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Database: UniProt
Entry: A0A0L6T5X8_9BURK
LinkDB: A0A0L6T5X8_9BURK
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ID   A0A0L6T5X8_9BURK        Unreviewed;       463 AA.
AC   A0A0L6T5X8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KNZ31566.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:KNZ31566.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:KNZ31566.1};
GN   ORFNames=AD742_16380 {ECO:0000313|EMBL:KNZ31566.1};
OS   Methylibium sp. NZG.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Methylibium.
OX   NCBI_TaxID=1686064 {ECO:0000313|EMBL:KNZ31566.1, ECO:0000313|Proteomes:UP000053102};
RN   [1] {ECO:0000313|Proteomes:UP000053102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bi G.;
RT   "Draft Genome Sequences of the MTBE Degrading Bacterium Methylibium sp.
RT   NZG.";
RL   Submitted (JUL-2015) 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:KNZ31566.1}.
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DR   EMBL; LGRD01000030; KNZ31566.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6T5X8; -.
DR   STRING; 1686064.AD742_16380; -.
DR   PATRIC; fig|1686064.3.peg.2093; -.
DR   Proteomes; UP000053102; 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: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; IPR016066; A-D-PHexomutase_CS.
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.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KNZ31566.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053102}.
FT   DOMAIN          7..139
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          159..252
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          257..365
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          371..449
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   463 AA;  49327 MW;  86D0E2231C3B0480 CRC64;
     MQIVASNFKA YDIRGVVGTT IDEAFAEHLG RAFGTEARHA GERAVAVGRD GRLSGPSLAA
     ALIRGLVATG LDVVDLGPVT TPMLYYVAAT RGAHGCHSGV MVTGSHNPKD YNGFKMVLAG
     RAIYGDQIQG LRRRMEAEDY FLSPGRAAAM DVLPEYRARI AGDCKLARTM KVVVDSGNGI
     PGASSPGILR ALGCDVTELY SEVDGDFPNH HPDPSKPENL AELIRTVQAT GAELGLAFDG
     DGDRLGVVTR DGQVIYPDRQ LMLLATDILV RNPGGTVIFD VKCTQRLAPA IVAAGGKPLM
     WKTGHSLIKA KMKEVKSPIS GEMSGHIFFG ERWFGFDDAT YTAARLLEIL SRSADPSAVL
     NALPTSFSTP ELNVPCAEGE PARVVKQLLE TASFPGSSEI ITIDGLRVEY DDGFGLIRPS
     NTTPVLVLRF EGHTPQALAR IEAAMMGALR TVKPDASFTA AAH
//
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