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Database: UniProt
Entry: A0A1G6L1N9_9BACI
LinkDB: A0A1G6L1N9_9BACI
Original site: A0A1G6L1N9_9BACI 
ID   A0A1G6L1N9_9BACI        Unreviewed;       580 AA.
AC   A0A1G6L1N9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
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=SAMN05421734_10769 {ECO:0000313|EMBL:SDC37299.1};
OS   Pelagirhabdus alkalitolerans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pelagirhabdus.
OX   NCBI_TaxID=1612202 {ECO:0000313|EMBL:SDC37299.1, ECO:0000313|Proteomes:UP000242949};
RN   [1] {ECO:0000313|Proteomes:UP000242949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S5 {ECO:0000313|Proteomes:UP000242949};
RA   Varghese N., Submissions S.;
RL   Submitted (SEP-2016) 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}.
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DR   EMBL; FMYI01000007; SDC37299.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6L1N9; -.
DR   STRING; 1612202.SAMN05421734_10769; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000242949; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242949}.
FT   DOMAIN          43..182
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          210..317
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          508..555
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   580 AA;  65256 MW;  FC08A50BA959F328 CRC64;
     MSWQTTYEKW KQFKQLDPEL KQQLEEMKDD EVKLEDSFYK ELEFGTGGLR GEIGPGSNRL
     NIYTIRKAAK GLADYIESQG EIAKQKGVAI SYDCRFKSPL FAMETAKTLA SQGIKAYVFE
     SLRSTPELSY AVRHLNTYSG VMVTASHNPP EYNGFKAYNQ FGGQLPPEEA EAVIDYVNQI
     DNELEIQVED EATLKEKGLI EMIGETVDRA YQSKLTSVVQ NKELIQEMGD DLSIVFTPLH
     GTGNVPIRQA LKQMGFNNVS VVASQEEPDP RFSTVKSPNP EENEAFELAI EQGIKQDADV
     LIGTDPDADR VGVAALNNQG EYEVLTGNQV GALMLEYLIK AKKANQTLDK GATLIKTIVT
     SEMGRDIAKA NGIDTIDTLT GFKFIGEKIK EFEDQQNRSF LFGYEESYGY LVEDFVRDKD
     AVQAAMLIAE VAAFYKNKGM TLYQGLQAIY EEYGYYYESL QALTLKGKEG AEKINELLVS
     FREEPPKEVA EQAVVKIEDY KTSCRLDVKK NVEESIDLPK SNVLKYFLAD GSWFCVRPSG
     TEPKVKFYFA VNGEAEFETK SKLNKLEFDV MKRVREFVNA
//
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