ID   A0A0A1FCC2_9BURK        Unreviewed;       559 AA.
AC   A0A0A1FCC2;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:AIY42161.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:AIY42161.1};
GN   ORFNames=LT85_3003 {ECO:0000313|EMBL:AIY42161.1};
OS   Collimonas arenae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=279058 {ECO:0000313|EMBL:AIY42161.1, ECO:0000313|Proteomes:UP000030302};
RN   [1] {ECO:0000313|EMBL:AIY42161.1, ECO:0000313|Proteomes:UP000030302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cal35 {ECO:0000313|EMBL:AIY42161.1,
RC   ECO:0000313|Proteomes:UP000030302};
RA   Uroz S., Tech J.J., Sawaya N.A., Frey-Klett P., Leveau J.H.J.;
RT   "Structure and function of bacterial communities in ageing soils: insights
RT   from the Mendocino ecological staircase.";
RL   Soil Biol. Biochem. 69:265-274(2014).
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}.
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DR   EMBL; CP009962; AIY42161.1; -; Genomic_DNA.
DR   RefSeq; WP_038490103.1; NZ_CP009962.1.
DR   AlphaFoldDB; A0A0A1FCC2; -.
DR   STRING; 279058.LT85_3003; -.
DR   KEGG; care:LT85_3003; -.
DR   HOGENOM; CLU_016950_8_1_4; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000030302; Chromosome.
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; 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, ECO:0000313|EMBL:AIY42161.1};
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}.
FT   DOMAIN          40..179
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          211..315
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          323..436
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          489..539
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   559 AA;  59707 MW;  3CD0638FC7874E2A CRC64;
     MKISPLAGKP APMALLVDVP KLVSAYYTNI PDPEVVEQRV AFGTSGHRGS SFDSSFNEAH
     VLAISQAICT YRSKHGINGP LFVGADTHAL SVSACASAVE VLAANGVDIM LAEGDEYTPT
     PAVSHAIINY NRGRSSGLAD GIVITPSHNP PEDGGFKYNP PNGGAADTDV TGWIEAAANA
     FLKGGLKDVK RMPLQKALRL DTTHRYDFLN TYVSELGLVI DMGVIRDAGI HLGVDPLGGA
     GVHYWQRIGE HYKLNLSVIS EEVDPTFRFM ALDWDGRIRM DPSSSYAMQR LLGMRDRYDI
     AFACDTDHDR HGIVTRSVGL MPANHYLAVA IEYLFQHRSQ WPQTAGVGKT VVSSQIIDRI
     CARLKRKLVE VPAGFKWFAD GLSDGSLGFG GEESAGATFL RLDGSAWTTD KDGLVPGLLA
     AEITARSGRD PGDAYRLLAS EFGDPVATRV EASATPAQKK MLAALSPQKI QSTELAGEKI
     QSVISKAPGN DAPVGGVRVA TAGGWFAARP SGTENIYKIY AESFHGEDHL QRIVKEAQAI
     VDAALAGASQ SQPPPAATK
//