ID   A0A2V3W226_9PROT        Unreviewed;       545 AA.
AC   A0A2V3W226;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:PXW88393.1};
GN   ORFNames=C8R34_10776 {ECO:0000313|EMBL:PXW88393.1};
OS   Nitrosomonas sp. Nm84.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=200124 {ECO:0000313|EMBL:PXW88393.1, ECO:0000313|Proteomes:UP000248024};
RN   [1] {ECO:0000313|EMBL:PXW88393.1, ECO:0000313|Proteomes:UP000248024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm84 {ECO:0000313|EMBL:PXW88393.1,
RC   ECO:0000313|Proteomes:UP000248024};
RA   Wagner M.;
RT   "Active sludge and wastewater microbial communities from Klosterneuburg,
RT   Austria.";
RL   Submitted (MAY-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:PXW88393.1}.
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DR   EMBL; QJJP01000007; PXW88393.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V3W226; -.
DR   Proteomes; UP000248024; 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:UP000248024}.
FT   DOMAIN          35..174
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          206..311
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          318..433
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          482..534
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   545 AA;  59610 MW;  30FCDC8FAEEEDBCD CRC64;
     MAGKPAETSM LVNVPRLITA YYSLVPDAAI PTQRVAFGTS GHRGSSFETS FNEWHVLAIS
     QAICDYRKEH GINGPLFLGI DTHALSESAY ASALEVLSAN GVEVMIADKN EYTPTPVISH
     AILTYNRGRK SGLADGIVIT PSHNPPDSGG FKYNPTHGGP AGSDITGCIE AMANAFLASG
     LQGVKRIPFE RAQRVATTHR HDFLNAYVND LSSVLDMDAI RDANIHMGVD PLGGAGVHYW
     RSIAERYGLN LTVVSETVDP TFHFMTLDWD GQIRMDPSSS YAMQRLIDNK DRFDIAFACD
     TDHDRHGIVT RNAGLLPPNH YLSVAIFYLF QYRPNWSKDA AIGKTVVSSQ MIDRVTEQLG
     RKLYEVPVGF KWFADGLLQG SLGFGGEESA GASFLRLNGS VWTTDKDGIV PALLSAEIIA
     RLGRDPGEIY RELELKFGES IYDRVEAAGT PEQKELLARL SPQQVKFTEL AGEKIQTILT
     HAPGNNAPIG GLKVISKSGW FAARPSGTED IYKIYAESFK GADHLHRIQE EAQTMVRDVL
     TAIPN
//