ID A0A061E9J5_THECC Unreviewed; 583 AA.
AC A0A061E9J5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN ORFNames=TCM_010981 {ECO:0000313|EMBL:EOY01047.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY01047.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY01047.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
CC -!- FUNCTION: This enzyme participates in both the breakdown and synthesis
CC of glucose. {ECO:0000256|ARBA:ARBA00003488}.
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:0000256|ARBA:ARBA00000443};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; CM001880; EOY01047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061E9J5; -.
DR STRING; 3641.A0A061E9J5; -.
DR EnsemblPlants; EOY01047; EOY01047; TCM_010981.
DR Gramene; EOY01047; EOY01047; TCM_010981.
DR eggNOG; KOG0625; Eukaryota.
DR InParanoid; A0A061E9J5; -.
DR OMA; IWVGQNG; -.
DR Proteomes; UP000026915; Chromosome 2.
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 GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR CDD; cd03085; PGM1; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
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:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 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; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915}.
FT DOMAIN 16..163
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 199..308
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 317..418
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 583 AA; 63419 MW; 3DEA05A57DC230EB CRC64;
MVFKVSKVPT TPYDGQKPGT SGLRKKVKVF VQPHYLQNFV QSTFNALTPE KVRGATLVVS
GDGRYFSKDA IQIIIKMAAA NGVRRIWVGQ NGLLSTPAVS AVIRERIGVD GSKATGAFIL
TASHNPGGPH EDFGIKYNME NGGPAPEAIT DKIFENTKTI TEYLIAEDLP NVDISAIGVT
SFGGPEAQFD VEVFDSASDY VKLMKSIFDF ELIRQLLSSP KFTFCYDALH GVAGAYAHRI
FVEELGAKES SLLNCVPKED FGGGHPDPNL TYAKELVARM GLGKSNSGVE PPEFGAAADG
DADRNMILGK RFFVTPSDSV AIIAANAVDA IPYFSSGLKG VARSMPTSAA LDVVAKNLEL
KFFEVVPTGW KFFGNLMDAG LCSVCGEESF GTGSDHIREK DGIWAVLAWL SILAYKNKEN
LDGDKLVTVE DIVRQHWATY GRHYYTRYDY ENVDAGAAKD LMAYLVKLQS SLGDVNTIVN
EAHSDVSNVV NADEFEYKDP VDGSVSKHQG IRFLFEDGSR LVFRLSGTGS EGATIRLYIE
QYEKDPSKTG RDSQEALAPL VEVALKLSKM QEFTGRSAPT VIT
//
