ID A0A1H3JPT2_9FIRM Unreviewed; 574 AA.
AC A0A1H3JPT2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
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 ORFNames=SAMN02910414_01524 {ECO:0000313|EMBL:SDY41911.1};
OS Lachnobacterium bovis DSM 14045.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnobacterium.
OX NCBI_TaxID=1122142 {ECO:0000313|EMBL:SDY41911.1, ECO:0000313|Proteomes:UP000183918};
RN [1] {ECO:0000313|EMBL:SDY41911.1, ECO:0000313|Proteomes:UP000183918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14045 {ECO:0000313|EMBL:SDY41911.1,
RC ECO:0000313|Proteomes:UP000183918};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNPG01000017; SDY41911.1; -; Genomic_DNA.
DR RefSeq; WP_074717680.1; NZ_FNPG01000017.1.
DR AlphaFoldDB; A0A1H3JPT2; -.
DR STRING; 1122142.SAMN02910414_01524; -.
DR eggNOG; COG1109; Bacteria.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000183918; 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; 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:UP000183918}.
FT DOMAIN 43..178
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 208..314
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 326..452
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 574 AA; 64044 MW; 6051F461E1AC24B2 CRC64;
MDFSKEYQRW LTDSYFDEDT KAELRAIEGD KAEIEDRFYR TLEFGTAGLR GVIGAGTNRM
NIYTVRQATQ GLANYILSQN AQDKGVVIAH DCRIMSPEFT QEAALCLAAN GIKTYVFPSL
RPTPELSFAV RKLGCTAGIV VTASHNPREY NGYKVYWEDG AQITPPHDTN IMAEVAKVTD
FSQVKTMDLQ AAKDAGLYIT VSDEIDEPYF AELRKQSIHP EIIKKVAKDI KVVYTPFHGT
GLESVQRVLK DLGFENVYIE PTQAVADGNF PTVDYPNPED PKAWELALKL AKEKDADIVL
ATDPDADRLG VYCKDTKTGE YVSFTGNMSG MLIAEYILRE KTKLGIMPEN PALIESIVTT
DMAKAIAKAY DVKLIEVLTG FKYIGEQIKN FEETGSNNYV FGLEESYGCL PGTYARDKDA
PAAVTMLCEV AAYCKNEGKT LWDAMIDLYE KYGYYKEGLS TLTLKGVDGA AELKKLMDKA
RSSKFEQIGD YKVLAIRDYA DDTRLDMETG KVGSTGLPKS NVLYYELENN AWCCVRPSGT
EPKIKFYFGI KGESMEDAES KLESLKNAVN ELFQ
//
