ID A0A0S8L0N8_9PROT Unreviewed; 313 AA.
AC A0A0S8L0N8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KPL27718.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:KPL27718.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:KPL27718.1};
DE Flags: Fragment;
GN ORFNames=AMJ72_07395 {ECO:0000313|EMBL:KPL27718.1};
OS Acidithiobacillales bacterium SM1_46.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales.
OX NCBI_TaxID=1703384 {ECO:0000313|EMBL:KPL27718.1, ECO:0000313|Proteomes:UP000052054};
RN [1] {ECO:0000313|EMBL:KPL27718.1, ECO:0000313|Proteomes:UP000052054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM1_46 {ECO:0000313|EMBL:KPL27718.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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:KPL27718.1}.
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DR EMBL; LJVB01000055; KPL27718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8L0N8; -.
DR Proteomes; UP000052054; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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 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; 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; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:KPL27718.1};
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 10..137
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 155..253
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 258..313
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT NON_TER 313
FT /evidence="ECO:0000313|EMBL:KPL27718.1"
SQ SEQUENCE 313 AA; 33868 MW; FC3070233397DDFA CRC64;
MPQPNGLPPE IFKAYDIRGI VGKTLTRAIV ERIGHAIGSE ARARGQNSVC IGRDGRLSGP
ELVKALARGL TRAGCDVVDI GCVPTPVLYF ATHFLGTHSG ISVTGSHNPP DYNGLKIMLA
GETLSGEAIQ SLRQRLLDNR LVQGDGMVAQ DDVREAYLAR ITSDVKLARK LKVVVDCGNG
VAGELAPELL RRLGCEVTEL YCEIDGRFPN HHPDPAHPEN LEDLIHTVTT GNYDVGLAFD
GDGDRLGVVS PDGQIIWPDR QLILYARDVL SRQPGAEIIY DVKCSRTVDA AIREAGGRPT
MWKTGHSLIK AKL
//
