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Database: UniProt
Entry: A0A3Q0FC14_VIGRR
LinkDB: A0A3Q0FC14_VIGRR
Original site: A0A3Q0FC14_VIGRR 
ID   A0A3Q0FC14_VIGRR        Unreviewed;       535 AA.
AC   A0A3Q0FC14;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
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   Name=LOC106771950 {ECO:0000313|RefSeq:XP_022641166.1};
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_022641166.1};
RN   [1] {ECO:0000313|RefSeq:XP_022641166.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_022641166.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_022641166.1; XM_022785445.1.
DR   AlphaFoldDB; A0A3Q0FC14; -.
DR   Proteomes; UP000087766; Chromosome 8.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd03089; PMM_PGM; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR   PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087766}.
FT   DOMAIN          15..158
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          191..292
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          298..399
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   535 AA;  57705 MW;  787AB57B3715C0C7 CRC64;
     MPYLDKTDFL KLQNGSDIRG VAIDGVEGEK VNLTEPVAEA IGAAFAAWLM EKKKADSSQH
     LRVSIGHDTR ISAKLLQNAI SRGLAGAGLE FVHYGLASTP AMFNCTLTKD EAFLCPADGS
     IMITASHLPF NRNGFKFFTN AGGLGKADIK DILERAADIY NQFTPESLKN SEKKALLNFK
     KVDYMIAYTS DLVKAVRKAA GNIEKPLEGF HIVVDAGNGA GGFFAEKVLK PLGAITSGSQ
     FLEPDGLFPN HIPNPEDKTA MKAITQAVLD NKADLGIIFD TDVDRSAAVD FTGREFNRNR
     LIALMAAIVL EEHPGTTIVT DSVTSDGLTT FIEKKLGGKH HRFKRGYKNV IDEAIRLNSI
     GEESHLAIET SGHGALKENH WLDDGAYLMV KILNKLASAR ASGNGGGSKV LTDLIEGLEE
     PAFATELRLK INQFHPDLKE GSFREYGEAV LKQLENSIGS DPSLHKAPVN YEGVRVSGHG
     GWFLLRLSLH DPVLPLNIEA PSNDDAVKLG LAVLEAVKGF GGLDTSALKK FVGAS
//
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