ID A0A0G1D408_9BACT Unreviewed; 474 AA.
AC A0A0G1D408;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I {ECO:0000313|EMBL:KKS56748.1};
GN ORFNames=UV20_C0006G0031 {ECO:0000313|EMBL:KKS56748.1};
OS Candidatus Magasanikbacteria bacterium GW2011_GWA2_42_32.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1619039 {ECO:0000313|EMBL:KKS56748.1, ECO:0000313|Proteomes:UP000034837};
RN [1] {ECO:0000313|EMBL:KKS56748.1, ECO:0000313|Proteomes:UP000034837}
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:KKS56748.1}.
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DR EMBL; LCDO01000006; KKS56748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1D408; -.
DR Proteomes; UP000034837; 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 7..137
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 155..251
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 257..363
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 474 AA; 53049 MW; 4D75BEE12760D084 CRC64;
MQVNPYMFRG YDLRGLVDKD LNLEIVEHLG KAHGTVLRRK GIVKAVVGYD CRKTSPEYSQ
AIARGLNATG VDVINIGMTM VGTFYWSQYF LNCQGGIFVT ASHNPAEYNG FKFAIDFSET
LVSEGIQELR KIVENEDYFV SERQGTEEKR DIRADYFSAL LQKFKIKKFK VVVDPSNATP
AALVPDLLRE AGCEVIEKNC NIDPAFPLGT PDPTEKIVAS RLAQEVLESG ADIGFSYDAD
GDRIGITDEK GRIIWNDVLV ALFAADVLDH HAGATIMYNT LCSKMVEETI MAKGGRPFMW
RTGHSFLKKK NQEVGAAFIG ELSGHFFFSA DFYNHDDGCY STLRLLDYLS RSGKKLSEAL
DELPLFISSP EIKIVCPDDK KVALMAKIAP ILKQDFPEAE VIDDERAGDG VRLDLADGMF
IIRYSQNGPY LTIKFEGKNQ ERYDGLKKYL AGLLHRFEEI DWSAKSNTNV EALE
//
