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Database: UniProt
Entry: A0A1U7NLU2_9FIRM
LinkDB: A0A1U7NLU2_9FIRM
Original site: A0A1U7NLU2_9FIRM 
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
//
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