
ETATALANII KLGLEISDIA QFTGRNEPTV IT
