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Database: UniProt
Entry: A0A179EQ84_ENTTH
LinkDB: A0A179EQ84_ENTTH
Original site: A0A179EQ84_ENTTH 
ID   A0A179EQ84_ENTTH        Unreviewed;       575 AA.
AC   A0A179EQ84;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
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   Name=pgm2 {ECO:0000313|EMBL:GEK35745.1};
GN   ORFNames=A6E74_07905 {ECO:0000313|EMBL:OAQ55408.1}, ETH01_00320
GN   {ECO:0000313|EMBL:GEK35745.1};
OS   Enterococcus thailandicus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=417368 {ECO:0000313|EMBL:OAQ55408.1, ECO:0000313|Proteomes:UP000078516};
RN   [1] {ECO:0000313|EMBL:OAQ55408.1, ECO:0000313|Proteomes:UP000078516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0711D 46 {ECO:0000313|EMBL:OAQ55408.1,
RC   ECO:0000313|Proteomes:UP000078516};
RA   Beukers A.G., Zaheer R., Goji N., Cook S.R., Amoako K., Chaves A.V.,
RA   Ward M.P., Mcallister T.A.;
RT   "Draft genome of an Enterococcus thailandicus strain isolated from bovine
RT   feces.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GEK35745.1, ECO:0000313|Proteomes:UP000321361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101867 {ECO:0000313|EMBL:GEK35745.1,
RC   ECO:0000313|Proteomes:UP000321361};
RA   Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT   "Whole genome shotgun sequence of Enterococcus thailandicus NBRC 101867.";
RL   Submitted (JUL-2019) 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:OAQ55408.1}.
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DR   EMBL; BJUG01000001; GEK35745.1; -; Genomic_DNA.
DR   EMBL; LWMN01000013; OAQ55408.1; -; Genomic_DNA.
DR   RefSeq; WP_067483863.1; NZ_LWMN01000013.1.
DR   AlphaFoldDB; A0A179EQ84; -.
DR   PATRIC; fig|417368.6.peg.2098; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000078516; Unassembled WGS sequence.
DR   Proteomes; UP000321361; 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:UP000078516}.
FT   DOMAIN          43..180
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          211..314
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          326..453
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          511..553
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   575 AA;  63534 MW;  602CC436285CDAFD CRC64;
     MSWEQVYEQW ANEVNLEENL KQQLTVLSQD SKQLEDAFYA PLGFGTAGMR GILGPGINRM
     NIYTVRQATE GLARFMDAQD PETKRRGVAI AYDSRHQSPE FAMEAAKTLA KHDIPSFVFE
     SLRPTPELSF AVRHLNAFTG IMITASHNPA AYNGYKVYGE DGGQMPPADA DALTKYVREV
     SNPLKVEVMS DEEVEHSGLI SIIGEEVDNA YLAEMKAVTI DHELIEEMGK DLKLVYTPLH
     GTGKMLGEKA LKQAGFEQFV LVPEQAIPDP DFTTVKSPNP EEHSAFEYAI RLGEKEGADL
     LIATDPDADR LGAAVRLPDG SYEVLTGNQL GAIMIQYILE AHQARKTMPA NPAVLKSIVS
     SELPTAIAKN YGATMFNVLT GFKFIAEKIQ QFEEDHSHTF MFGFEESYGY LVKPFVRDKD
     AIQALVLLAE VAAFYKKQGK TLYDGLQSIF ETYGYYAEKT ISVTMSGQEG SAKIAALMEK
     FRQEAPTEFA GAKVLQTEDF KKLTRTDAAG NVEALTTPPS DVLKYMLEEQ GWVAIRPSGT
     EPKIKFYIGV KGNSQDDAEA KIAAYEASIQ AITKD
//
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