ID R9J8X8_9FIRM Unreviewed; 573 AA.
AC R9J8X8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=C807_02124 {ECO:0000313|EMBL:EOS30583.1};
OS Lachnospiraceae bacterium 28-4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=397287 {ECO:0000313|EMBL:EOS30583.1, ECO:0000313|Proteomes:UP000014112};
RN [1] {ECO:0000313|EMBL:EOS30583.1, ECO:0000313|Proteomes:UP000014112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-4 {ECO:0000313|EMBL:EOS30583.1,
RC ECO:0000313|Proteomes:UP000014112};
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 28-4.";
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:EOS30583.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ASSU01000016; EOS30583.1; -; Genomic_DNA.
DR AlphaFoldDB; R9J8X8; -.
DR STRING; 397287.C807_02124; -.
DR PATRIC; fig|397287.3.peg.2314; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_0_0_9; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000014112; 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:UP000014112}.
FT DOMAIN 43..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 207..312
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 326..452
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 573 AA; 64671 MW; 39934B406B574BE2 CRC64;
MSYQEEFNFW LNDAYFDEDT KNELLAIRND EKEIEDRFYK ELEFGTGGLR GVIGAGTNRM
NIYTVRKATQ GLANYILKQG GKEKGVAIAY DSRRKSPEFA DEAALCLAAN GIKAYVFDAL
RPTPELSFAL RKLGCISGIV ITASHNPPEY NGYKAYWEDG AQVTAPKDKE IITEVKNVTD
YHEVKTMDKE EAIKAGLYQV IGAEIDDAYM EELKKQIIHP EIIKEMADDI KIVYSPFHGT
GNVPVRRILS ELGFKHVYVV PEQELPDPDF TTLDYPNPED PKAFTLALKL AKEKNADIVL
ATDPDADRLG IYALDTKSGE YVSFTGNMSG MLIAEYILRE RTAVGAMPEN PALVTTIVTT
NMAKAISDDY HVKCIEVLTG FKYIGEQIKW FEQSGSNHYV FGLEESYGCL AGTHARDKDA
VVAVMCLCEM AAWCKKHGKT VWDQMLDLYE KYGYFKETQY AITLKGIEGS RQIAAIMDKL
RNDPPKEFGD WKVLEFRDYD RNRILNMESG EERETGLPQS NVLYFDLTDD SWCCARPSGT
EPKLKFYMGV KGNSLEDAQE KVEKLTEALK AHI
//
