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Database: UniProt
Entry: A0A1R3GRH0_COCAP
LinkDB: A0A1R3GRH0_COCAP
Original site: A0A1R3GRH0_COCAP 
ID   A0A1R3GRH0_COCAP        Unreviewed;       581 AA.
AC   A0A1R3GRH0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=CCACVL1_23974 {ECO:0000313|EMBL:OMO60661.1};
OS   Corchorus capsularis (Jute).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX   NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO60661.1, ECO:0000313|Proteomes:UP000188268};
RN   [1] {ECO:0000313|EMBL:OMO60661.1, ECO:0000313|Proteomes:UP000188268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC   TISSUE=Whole seedling {ECO:0000313|EMBL:OMO60661.1};
RA   Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA   Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA   Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT   "Corchorus capsularis genome sequencing.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OMO60661.1}.
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DR   EMBL; AWWV01013668; OMO60661.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R3GRH0; -.
DR   STRING; 210143.A0A1R3GRH0; -.
DR   EnsemblPlants; OMO60661; OMO60661; CCACVL1_23974.
DR   Gramene; OMO60661; OMO60661; CCACVL1_23974.
DR   OMA; IWVGQNG; -.
DR   OrthoDB; 5476118at2759; -.
DR   Proteomes; UP000188268; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
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:UP000188268}.
FT   DOMAIN          16..163
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          199..307
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          316..417
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   581 AA;  63374 MW;  821383B8F139CED0 CRC64;
     MVFKVSKVQT KPFEGQKPGT SGLRKKVKVF VQPHYLENFV QSTFNALTPA KVRGATLVVS
     GDGRYYSKDA IQIIIKMSAA NGVRRVWVGQ NGLLSTPAVS AVIRERVGAD GSKATGSFIL
     TASHNPGGPH EDFGIKYNME NGGPAPESIT DKIFENTKTI TEYLIAEDLP NVDISSVGVT
     NFGGPEGPFD VEVFDSASDY VKLMKSIFDF ELIRKLLSSP KFTFCYDALH GVAGAYAHRI
     FVEELGAKES SLLNCVPKED FGGGHPDPNL TYAKELVNRM GLGKSSEVEP PEFGAAADGD
     ADRNMILGKR FFVTPSDSVA IIAANAVDAI PYFSSGLKGV ARSMPTSAAL DVVAKNLKLK
     FFEVPTGWKF FGNLMDAGLC SVCGEESFGT GSDHIREKDG IWAVLAWLSI LAYKNKDNLN
     GNKLVTVEDI VRQHWATYGR HYYTRYDYEN VDAGAAKELM AYLVKLQSSL DEINTIVKGA
     RSDVSKVVNA DEFEYKDPVD GSISKHQGIR FLFEDGSRLV FRLSGTGSEG ATIRLYIEQY
     EKDSSKTGRD SQEALAPLVE VALKLSKMQE FTGRSAPTVI T
//
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