ID E0S0H5_BUTPB Unreviewed; 592 AA.
AC E0S0H5;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 OrderedLocusNames=bpr_I0554 {ECO:0000313|EMBL:ADL33300.1};
OS Butyrivibrio proteoclasticus (strain ATCC 51982 / DSM 14932 / B316)
OS (Clostridium proteoclasticum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=515622 {ECO:0000313|EMBL:ADL33300.1, ECO:0000313|Proteomes:UP000001299};
RN [1] {ECO:0000313|EMBL:ADL33300.1, ECO:0000313|Proteomes:UP000001299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51982 / DSM 14932 / B316
RC {ECO:0000313|Proteomes:UP000001299};
RX PubMed=20689770; DOI=10.1371/journal.pone.0011942;
RA Kelly W.J., Leahy S.C., Altermann E., Yeoman C.J., Dunne J.C., Kong Z.,
RA Pacheco D.M., Li D., Noel S.J., Moon C.D., Cookson A.L., Attwood G.T.;
RT "The glycobiome of the rumen bacterium Butyrivibrio proteoclasticus B316(T)
RT highlights adaptation to a polysaccharide-rich environment.";
RL PLoS ONE 5:E11942-E11942(2010).
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; CP001810; ADL33300.1; -; Genomic_DNA.
DR AlphaFoldDB; E0S0H5; -.
DR STRING; 515622.bpr_I0554; -.
DR KEGG; bpb:bpr_I0554; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_0_0_9; -.
DR Proteomes; UP000001299; Chromosome 1.
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:UP000001299}.
FT DOMAIN 57..197
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 225..330
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 343..470
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 592 AA; 66007 MW; 0AEC75222E4ACA2B CRC64;
MITDILNNEE DKIMSDAKKQ LEYWLGDSYF DEETKQELLS IRNDEAEVED RFYRELEFGT
GGLRGVIGAG TNRMNKYTVR KASQGLANYI KKNGGADAAK RGVAISFDCR KFSPEFADET
ALCLAANGIK AYVSDILRPT PELSFALREF GCIAGVMITA SHNPPEYNGY KVYWEDGAQI
TPPHDTGIIS EVMAITDYHD VKTMSKEDAI AAGLYVSFGE EIDDKYMVEL KKQIIHKDVI
DEMADKFTIV YSPFHGTGNL PVRRVLKELG FKNVFVVPEQ ELPDPEFTTL AYPNPEDPKA
FELALKLAKE KDADIVLATD PDADRLGIYA KDNKTGEYVA FTGNMSGMLI GDYILRERQA
TGTMPANPAF VTTIVTTNMA RVVAEKYGLH YIEVLTGFKY IGEQIKLFEQ NGQSHNYVFG
LEESYGCLAG THARDKDAVV AVMMLCELAA FYKKQGKSVW DAMIDMYEEY GYYKEGQYSI
TMKGKEGAEQ IAALMDRLRS NPPKEFGSFK VVEFRDYKTG KTLDMATGKE GQTGLPTSNV
LYFALDNDAW CCARPSGTEP KIKFYMGVKG TGLEDADKLQ KELTDAVKAV IG
//
