ID A0A1U7NLU2_9FIRM Unreviewed; 568 AA.
AC A0A1U7NLU2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=BO225_07445 {ECO:0000313|EMBL:OLU45978.1};
OS Dubosiella newyorkensis.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Dubosiella.
OX NCBI_TaxID=1862672 {ECO:0000313|EMBL:OLU45978.1, ECO:0000313|Proteomes:UP000186705};
RN [1] {ECO:0000313|EMBL:OLU45978.1, ECO:0000313|Proteomes:UP000186705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NYU-BL-A4 {ECO:0000313|EMBL:OLU45978.1,
RC ECO:0000313|Proteomes:UP000186705};
RA Cox L.M., Sohn J., Tyrrell K.L., Citron D.M., Lawson P.A., Patel N.B.,
RA Iizumi T., Perez-Perez G.I., Goldstein E.J., Blaser M.J.;
RT "Description of two novel members of the family Erysipelotrichaceae:
RT Ileibacterium lipovorans gen. nov., sp. nov. and Dubosiella newyorkensis,
RT gen. nov., sp. nov.";
RL Submitted (NOV-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 -!- 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:OLU45978.1}.
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DR EMBL; MPKA01000077; OLU45978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7NLU2; -.
DR STRING; 1862672.BO225_07445; -.
DR Proteomes; UP000186705; 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:UP000186705}.
FT DOMAIN 42..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 221..309
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 318..443
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 504..539
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 568 AA; 63371 MW; F724AF7F342CC487 CRC64;
MSIVEERYEK WVNHPNLDPQ YLEELKGMSE EEKNDAFYTL IEFGTAGMRG LLGPGTNRIN
LHTIRKVTQG YANYIKAHGE KACEEGIAIG YDNRHMSREF AFDCAKILAK NGINSYVFES
LRPTPELSFA VRHLHCFGGI MITASHNPRE YNGYKLYDDK GCQLVPALAS QVIDQVNAIE
DELAIDATVT PEEEKRITVI GKDVDEAYYE KVLGIQLNPD VTKDIKIVFS PEHGTANIPV
RTVYERAGYN CIPVEEQCTP DPDFSNTPTP NPEQIGAYEL ALKYAKDNDA DIILVCDPDA
DRMGVGVKHD GDYVIMTGNQ SGAVLLEYIL SQMEAHGIMP ENPVMFNTVV TSDLGEKVAS
AHGTETEKTL TGFKFIGEKV AKYEKTGEKN YVFGYEESYG SLIKPFVRDK DAPQACLMLA
EAASFYKQQG KDLIDVLNDL YEQHGTYEES QVALTLSGEA GANRIKEILA DLRKDAPKEI
GGTPVVRFED YKESVIKENG ETKELTGFTK SDVLKYYLED GSWIAVRPSG TEPKCKFYYC
IKGDNALDAH EKTLNYQKAM AELTGTNE
//