ID A0A0A1GYX3_9LACO Unreviewed; 574 AA.
AC A0A0A1GYX3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-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=pgm {ECO:0000313|EMBL:BAP86198.1};
GN ORFNames=LOOC260_116920 {ECO:0000313|EMBL:BAP86198.1};
OS Paucilactobacillus hokkaidonensis JCM 18461.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1291742 {ECO:0000313|EMBL:BAP86198.1, ECO:0000313|Proteomes:UP000031620};
RN [1] {ECO:0000313|EMBL:BAP86198.1, ECO:0000313|Proteomes:UP000031620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LOOC260 {ECO:0000313|EMBL:BAP86198.1,
RC ECO:0000313|Proteomes:UP000031620};
RA Tanizawa Y., Tohno M., Kaminuma E., Nakamura Y., Arita M.;
RT "Complete genome sequence and analysis of Lactobacillus hokkaidonensis
RT LOOC260T.";
RL Submitted (NOV-2014) 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; AP014680; BAP86198.1; -; Genomic_DNA.
DR RefSeq; WP_041094265.1; NZ_AP014680.1.
DR AlphaFoldDB; A0A0A1GYX3; -.
DR STRING; 1291742.LOOC260_116920; -.
DR KEGG; lho:LOOC260_116920; -.
DR HOGENOM; CLU_016950_0_0_9; -.
DR Proteomes; UP000031620; Chromosome.
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}.
FT DOMAIN 43..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..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 515..551
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 574 AA; 63751 MW; 8E640C38E92A12F5 CRC64;
MSWKDTYQTW LNETSLELSL KNELQDMATN ETKLEDAFYA PLSFGTAGMR GLLGPGINRM
NIYTVRQATE GLARFMDTLD ESVKTRGVAI SFDSRHHSQD FAHEAAHVLG AHGIKSFVFE
GLRPTPELSF TVRHLHTYAG IMITASHNPK EYNGYKIYGE DGGQMPPKES DLITSYVRKV
SDLFNIQVAD ETQLMNDHTM KIIGDDVDQA YLAKVKTVTI NPKLAQEVGK DMKLVFTPLH
GTGQMLGEKA LQNAGFTNYE IVPEQAQPDP DFSTVTKPNP EDPAAFTLAI ELGKKVNADV
LVAVDPDADR LGTAVRQPNG EYQLLTGNQI ASVLLHYILE AHKQAGDLPV NAAVVKSIVS
TEFATKIAQS YNVAMINVLT GFKYIAQKIE QFEATGEHSY MFGFEESYGY LIKPFVHDKD
AIQSLVLLAE VAAYYRSQGK TLYDGLQELF QEYGYFREKT ISQTYAGIDG ADQIKALMKK
FREEAPTHFA GHAIVATEDF STQTKTTSDG KIVKIDLPVA NVLKYLLDDE TWIAIRPSGT
EPKLKFYIGT NAESLELANQ KLADFETALN EFIA
//
