ID A0A078KI03_9FIRM Unreviewed; 573 AA.
AC A0A078KI03;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Phosphoglucomutase {ECO:0000256|ARBA:ARBA00039995};
DE AltName: Full=Alpha-phosphoglucomutase {ECO:0000256|ARBA:ARBA00041467};
DE AltName: Full=Glucose phosphomutase {ECO:0000256|ARBA:ARBA00041398};
GN Name=pgcA {ECO:0000313|EMBL:CDZ23171.1};
GN ORFNames=CCDG5_0020 {ECO:0000313|EMBL:CDZ23171.1};
OS [Clostridium] cellulosi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=29343 {ECO:0000313|EMBL:CDZ23171.1, ECO:0000313|Proteomes:UP000032431};
RN [1] {ECO:0000313|Proteomes:UP000032431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5 {ECO:0000313|Proteomes:UP000032431};
RA Wibberg D.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005164}.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; LM995447; CDZ23171.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078KI03; -.
DR STRING; 29343.CCDG5_0020; -.
DR KEGG; ccel:CCDG5_0020; -.
DR PATRIC; fig|29343.3.peg.22; -.
DR HOGENOM; CLU_016950_0_0_9; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000032431; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
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 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 Isomerase {ECO:0000313|EMBL:CDZ23171.1};
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000032431}.
FT DOMAIN 42..177
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 207..312
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 325..449
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 573 AA; 64269 MW; 6DBCCD300B0F0B91 CRC64;
MDYKERYHDW CTNPVFDEKT REELKNLKDE KEIQDRFYKD LTFGTGGLRG IIGAGTNRMN
IYTVAKATQG LANYIIANGG QSKGVAIAYD SRNFSREFAE KTALTLNANG IKTYLFESLR
PTPELSFALR ELHCIAGVVI TASHNPPEYN GYKVYWEDGA QITPPRDQEI IDEVNAVTSF
GAIKTIDKAE AISKGLFNII GEEIDRRYYD ALKKLVLSPE AIKKAAKELK IVYTPLHGTG
NIPVRTILKE LGFENVYVVP EQELPDGNFS TLSYPNPEDP KAFTLALKLA KEKDADLVLA
TDPDADRLGV YAKDTKTGEY KSFTGNMSGL LIAEYELSVR KKLGKLPKNG ALIKTIVSSN
MANEIAKEYG IKLIEVLTGF KYIGEQIKLF EQNHNYEYLF GFEESYGCLV GTHARDKDAV
VAVMALCEAA AYYREQGLTL WDQMLRIYEK YGYYKEDLTS ITLKGLDGAE KIQSILKNMR
NNPPQRFGSF KVTAVRDYLT GEITEVESGA KKPTGLPKSN VLYYELENNA WCCVRPSGTE
PKVKFYMGVK GSSLENAQKL LEELKNSMMA LVK
//
