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Database: UniProt
Entry: A0A2T4U6I4_9BACI
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ID   A0A2T4U6I4_9BACI        Unreviewed;       577 AA.
AC   A0A2T4U6I4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
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   ORFNames=C6Y45_08490 {ECO:0000313|EMBL:PTL39008.1};
OS   Alkalicoccus saliphilus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalicoccus.
OX   NCBI_TaxID=200989 {ECO:0000313|EMBL:PTL39008.1, ECO:0000313|Proteomes:UP000240509};
RN   [1] {ECO:0000313|EMBL:PTL39008.1, ECO:0000313|Proteomes:UP000240509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6AG {ECO:0000313|EMBL:PTL39008.1,
RC   ECO:0000313|Proteomes:UP000240509};
RA   Zhao B.;
RT   "Alkalicoccus saliphilus sp. nov., isolated from a mineral pool.";
RL   Submitted (MAR-2018) 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:PTL39008.1}.
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DR   EMBL; PZJJ01000011; PTL39008.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4U6I4; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000240509; 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:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
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   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022526};
KW   Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
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}.
FT   DOMAIN          43..179
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          210..319
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          327..453
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          510..552
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   577 AA;  64849 MW;  EF755D705F1E5BD9 CRC64;
     MEWKKQYERW KSELNLDPEL SKALKKLTGN EKMLEDSFYK NLEFGTGGMR GEIGPGTNRM
     NIYTIRKGAQ GLADFIKEAG EQAVQKGVVI AHDNRRMSKE FALEAACTLG ANGIKTYLFK
     ELRPTPQLSY AVRKLATHAG VMVTASHNPP EYNGFKVYGE DGAQLIPEEA DRLIAKVDAV
     ADELNIETKE AVHLEEKGLL HWVLEELDEA YARELQTVLI DREVIREQAD NFSIVFTPLH
     GTATVPMQRA LKEAGFNKVF TVEEQAVPDT EFSTVSSPNP EEAGAFELAM KLGDEKQADL
     LIATDPDADR IGLVVRDDKG EYIVLSGNQT GALLLDYLLS KKSEKGELPA NGVMIKTIVT
     SELGRAVAEA YNVTSLDVLT GFKFIGEKIR EYDTTGEYKF LFGYEESYGY LIEPFARDKD
     AIQPGLLAAE MGAYYKAQGM TLYEGLQNLY KTYGYFYEDL ASFTFKGKEG AEKIQRIMEV
     FRKRADERSL SEDTDYIEDY LRGERTFMDG RNKEQIELPE SNVLKVFLQD GSWYCLRPSG
     TEPKIKCYFG VKAGTHEQAE ASLRSLKENT LAEIEKI
//
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