ID   A0A0G0AAE8_9BACT        Unreviewed;       464 AA.
AC   A0A0G0AAE8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0000313|EMBL:KKP53523.1};
GN   ORFNames=UR43_C0004G0064 {ECO:0000313|EMBL:KKP53523.1};
OS   candidate division TM6 bacterium GW2011_GWF2_33_332.
OC   Bacteria; Candidatus Dependentiae.
OX   NCBI_TaxID=1619080 {ECO:0000313|EMBL:KKP53523.1, ECO:0000313|Proteomes:UP000034634};
RN   [1] {ECO:0000313|EMBL:KKP53523.1, ECO:0000313|Proteomes:UP000034634}
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:KKP53523.1}.
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DR   EMBL; LBPE01000004; KKP53523.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0AAE8; -.
DR   Proteomes; UP000034634; 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          4..136
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          158..258
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          262..371
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          381..453
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   464 AA;  52572 MW;  4C043AD916180FD6 CRC64;
     MLPNIFREYD IRGVIGKSFL IDEAENLAQS IVTYFLSKNP NINTVTVAMD GRIHSQAIKE
     KVINSITQMG INVIDIGLCP TPTFYFSLFM HPESTSGLMI TASHNPKEYN GMKICFEKQS
     VFGKEIQEIK KISESQNFFE NKTGKVGTVA KYDATNLYIK WLTDNFAHLK NLPISALIDC
     GNGTAGAILP QLISAMGWKN VKTIYEEIDG NFPNHEADPT TYENMHEIIL KLKNNSTFEL
     GIGFDGDCDR MSPITKNGKI VEGDKLLALF SKQILKDVPN ATIVFDIKSS CGLMELLEEW
     GAKQILAPSG HSLIKNTMIQ NNAMLAGELS CHFFFKHRYF GYDDGIYAMM RTFEILLEEN
     KSLEELLQIF PQKFSSPEYR LTCKEEEKQE IVEKVKSYFS QKVDAKLITI DGIRAQLPFG
     WGLVRASNTQ PAMTLRFEAN SYENLEAIKY EFKIALNPYF QTDF
//