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Database: UniProt
Entry: R5SKV9_9FIRM
LinkDB: R5SKV9_9FIRM
Original site: R5SKV9_9FIRM 
ID   R5SKV9_9FIRM            Unreviewed;       558 AA.
AC   R5SKV9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
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   ORFNames=BN483_00739 {ECO:0000313|EMBL:CCZ45552.1};
OS   Firmicutes bacterium CAG:129.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263003 {ECO:0000313|EMBL:CCZ45552.1, ECO:0000313|Proteomes:UP000018410};
RN   [1] {ECO:0000313|EMBL:CCZ45552.1, ECO:0000313|Proteomes:UP000018410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:129 {ECO:0000313|Proteomes:UP000018410};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCZ45552.1}.
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DR   EMBL; CBAB010000056; CCZ45552.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5SKV9; -.
DR   Proteomes; UP000018410; 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; 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   Magnesium {ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|RuleBase:RU004326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018410}.
FT   DOMAIN          44..177
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          223..311
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          320..447
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   558 AA;  60685 MW;  41D1302F748CA1BA CRC64;
     MTALNTYRRW LARVEDDALR AELSALDEVR DAAQIEDRFY RDLAFGTGGL RGVLGAGTNR
     MNVYVVRRAT QGLAAYLKAA GLPLRCAIAY DSRIGSARFA RETARVLAAN GVTAYLYPRL
     EPTPALSWAV RYYGCGAGVC VTASHNPAAY NGYKVYGPDG CQITLETADA VSKHIGAADH
     FDGVRLCGFA DALADGTICM IGEDCLEAFL DAVERRSVWD GDRSALRVVY TPLNGTGREC
     VTKILRRIGV TDVTLVPEQA WPDGSFPTCP YPNPEERAAL EHGLALARET RADLLLGTDP
     DCDRMGAAVP DGGDYRLLTG NEMGVLLLDY LCRRRSENGT MPARPVAVTT IVSTDMADAV
     AAHYGVELRR TLTGFKFIGE QIGELERAGE TERYLFGFEE SYGYLSGPHV RDKDAVNAAL
     LCCEMAAWYR AQGMTLAQAM DALYEKFGYY RNELQSVVLP GEDGMERMSA ILTALRAAPP
     HTLAGERVTR VRDYLGGLDS LPASDVLELR TAHVKVIVRP SGTEPKLKLY YSAHARTMAG
     AAALCAAARR DMSARLGE
//
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