ID   A0A0G1IIJ1_9BACT        Unreviewed;       473 AA.
AC   A0A0G1IIJ1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:KKT31657.1};
GN   ORFNames=UW18_C0003G0241 {ECO:0000313|EMBL:KKT31657.1};
OS   Microgenomates group bacterium GW2011_GWF1_44_10.
OC   Bacteria.
OX   NCBI_TaxID=1618537 {ECO:0000313|EMBL:KKT31657.1, ECO:0000313|Proteomes:UP000034538};
RN   [1] {ECO:0000313|EMBL:KKT31657.1, ECO:0000313|Proteomes:UP000034538}
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}.
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:KKT31657.1}.
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DR   EMBL; LCHI01000003; KKT31657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1IIJ1; -.
DR   Proteomes; UP000034538; Unassembled WGS sequence.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; 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; IPR036900; A-D-PHexomutase_C_sf.
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   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE   3: Inferred from homology;
FT   DOMAIN          12..143
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          158..255
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          261..367
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   473 AA;  52852 MW;  DC18033481EFC3DC CRC64;
     MYQLVPSISP VIFRGYDIRG LVGSELTEDV YYTLGRAYAT FLRKRRVREA TVGMDNRLSS
     EVFAKAFRQG LNDGGVDSIF LGLSLSQIVY FSSYECKTKG AAMITASHNP KEFNGLKLGT
     GYSETMETAE INEYKEIVRN GKFSEGRGTD RTIDIFESYA HHLLKHFSLT KKWKVVIDAC
     STGSGVFYPQ LFEQAGCEVV RQNCEPDGNF PSGVPDPTES EVLERLAARV LAEKADIGFA
     YDTDGDRMAC VDSTGQVLYM DQIIALFVKD VLSTMPNAPI IFNTLCSQVV RETIVSQGGK
     PIMWVTGHSF IKAKVKEEKA PFGGELSGHI YFTDNFYGHD DGAYASLRLL QYLESKNHSL
     NQEIAVLPKF ISSPEIKLGL ADAIKFEVIK TQIAPVFHQK WPTALFTEID GVRAEENGNM
     VIIRASQNGP YITIKFESKT QQGYDELKKD IRELLHSIPE IDWSKGVNIH AFE
//