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Database: UniProt
Entry: A0A069PLX8_9BURK
LinkDB: A0A069PLX8_9BURK
Original site: A0A069PLX8_9BURK 
ID   A0A069PLX8_9BURK        Unreviewed;       463 AA.
AC   A0A069PLX8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KDR41668.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:KDR41668.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:KDR41668.1};
GN   ORFNames=BG61_16285 {ECO:0000313|EMBL:KDR41668.1};
OS   Caballeronia glathei.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=60547 {ECO:0000313|EMBL:KDR41668.1, ECO:0000313|Proteomes:UP000027466};
RN   [1] {ECO:0000313|EMBL:KDR41668.1, ECO:0000313|Proteomes:UP000027466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 50014 {ECO:0000313|EMBL:KDR41668.1,
RC   ECO:0000313|Proteomes:UP000027466};
RA   Liu X.Y., Li C.X., Xu J.H.;
RT   "Draft Genome Sequences of Four Burkholderia Strains.";
RL   Submitted (MAR-2014) 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}.
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:KDR41668.1}.
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DR   EMBL; JFHC01000025; KDR41668.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A069PLX8; -.
DR   STRING; 60547.GCA_000751215_02737; -.
DR   Proteomes; UP000027466; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03089; PMM_PGM; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 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   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KDR41668.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027466}.
FT   DOMAIN          4..143
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          158..255
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          260..367
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          374..452
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   463 AA;  50740 MW;  23D46B86B69C0A56 CRC64;
     MSQSIFKAYD IRGIVGKTVD ADVARSIGRA FGSEIRKQGG DSVVVARDGR LSGPELVGAL
     ADGLRQAGVD VVDVGMVPTP VGYFAASVPL QLPTGERRVD SCMVVTGSHN PPDYNGFKMV
     LRGAAIYGEQ IQALYQRIVN SDFTQGEGTY TEYDISQAYL DRIVSDVKPV RPMKIVVDTG
     NGVAGGLAPR LFRALGCELV ELFTDIDGTF PNHHPDPAHP ENLQDVIRAL KETDAEIGFA
     FDGDGDRLGV VTKDGQVIYP DRQLMLFAQE VLSRNKGGQI IYDVKCTRNL AKWVREQGGE
     PLMWKTGHSL VKAKLRETGA PLAGEMSGHV FFKDRWYGFD DGLYTGARML EILSRVADPS
     KLLNDLPNSL STPELQLKLE EGENFELIAR LQKSAKFEGA DDVLTIDGLR VEYPDGFGLA
     RSSNTTPVVV MRFEADSDAA LKRIQEDFRR VILAEKPDAK LPF
//
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