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Database: UniProt
Entry: C4GDQ1_9FIRM
LinkDB: C4GDQ1_9FIRM
Original site: C4GDQ1_9FIRM 
ID   C4GDQ1_9FIRM            Unreviewed;       560 AA.
AC   C4GDQ1;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 59.
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=GCWU000342_02225 {ECO:0000313|EMBL:EEP27530.1};
OS   Shuttleworthia satelles DSM 14600.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Shuttleworthia.
OX   NCBI_TaxID=626523 {ECO:0000313|EMBL:EEP27530.1, ECO:0000313|Proteomes:UP000003494};
RN   [1] {ECO:0000313|EMBL:EEP27530.1, ECO:0000313|Proteomes:UP000003494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14600 {ECO:0000313|EMBL:EEP27530.1,
RC   ECO:0000313|Proteomes:UP000003494};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2009) 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:EEP27530.1}.
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DR   EMBL; ACIP02000007; EEP27530.1; -; Genomic_DNA.
DR   RefSeq; WP_006907201.1; NZ_GG665867.1.
DR   AlphaFoldDB; C4GDQ1; -.
DR   STRING; 626523.GCWU000342_02225; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_0_0_9; -.
DR   Proteomes; UP000003494; 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:UP000003494}.
FT   DOMAIN          41..177
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          216..308
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          321..447
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   560 AA;  61258 MW;  1D1CD10F60C994D5 CRC64;
     MYQEEYQRWL TADLEDLDLR RELLSIQGKD EEIKDRFAVS LKFGTAGLRG VIGAGTNRMN
     IKLVGQATQG LANWVKTQGG NQSVAISYDS RIKSDVFARR AASVLAANGI RVFIYDALMP
     VPALSFATRY YGCNAGIMIT ASHNPAKYNG YKAYGPDGCQ MTDDAAAIVY EEIQKTDILT
     GVSCDSFAAG VASGKIQFIG DDCKKAFYQA IEERQVRPGL CKSASLKLVY SPLNGTGLVP
     VTQVLSDIGI EDIRLVPEQQ YPNGYFTTAP YPNPEIRQAL SYGLDLAEKE GADLMLATDP
     DADRVGIAMR CPDGSYELVS GNEMGALLLD YICAGRIETG TMPVDPVAVK SIVSTPLADA
     IASHYGVEMR SVLTGFKWIG DQIAGLEAKG EVDRFIFGFE ESYGYLAGPY VRDKDAVIAS
     MLICEMAAYY RSIGSSIKER LEEIYRSYGR YLNQVDSYEF PGLSGMDTMA RIMDSFRSAP
     PRDFAGIAVT AVHDYEKSEE TGLPKSNVLI YELEDGSSLV IRPSGTEPKI KNYFTTRGKD
     LAEAQAKKDL LASAIRPLMK
//
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