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Database: UniProt
Entry: A0A0G0Q232_9BACT
LinkDB: A0A0G0Q232_9BACT
Original site: A0A0G0Q232_9BACT 
ID   A0A0G0Q232_9BACT        Unreviewed;       449 AA.
AC   A0A0G0Q232;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:KKR31426.1};
GN   ORFNames=UT64_C0061G0008 {ECO:0000313|EMBL:KKR31426.1};
OS   Candidatus Falkowbacteria bacterium GW2011_GWF2_39_8.
OC   Bacteria; Candidatus Falkowbacteria.
OX   NCBI_TaxID=1618642 {ECO:0000313|EMBL:KKR31426.1, ECO:0000313|Proteomes:UP000034137};
RN   [1] {ECO:0000313|EMBL:KKR31426.1, ECO:0000313|Proteomes:UP000034137}
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:KKR31426.1}.
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DR   EMBL; LBXO01000061; KKR31426.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0Q232; -.
DR   PATRIC; fig|1618642.3.peg.947; -.
DR   Proteomes; UP000034137; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   InterPro; IPR006352; GlmM_bact.
DR   NCBIfam; TIGR01455; glmM; 1.
DR   PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR   PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          3..137
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          160..256
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          260..367
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          376..444
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   449 AA;  49081 MW;  9366C1913A61F569 CRC64;
     MKKLFGTDGI RGIVNEANMN VELALRFGQS LVVYCQKNNI APIIFISRDT RGSGPMLEMA
     VSAGIMSLGG KAVSSGIIPT PGLAFMVKQM GVGMGLMVSA SHNDYSYNGF KLFKNDGTKM
     NEQEEEELEN IILNDEFDFS TGKEFVNSDL EIVDVQPIKE YAEFLIKALP EKVGENFKIV
     LDCANGATAE VAPIVFEQIG ADIVTIADCP DGKNINDDCG SQYTANLSRK VVEEGAHLGL
     AFDGDGDRMI AVAEDGSVLT GDQLLYIYAQ LLLELEHFTN KIVVSTVMSN INFINNLKKL
     GIEHVVTEVG DRAVFQAMQE REAVIGGEES GHIIFSKHQT TGDGILSGLM LVWAMKIFGK
     SLSEMSNQFS LAPKVLVNVP VKEKTSLDLI PEIVEEIRQA EEVLQETGRI LVRYSGTENL
     CRIMVEGENE TQINKIAEAI ALIVNEKLN
//
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