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Database: UniProt
Entry: A0A058ZXZ1_EUCGR
LinkDB: A0A058ZXZ1_EUCGR
Original site: A0A058ZXZ1_EUCGR 
ID   A0A058ZXZ1_EUCGR        Unreviewed;       673 AA.
AC   A0A058ZXZ1;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=EUGRSUZ_K00185 {ECO:0000313|EMBL:KCW46324.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW46324.1};
RN   [1] {ECO:0000313|EMBL:KCW46324.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW46324.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231}.
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DR   EMBL; KK198763; KCW46324.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A058ZXZ1; -.
DR   STRING; 71139.A0A058ZXZ1; -.
DR   EnsemblPlants; KCW46324; KCW46324; EUGRSUZ_K00185.
DR   Gramene; KCW46324; KCW46324; EUGRSUZ_K00185.
DR   InParanoid; A0A058ZXZ1; -.
DR   OMA; YIPDYAG; -.
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:SF59; PHOSPHOGLUCOMUTASE, CHLOROPLASTIC; 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}.
FT   DOMAIN          101..240
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          273..376
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          385..506
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   673 AA;  73238 MW;  E6CB2198FD674EBB CRC64;
     MAFSLKPHHS RRLLRSSRAK IAQPSSSNVG NVVAFPRPVS SSLSVLSSSA AQPAAAAAAK
     STPLRAPRSP LVVRASSSAA AIAEPEGIKI NSVPTKPIEG QKTGTSGLRK KVKVFMQENY
     LANWIQALFN SLPPEDYRNG VLVLGGDGRY FNREAAQIII KIAAGNGVGK ILVGRDGIMS
     TPAVSAVIRK REANGGFIMS ASHNPGGPEY DWGIKFNYNS GQPAPESITD KIYGNTLSIS
     EIKMADIVDV DLSRLGTTKF GNFSVEVVNP VSDYLELMEN VFDFQLIKTL VSRPGFRFIF
     DAMHAVTGAY AKPIFVDKLG ASPDSISNGV PSEDFGHGHP DPNLTYAKDL VDIMYGENAP
     DFGAASDGDG DRNMILGKGF FITPSDSVAI IAANAQQSIP YFRNGAKGLA RSMPTSGALD
     RVAQKLNLPF FEVPTGWKFF GNLMDAGKLS ICGEESFGTG SDHIREKDGI WAVLAWLSIL
     AYRNKDKKPG EQLVSVSDIA KEHWATYGRN FFSRYDYEEC ESEGANKMVE YLRDLVSKSK
     EGEKYGDYIL QFADDFTYTD PVDGSVVSKQ GVRFVFTDGS RIIYRLSGTG SAGATIRIYI
     EQFESDASRH DVDAQIALKP LIGRLAIPLP MVFYYARDFL TLSCFISSFL LDLALSISKL
     KEFTGREKPT VIT
//
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