ID   A0A0G0BE02_9BACT        Unreviewed;       473 AA.
AC   A0A0G0BE02;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I {ECO:0000313|EMBL:KKP67639.1};
GN   ORFNames=UR66_C0012G0003 {ECO:0000313|EMBL:KKP67639.1};
OS   Candidatus Moranbacteria bacterium GW2011_GWE1_35_17.
OC   Bacteria; Candidatus Moranbacteria.
OX   NCBI_TaxID=1618707 {ECO:0000313|EMBL:KKP67639.1, ECO:0000313|Proteomes:UP000034945};
RN   [1] {ECO:0000313|EMBL:KKP67639.1, ECO:0000313|Proteomes:UP000034945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKP67639.1}.
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DR   EMBL; LBQA01000012; KKP67639.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0BE02; -.
DR   STRING; 1618707.UR66_C0012G0003; -.
DR   PATRIC; fig|1618707.3.peg.1177; -.
DR   Proteomes; UP000034945; Unassembled WGS sequence.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004326};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          7..137
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          155..252
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          258..366
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          372..455
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   473 AA;  53332 MW;  2C44C15976B29359 CRC64;
     MKINPHIFRG YDLRGVVDED LNVEIVEHIG KAFGTYLKRA GIAKALISYD CRVTSKDYSE
     AMARGLNWAG TDVINIGMNL VGTFYWAQYH LDCKGGVFVT ASHNPAQYNG FKFANDFSET
     LVSDGMQELR RMVQEDDVEE GEKAGEIKSV DIRKEYLEDI SNRLPLSEKF KVVIDPSCST
     AGAILPDFLR SVGCEVVEKN CEIDPSFPIG TPDPTESAVA ERLRTEVLEA GADIGFSYDP
     DGDRIGIVSD KGEIIWNDVL VAIFAVDVLH THPGEKIMFN TLCSKVVPET IVKYGGEPFM
     WRTGHSFLKK KNQEIKAAFI GELSGHFFFS ADYYNHDDGF YSTMRLLSYL ARTKKKMSEA
     ISELPKYFSS PEIKVGCADD KKVDLISRVS DVLKKDYPDA EVIDDERAGD GVRLDMEDSM
     FIVRYSQNGP YLTIKFEANS QEKYNHLKVY IRELLHKYEE IDWSFGANVE SLE
//