ID A0A0G1QMH8_9BACT Unreviewed; 476 AA.
AC A0A0G1QMH8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KKU09855.1};
GN ORFNames=UX13_C0028G0005 {ECO:0000313|EMBL:KKU09855.1};
OS Candidatus Woesebacteria bacterium GW2011_GWB1_45_5.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618581 {ECO:0000313|EMBL:KKU09855.1, ECO:0000313|Proteomes:UP000034329};
RN [1] {ECO:0000313|EMBL:KKU09855.1, ECO:0000313|Proteomes:UP000034329}
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:KKU09855.1}.
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DR EMBL; LCLA01000028; KKU09855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1QMH8; -.
DR Proteomes; UP000034329; 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; 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 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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326}.
FT DOMAIN 12..144
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 163..258
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 264..371
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 476 AA; 53629 MW; 7009F8ACB63AB2A4 CRC64;
MYDVSKAVFK DNIFRGYDIR GIYGEELNDE GAYVIGRAYG TFLSQRRINE AVVTGDNRLS
TDLVKKAVIE GLLDSGINVI DHGLGLVYFM YFSQYLNQSK GGVNVSASHN PKEYNGFKLA
VGFSDTMVTE EILQLKEIAK KGEFVKPAKK GTFQQKEIFE AYKKDLYKRM PEKLDFKIVV
DGGNCTSGKF MPDILRGTGC EIIEQNTELD GNFPLGTPDP TEKDYLTRLA EGVRKNKADL
GFCYDPDGDR IGIVDEDGSM IWNDVLVSIF ATDILDFVPE TKIIFNTLCS KQVTDVIKAK
GGNPVMWLTG HSFIKAKLKE ERGLFGGELS GHFFFMDNFY GHDDCAYASL RLLNYLKRVG
KTLKQVVAEL PRYVSSPEIK LGLADEIKFE FVKNVVGQEL KNLYPDAEYV EIDGVRMDTL
TKMAIVRASQ NGPYITIKYE GKTQVEYDEL KVQLRGMLKS HKEINWSYGV NTDAFE
//
