ID   A0A1H6SWX9_9FIRM        Unreviewed;       600 AA.
AC   A0A1H6SWX9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE            EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN   ORFNames=SAMN02910453_1237 {ECO:0000313|EMBL:SEI72448.1};
OS   Lachnospiraceae bacterium A10.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1520821 {ECO:0000313|EMBL:SEI72448.1, ECO:0000313|Proteomes:UP000198998};
RN   [1] {ECO:0000313|EMBL:SEI72448.1, ECO:0000313|Proteomes:UP000198998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A10 {ECO:0000313|EMBL:SEI72448.1,
RC   ECO:0000313|Proteomes:UP000198998};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC         Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC         EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
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}.
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DR   EMBL; FNYN01000003; SEI72448.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6SWX9; -.
DR   Proteomes; UP000198998; 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; cd05799; PGM2; 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; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR   PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 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   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   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004326};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198998}.
FT   DOMAIN          64..208
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          241..341
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          354..480
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          530..584
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   600 AA;  67222 MW;  4E8FC6151B222371 CRC64;
     MEVEQSSVPL SLFRNDLGGK RMGYQEMYEE WLKKVPEGDA LYSELLAMKE DEKEKEESFY
     QNLSFGTAGL RGKVGAGTNR MNVYTVSKAT QGISDYICQV SASDEALSDA KERGVVIAHD
     PRHFSSEFAR LAACIFASHG IRVFTFPELR PTPELAYMIR KLHAVSGINI TASHNPKEYN
     GYKAYWEDGC QVSSEVADGM TACIEKVDLW SGYMEDAEDA FDMYVEDGMI TILDEAYDRA
     YLDKIESLKI HDGEELDLTI PLVYTPLNGC GSVPFREMLH DRGFKSFMIV PEQRDPDPDF
     TTVGYPNPED PKAFALSEKY GREFGAELLM ATDPDADRFA IEIRDSEGNY VPLNGNQTGY
     LLVNYVLEGH KTAGTLPAKG AMVKSIVTST LSTIMAEDYG VEMFETLTGF KNICGKIPYL
     HENGYTYLFG YEESVGYAAC EGIRDKDGIS AGMLVAEAAA YYRKQGKTLW DVLQDIYAKY
     GYFAEDEPNL VLEGIAGAER IKRMMKWFRA NIPTSVAGIK VSEVRDYLDG YTDPTGKSNI
     PPQNAIRLFL ENGSWFAVRP SGTEPKIKFY FYSNQESREE ALAVNARIRE DVLSRIESVE
//