ID A0A0G0JC49_9BACT Unreviewed; 471 AA.
AC A0A0G0JC49;
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=Phosphoglucomutase {ECO:0000313|EMBL:KKQ25731.1};
GN ORFNames=US40_C0006G0048 {ECO:0000313|EMBL:KKQ25731.1};
OS Candidatus Roizmanbacteria bacterium GW2011_GWC2_37_13.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1618486 {ECO:0000313|EMBL:KKQ25731.1, ECO:0000313|Proteomes:UP000034917};
RN [1] {ECO:0000313|EMBL:KKQ25731.1, ECO:0000313|Proteomes:UP000034917}
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:KKQ25731.1}.
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DR EMBL; LBSV01000006; KKQ25731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0JC49; -.
DR Proteomes; UP000034917; 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 8..124
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 158..253
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 259..366
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 471 AA; 52847 MW; F906DBDA6CCAF343 CRC64;
MAQIPDHVFR GYDLRGVVGT ELDEERVELL GKAYATWLLE RRIYDCVIGY DSRESSPKFC
EVMVKALTES GITVYNIGIT LSQIAYFAQY YFRTRGMVMI TASHNPKEYN GFKFATGFSA
TMETDEVIAF RELVRSGKFI KLDKKGSHIK KDIFQIYKED LLKKIGAIKK FKVVVDSCAA
TTGLFLPEIL RAVGCEVIEQ NTKPDPSFPV GVADPTEKEV QERLAKRVVS EKADLGFSYD
TDGDRIGIVD NEGSLIWNDV LVSIFSKDIL DFLPGAKIIY NALCSKQVTE VIDQAGGKGI
LWKVGHSFIK AKAREEGAAF GGELSGHFFF LDNFYGHDDG AIASLRLLAY LTRVNKSLKQ
VISDLPHYFS SPEIKVGCAD AIKFQFVSDK IGDELKKLYP QAKFNTIDGV RADTENEMII
FRASQNGPYL TVKFEAKTQE KYDFLKKKIA EILHKFSEVD FKSGVNVDSL K
//