ID G2FL81_9FIRM Unreviewed; 580 AA.
AC G2FL81;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
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 Name=pgcA {ECO:0000313|EMBL:EGW41589.1};
GN ORFNames=DOT_0442 {ECO:0000313|EMBL:EGW41589.1};
OS Desulfosporosinus sp. OT.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW41589.1, ECO:0000313|Proteomes:UP000004928};
RN [1] {ECO:0000313|EMBL:EGW41589.1, ECO:0000313|Proteomes:UP000004928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT {ECO:0000313|EMBL:EGW41589.1,
RC ECO:0000313|Proteomes:UP000004928};
RX PubMed=21994931; DOI=10.1128/JB.06018-11;
RA Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL J. Bacteriol. 193:6104-6105(2011).
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:EGW41589.1}.
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DR EMBL; AGAF01000023; EGW41589.1; -; Genomic_DNA.
DR RefSeq; WP_009613427.1; NZ_AGAF01000023.1.
DR AlphaFoldDB; G2FL81; -.
DR PATRIC; fig|913865.3.peg.402; -.
DR eggNOG; COG1109; Bacteria.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000004928; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
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 Isomerase {ECO:0000313|EMBL:EGW41589.1};
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326}.
FT DOMAIN 42..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..313
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 325..446
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 580 AA; 65266 MW; 713B8DEF12CC419F CRC64;
MSIQDRYTLW SEHPYFEEEI RQELRRITDP QEIEDRFYTD LEFGTGGLRG IIAAGTNRMN
KYVIRKATQG LAECVCDHGQ EGMKRGVVIA YDSRKYSSEF ALEAALVLAQ NGVKVYLFNA
LRPTPELSYA VRQLHALAGI VVTASHNPKE YNGYKVYWDD GGQVPPVKAD QILARIEARE
SWLGIEPMSI ENAKTSGLLE IIGEEIDQSY LAQVRKLALH PDLDEQKGKE LRIVYTPLHG
AGNILVRRAL AELGFCSVTV VPEQELPDPE FTTVPYPNPE IPATFELARK YGMELKADLL
LATDPDADRL GVVLRDLNGD FVQLTGNQIG ILLTYYILSQ KKALGTLPDN ATIIKTVAST
DLADEVARYF NVRVENVLTG FKFIAEKERE MEEGGWGTFQ FGFEESYGYL AGDFVRDKDA
VIASILLAEA ALYYRQVEGR SLFDVLELIY GKFGYYLDDQ ESLALRGIQG KEEIARIMNS
LRLEEILELG GIPIWKIDDY EQRIGKDTST GQTYPLTLPH SNVLRFSFHG GGFVMVRPSG
TEPKIKFYFS VKADTLPEAK DTLHRVKTDV MNRIAQIRSV
//
