ID W9EHC7_9LACO Unreviewed; 580 AA.
AC W9EHC7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Phosphoglucomutase {ECO:0000256|ARBA:ARBA00039995};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
DE AltName: Full=Alpha-phosphoglucomutase {ECO:0000256|ARBA:ARBA00041467};
DE AltName: Full=Glucose phosphomutase {ECO:0000256|ARBA:ARBA00041398};
GN ORFNames=B808_409 {ECO:0000313|EMBL:ETO40671.1};
OS Fructilactobacillus florum 8D.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Fructilactobacillus.
OX NCBI_TaxID=1221538 {ECO:0000313|EMBL:ETO40671.1, ECO:0000313|Proteomes:UP000019474};
RN [1] {ECO:0000313|EMBL:ETO40671.1, ECO:0000313|Proteomes:UP000019474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8D {ECO:0000313|EMBL:ETO40671.1,
RC ECO:0000313|Proteomes:UP000019474};
RA Kim E.B., Marco M.L.;
RT "Genome sequencing of Lactobacillus florum 8D.";
RL Submitted (AUG-2012) 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 -!- 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:ETO40671.1}.
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DR EMBL; ALXG01000016; ETO40671.1; -; Genomic_DNA.
DR RefSeq; WP_035421611.1; NZ_ALXG01000016.1.
DR AlphaFoldDB; W9EHC7; -.
DR PATRIC; fig|1221538.3.peg.414; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000019474; 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 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 Pfam; PF00408; PGM_PMM_IV; 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: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:UP000019474}.
FT DOMAIN 47..177
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 215..318
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 330..457
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 517..563
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 580 AA; 64722 MW; 3EEC78CC13E4212E CRC64;
MINQAELDSR YSTWLTAPHL PVDLHRELVQ MKDNQQLLAD AFGTSLSFGT AGMRGILGAG
TNRMNIYTVR QATEGLAKMM ETLPAAERER GVAISFDSRY HSCDFAHEAA GVLGAHGIKS
FIFDDLRPTP ELSFAVRHLH TYAGIMITAS HNPKQYNGYK IYGPDGGQMP PQESDLMTSY
VRQVADLFAI KTVSEPELRH KGLVQVIGED VDVAYLDKIK TVNINHDLIR DVGKQLKFVY
TPLHGTGKII TRRALNQAGF QNYDTVVAQT IADPEFPTTP FPNPEFAQTF DLAIQLGKQE
AADVLIATDP DADRLGAAVR QPNGEYQLMT GNQIASVLLD YLLKAKQRLH DLPENGVVVK
SIVSTELATA IADHYGVKMK NVLTGFKFIA EQIKNFETNH DHTFLFGFEE SFGYLIKPFV
RDKDAVQSTM LLAEVAAFYK QQQLTLYDGL NQLYQEYGYY REKTIAKDFP GLDGQATMSK
LMSEFRATPI QNLNGQPVTA LDDFKTGIRR TADGQKTKLD LPTSDVLKYW FADDTWLAIR
PSGTEPKIKF YLGVKAPTEA EATERLTQYE AALQQQLPQA
//
