ID   A0A1I5GKN3_9BURK        Unreviewed;       556 AA.
AC   A0A1I5GKN3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:SFO36503.1};
GN   ORFNames=SAMN05443579_102634 {ECO:0000313|EMBL:SFO36503.1};
OS   Variovorax sp. PDC80.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1882827 {ECO:0000313|EMBL:SFO36503.1, ECO:0000313|Proteomes:UP000199369};
RN   [1] {ECO:0000313|Proteomes:UP000199369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PDC80 {ECO:0000313|Proteomes:UP000199369};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOWG01000002; SFO36503.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5GKN3; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000199369; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199369}.
FT   DOMAIN          47..186
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          218..323
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          331..448
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          498..546
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   556 AA;  59542 MW;  E649C3546211313E CRC64;
     MSPASKTSAP AALPGQPAPH DLLVNVPRLI SAYYSGRPDP SVAAQRVAFG TSGHRGSSFD
     NGFNEWHVLA ISQAICDYRR QKGIDGPLFL GIDTHALSTP AFNSAVEVLA ANGVELMLSQ
     DDEYTPTPAV SHAILVYNRG RTTGLADGIV ITPSHNPPES GGFKYNPPNG GPAGTDITSA
     VEAAANGFLA NGLQGVKRLP LAQALKASTT HRHDYLNTYV EDLAQVLDMD AIRDVRIELG
     VDPLGGAGVH YWPAIAERYK LSRLTVLSQE VDPTFRFMSL DWDGRIRMDP SSPDAMHQLI
     ALKDRFGIAF ACDTDHDRHG VVAGSSGLMQ PNSYLAVMID YLYTHRPDWP AAAAVGKTVV
     SSRMIDRVAQ RLGRRLYEVP VGFKWFVDGL VDGSLAFGGE ESAGATFLRR DGTAWTTDKD
     GIVPALLSAE IAARTGRDPG ERYAELTQAL GRPVSDRVDA AATVEQKKRL SSLSPAQIRS
     TELAGEKIVE VLSHAPGNGA AIGGVKVVTE NGWFAARPSG TENIYKIYGE SFQGQEHLAR
     ILEEAQQVVD GALAAP
//