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Database: UniProt
Entry: R9JPE5_9FIRM
LinkDB: R9JPE5_9FIRM
Original site: R9JPE5_9FIRM 
ID   R9JPE5_9FIRM            Unreviewed;       577 AA.
AC   R9JPE5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=C808_04311 {ECO:0000313|EMBL:EOS36095.1};
OS   Lachnospiraceae bacterium M18-1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1235792 {ECO:0000313|EMBL:EOS36095.1, ECO:0000313|Proteomes:UP000014090};
RN   [1] {ECO:0000313|EMBL:EOS36095.1, ECO:0000313|Proteomes:UP000014090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M18-1 {ECO:0000313|EMBL:EOS36095.1,
RC   ECO:0000313|Proteomes:UP000014090};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium M18-1.";
RL   Submitted (APR-2013) 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:EOS36095.1}.
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DR   EMBL; ASSV01000038; EOS36095.1; -; Genomic_DNA.
DR   AlphaFoldDB; R9JPE5; -.
DR   STRING; 1235792.C808_04311; -.
DR   PATRIC; fig|1235792.3.peg.4668; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_0_0_9; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000014090; 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:UP000014090}.
FT   DOMAIN          43..180
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          207..316
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          325..448
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   577 AA;  63861 MW;  EA9CED3185E11499 CRC64;
     MEYKERYQEW LSNPYFDADT KAELEGIKED DNEIKERFYM DLEFGTAGLR GIIGAGTNRM
     NIYTVRKATQ GLANYIIKNG SADKGVAIAY DSRRMSPEFA DEAALCLAAN GIKAYVFESL
     RPTPELSFAV RKLSCIAGIN ITASHNPPEY NGYKVYWADG AQITPPHDKG IMDEVKAVED
     YTTMKTMPLD AAKEKGLYES IGADIDDAYI AELKKQVKHQ DAIDAAAKDL KIVYTPLHGT
     GNIPARRILK ELGFENVYVV KEQELPDGEF PTVSYPNPEA AEAFELGLKL AKEIDADIVL
     ATDPDADRLG VRVKDKNGEY HTLTGNMSGC LLADYEIGEK KEIDGGLPAD GKFIKTIVTT
     NMADAIAKYY GVDLIECLTG FKFIGQQILG FETSGKGEYL FGFEESYGCL IGTHARDKDA
     IVATMALCEA AAFYKTLDMT LWDAMIAMYD RYGYYKDDIQ SITLKGIEGL AKIQEILETL
     RKNPPAEIAG YKVLKARDYK ADTIRDMESG EVTGTGLPSS NVLYYDLTDD AWVCVRPSGT
     EPKVKFYYGV KGISMEDADA KSEAMGKEVL AMIDRML
//
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