ID A0A371AWZ3_9FIRM Unreviewed; 575 AA.
AC A0A371AWZ3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=DWV06_07155 {ECO:0000313|EMBL:RDU24061.1};
OS Anaerosacchariphilus polymeriproducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerosacchariphilus.
OX NCBI_TaxID=1812858 {ECO:0000313|EMBL:RDU24061.1, ECO:0000313|Proteomes:UP000255036};
RN [1] {ECO:0000313|EMBL:RDU24061.1, ECO:0000313|Proteomes:UP000255036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCWD5 {ECO:0000313|EMBL:RDU24061.1,
RC ECO:0000313|Proteomes:UP000255036};
RA Kim W., Yang S.-H., Oh J., Lee J.-H., Kwon K.K.;
RT "Anaerosacharophilus polymeroproducens gen. nov. sp. nov., an anaerobic
RT bacterium isolated from salt field.";
RL Submitted (JUL-2018) 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}.
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:RDU24061.1}.
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DR EMBL; QRCT01000016; RDU24061.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371AWZ3; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000255036; 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:UP000255036}.
FT DOMAIN 44..181
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 327..436
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 575 AA; 65186 MW; 1F7633303C30F409 CRC64;
MKDYIKEYEN WCFDEYFEEE DRKELLGLKG QQEEIQDRFY KDLEFGTGGL RGIIGAGTNR
INIYTVRKAT QGLANYILKQ EKEEKSVAIA FDSRRMSSEF AMEAALCLAG NGIKVYLFEE
LRPTPELSFA VRHLGCIAGI VITASHNPPE YNGYKVYWED GAQITYPKDV EIIAEVNKVN
DYKTVKIIDK NEALDSGLLI FIGNEIDSLY MQALKRLVIN PDLVEQVGKK LKIVYTPIHG
TGNVPVRRIL KELGFEHVYV VPEQEMPDEN FSTVKYPNPE DKEVFKLALE LAKKVDADII
LATDPDADRL GVYAKDSKTG QFKAFTGNMS GALICEYLFS QKREKGRLSS KGALVKTIVT
TNMADAIAKR YGATLIETLT GFKYIGEQIK LFEQNKKYEF EFGFEESYGC LLGTHARDKD
AVVAVMTLCE AAAYYKNLGI TLWDQMIRMY ETYGYFREDL HTKTFKGAEG AVQIQSLLDS
LRENPLKEVG GYQVKSISDF LTGEKKYLGD GKAEKIKLLK SNVLYYELEN DAWFCVRPSG
TEPKIKYYFG VNGFGFEDSE KKLEQLKQGV LSLGE
//
