ID A0A0R1WKK6_9LACO Unreviewed; 574 AA.
AC A0A0R1WKK6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 28-JAN-2026, entry version 32.
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=FC40_GL001023 {ECO:0000313|EMBL:KRM18343.1};
OS Ligilactobacillus hayakitensis DSM 18933 = JCM 14209.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1423755 {ECO:0000313|EMBL:KRM18343.1, ECO:0000313|Proteomes:UP000051054};
RN [1] {ECO:0000313|EMBL:KRM18343.1, ECO:0000313|Proteomes:UP000051054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18933 {ECO:0000313|EMBL:KRM18343.1,
RC ECO:0000313|Proteomes:UP000051054};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Genome Announc. 6:8322-8322(2015).
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:KRM18343.1}.
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DR EMBL; AZGD01000095; KRM18343.1; -; Genomic_DNA.
DR RefSeq; WP_025022111.1; NZ_AZGD01000095.1.
DR AlphaFoldDB; A0A0R1WKK6; -.
DR STRING; 1423755.FC40_GL001023; -.
DR PATRIC; fig|1423755.3.peg.1080; -.
DR eggNOG; COG1109; Bacteria.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000051054; 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:0008973; F:phosphopentomutase activity; IEA:TreeGrafter.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:TreeGrafter.
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 2B-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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022526};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
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:UP000051054}.
FT DOMAIN 43..181
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..314
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 327..451
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 509..560
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 574 AA; 64055 MW; 10CBEF3947A54747 CRC64;
MSWEKTYQLW DKNTELPTDL RQSLDELKEN KETLEDAFYA PLEFGTAGMR GVLGAGINRM
NIYTVRQATE GLAMLMDGLS EDVKKRGVAI SYDSRHHSQD FAFEAARVLG QHNIPTYVFE
SLRPTPELSF AVRHLHTYAG IMITASHNPK QYNGYKIYGE DGAQMPPKES DLITEYIRKV
DDLFAIKVAN KDSLINEGLL KIVGSEIDKP YLDEIKSVTI NQELVAEEGK AMKLIFTPLH
GTGAMLGEKA LRQAGFENFT MVPEQATPDA DFSTVKLPNP EDPAAFDLAI KLGKQQGADL
LIAVDPDADR LGAAVRQPSG EYQLLTGNQI AAIMLNYILT ARKEAGSLPA NAAAVKSIVS
SEFATKVAES YNVKMINVLT GFKFIAEQIK NFEDTNSNTF MFGFEESYGY LVRSFVRDKD
SIQALVLLAE VAAYYNKQGK NLYDGLQELF EKHGYFAEKT TSLTFDGVEG VQQIKDLMTK
FRNESPVDFA GYKVVAMEDF DKSEKRYTNG TVEKIDMPKS NVLKYLLEDG TWIAVRPSGT
EPKIKFYIGT HGKDQDQANE KRASFDSAIQ SFVK
//
