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Database: UniProt
Entry: A0A225DEA2_9BACT
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ID   A0A225DEA2_9BACT        Unreviewed;       579 AA.
AC   A0A225DEA2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:OWK39792.1};
GN   ORFNames=FRUB_05682 {ECO:0000313|EMBL:OWK39792.1};
OS   Fimbriiglobus ruber.
OC   Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC   Fimbriiglobus.
OX   NCBI_TaxID=1908690 {ECO:0000313|EMBL:OWK39792.1, ECO:0000313|Proteomes:UP000214646};
RN   [1] {ECO:0000313|Proteomes:UP000214646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP5 {ECO:0000313|Proteomes:UP000214646};
RA   Ravin N.V., Rakitin A.L., Ivanova A.A., Beletsky A.V., Kulichevskaya I.S.,
RA   Mardanov A.V., Dedysh S.N.;
RT   "Genome analysis of Fimbriiglobus ruber SP5, the first member of the order
RT   Planctomycetales with confirmed chitinolytic capability.";
RL   Submitted (JUN-2017) 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:OWK39792.1}.
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DR   EMBL; NIDE01000009; OWK39792.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A225DEA2; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000214646; 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:UP000214646}.
FT   DOMAIN          40..179
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          210..315
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          323..441
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          483..539
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
FT   REGION          550..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   579 AA;  62629 MW;  E512595484A23333 CRC64;
     MKVSSLAGKP ADPSVLVNVP RLITAYFAEA PDASVPAQRV EFGTSGHRGS SFDTAFNEWH
     ILAISQAICL YRLRKGIDGP LFLGMDTHAL SVPALASALE VLAANGVEVL LAKDDEYTPT
     PAVSHAILTY NRGRTTGRAD GIVVTPSHNP PHDGGFKYNP PHGGPAEPAI TGWIEAKANE
     FLASGLRGVN RVPYERALRA STTHRHDYLD AYTKDLGNVI DMDAIRGAKI RLGVDPLGGA
     GVHYWEPIAE RYGLNLTVVN KVVDPTFRFM TVDWDGQIRM DPSSPYAMAR LIGLKDQFDI
     AFACDTDHDR HGIVTRSAGL LPPNHYLSVV VRYLFQHRPT WSNGAAVGKT LVSTQMIDRV
     AAKLDRKLYE VPVGFKWFVD GLLDGSLGFG GEESAGASFL RRDGSVWTTD KDGIIPALLA
     AEITARMGRD PGELYRDLTR EFGEPAYDRV ESPATPGQKQ LLAKLSPQQV KLTELAGEKI
     RAILTRAPAN DAPIGGLKVV AESGWFAARP SGTESIYKIY AESFKGADHL KRILEEARTI
     VGAALDAGSA PDAALTSPAP HEQTVSEAEE LWRAEGNPN
//
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