ID A0A151ARG0_9CLOT Unreviewed; 578 AA.
AC A0A151ARG0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
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:KYH30163.1};
GN ORFNames=CLCOL_01010 {ECO:0000313|EMBL:KYH30163.1};
OS Clostridium colicanis DSM 13634.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121305 {ECO:0000313|EMBL:KYH30163.1, ECO:0000313|Proteomes:UP000075374};
RN [1] {ECO:0000313|EMBL:KYH30163.1, ECO:0000313|Proteomes:UP000075374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13634 {ECO:0000313|EMBL:KYH30163.1,
RC ECO:0000313|Proteomes:UP000075374};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium colicanis DSM 13634.";
RL Submitted (FEB-2016) 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}.
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:KYH30163.1}.
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DR EMBL; LTBB01000001; KYH30163.1; -; Genomic_DNA.
DR RefSeq; WP_061857055.1; NZ_LTBB01000001.1.
DR AlphaFoldDB; A0A151ARG0; -.
DR STRING; 1121305.CLCOL_01010; -.
DR PATRIC; fig|1121305.3.peg.103; -.
DR Proteomes; UP000075374; 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: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:KYH30163.1};
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000075374}.
FT DOMAIN 42..179
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 208..318
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 325..448
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 578 AA; 65596 MW; 39F864C7B6C4E5A1 CRC64;
MDYLEKYNTW LNSKIIDEKT KEELRNISEE KELEDRFYKD LEFGTGGLRG IIGAGSNRMN
VYTVGKATQG LAEYLLNKYY DEDISVSIAY DSRNMSKEFA EFAALTLCAN GIKVNLFESL
RPTPILSYTV RYLKSKAGIV ITASHNPKEY NGYKVYGEDG GQVTDDTAKE ILSFINNIDD
FSKIKFIDMD EAKKSGLLRI IGEEVDNAYI DKVKNLSIRK DLVKEKAKEL KIIYTPLHGT
GNIPVRRVLK ELGYENVHVV KEQEMPDGNF PTAEYPNPEE SKVFNLALKM AEEIEPDIIF
GTDPDCDRIG AVVKDNRGEY KVLTGNMMGA LLTEYILSSL KEKGSLPKNG VVIKTIVTTD
MTAEIAKSFN VEVIDVLTGF KYIGEKIKEF EKTGEKSYIF GFEESYGYLA GTFVRDKDAV
IASMLICEMA LYYKQKGMSL YDGLMNLYDK YGFFKEELVS IKLEGKDGQE KIWKILEHLR
HSMKSDLNGT KIVRKLDYKK RIEKNLITLA EYVIDLPESN VLKFILEDDS SFVVRPSGTE
PKMKIYLSVK GNSITDAKIK MNTLKESVME IINNSCNQ
//
