PGM2_DICDI
ID PGM2_DICDI Reviewed; 603 AA.
AC Q54UQ2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable phosphoglucomutase-2;
DE Short=PGM 2;
DE EC=5.4.2.2;
DE AltName: Full=Glucose phosphomutase 2;
GN Name=pgmB; ORFNames=DDB_G0280897;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: This enzyme participates in both the breakdown and synthesis
CC of glucose. {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; AAFI02000039; EAL66990.1; -; Genomic_DNA.
DR RefSeq; XP_640969.1; XM_635877.1.
DR AlphaFoldDB; Q54UQ2; -.
DR SMR; Q54UQ2; -.
DR STRING; 44689.DDB0238765; -.
DR PaxDb; Q54UQ2; -.
DR EnsemblProtists; EAL66990; EAL66990; DDB_G0280897.
DR GeneID; 8622773; -.
DR KEGG; ddi:DDB_G0280897; -.
DR dictyBase; DDB_G0280897; pgmB.
DR eggNOG; KOG1220; Eukaryota.
DR HOGENOM; CLU_016950_0_1_1; -.
DR InParanoid; Q54UQ2; -.
DR OMA; YKAYWEE; -.
DR PhylomeDB; Q54UQ2; -.
DR Reactome; R-DDI-3322077; Glycogen synthesis.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-70171; Glycolysis.
DR Reactome; R-DDI-70221; Glycogen breakdown (glycogenolysis).
DR Reactome; R-DDI-70370; Galactose catabolism.
DR Reactome; R-DDI-71336; Pentose phosphate pathway.
DR PRO; PR:Q54UQ2; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0008973; F:phosphopentomutase activity; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006166; P:purine ribonucleoside salvage; 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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Isomerase;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..603
FT /note="Probable phosphoglucomutase-2"
FT /id="PRO_0000328516"
FT ACT_SITE 149
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 149..150
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 314..315
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 416..418
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 430
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
SQ SEQUENCE 603 AA; 67535 MW; D2E413FEC3995117 CRC64;
MTDKINNLIN QWLKWDKNEI TRKEIEQLKE NNNEKELLVR LEERIQFGTA GLRGAMRAGF
SCMNDLTVTQ ASQGLCEYVI ETIEQSKSKG IVIGYDGRHN SYIFAKITAA TFKSKGFKVY
LFSHIVPTPY VSFAVPNLKA AIGVMITASH NPKNDNGYKV YWETGCQINT PHDKGISKKI
DENLEPWSNV DATSDIKYGN GDDGESMIDP LSVITELYNK NIKEYSVGSK IELANEPIVY
TAMHGVGGVY AKKAFETFQL KPFIPVAQQI EPDAEFPTVT YPNPEEGKGA LKLSIETAEA
NNSRLILAND PDADRLAVAE KLADGSWKVF NGNEIGVLLA DWAWTNRSTL TKGGSTLENN
KYFMINTAVS SAMLKTMSEK EGFIHQECLT GFKWIGNAAY NAINNNDGTT FLFGYEEAIG
FQYGDVSFDK DGVRAAAIFA EFALSLYKKG SSVQDHLESM YKRYGYHISK NRYFFCYEPS
KMVSIFNKIR NDGKYLTKLG DDDDEQFTIT RIRDLTTGYD NGYPDCKARL PVSSSTQMIT
FYFKNGGIAT LRGSGTEPKL KYYVEMIGEV KSNVESTLTK AVELVINQLL KPIENQLEPP
KDD
