ID   A0A366ID47_9GAMM        Unreviewed;       547 AA.
AC   A0A366ID47;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:RBP67553.1};
GN   ORFNames=DES54_10166 {ECO:0000313|EMBL:RBP67553.1};
OS   Brenneria salicis ATCC 15712 = DSM 30166.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Brenneria.
OX   NCBI_TaxID=714314 {ECO:0000313|EMBL:RBP67553.1, ECO:0000313|Proteomes:UP000253046};
RN   [1] {ECO:0000313|EMBL:RBP67553.1, ECO:0000313|Proteomes:UP000253046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 30166 {ECO:0000313|EMBL:RBP67553.1,
RC   ECO:0000313|Proteomes:UP000253046};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:RBP67553.1}.
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DR   EMBL; QNRY01000001; RBP67553.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366ID47; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000253046; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05801; PGM_like3; 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; IPR005852; PGM_a-D-Glc-sp.
DR   NCBIfam; TIGR01132; pgm; 1.
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   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          40..178
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          210..317
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          320..440
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          491..539
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   547 AA;  58721 MW;  0EB50342339C64BE CRC64;
     MANHPRAGQP TRQSDLINVA QLTSQYYVLR PEVGNAAHAV KFGTSGHRGS AGRHSFNETH
     ILAIAQAIAE ERKKQGISGP CYVGKDTHAL SEPAFISVLE VLTANGVDVI VQQDNGFTPT
     PAVSNAILAH NRQGGAQADG IVITPSHNPP EDGGIKYNPP NGGPADTNLT SVVEKRSNAL
     LADELRDVKR ITLDQAWKSG YLHEQDLVQP YVEGLTSVVD MAAIQRAGLK LGVDPLGGSG
     IAYWQRIAEH YKLDLTLVND AVDQTFRFMT LDHDGVIRMD CSSVSAMAGL LALRDKFDLA
     FANDPDYDRH GIVTPAGLMN PNHYLAVSIN YLFQHRPQWG ESVAVGKTLV SSAMIDRVVA
     DLGRKLVEVP VGFKWFVDGL FDGSFGFGGE ESAGASFLRF DGTPWSTDKD GIIMCLLAAE
     ITAVTGKNPQ QHYDDLAQRF GAPSYNRIQA SATQAQKAAL SRLSPEQVSA STLAGDAITA
     RLTTAPGNGA AIGGLKVMTD NGWFAARPSG TEEAYKIYCE SFLGAEHRER IEKEAVEIVS
     NVLANAS
//