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Database: UniProt
Entry: A0A0S8DUC9_9BACT
LinkDB: A0A0S8DUC9_9BACT
Original site: A0A0S8DUC9_9BACT 
ID   A0A0S8DUC9_9BACT        Unreviewed;       485 AA.
AC   A0A0S8DUC9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Phosphoglucomutase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AMJ78_07825 {ECO:0000313|EMBL:KPK39829.1};
OS   Omnitrophica WOR_2 bacterium SM23_29.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1703776 {ECO:0000313|EMBL:KPK39829.1, ECO:0000313|Proteomes:UP000050824};
RN   [1] {ECO:0000313|EMBL:KPK39829.1, ECO:0000313|Proteomes:UP000050824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_29 {ECO:0000313|EMBL:KPK39829.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPK39829.1}.
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DR   EMBL; LJUB01000093; KPK39829.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8DUC9; -.
DR   Proteomes; UP000050824; Unassembled WGS sequence.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05800; PGM_like2; 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; 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   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 2.
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}.
FT   DOMAIN          3..140
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          163..263
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          268..379
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          415..463
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   485 AA;  54118 MW;  4614FAF30FF7BA78 CRC64;
     MSIKFGTSGW RAVIADEFTF PNVRKASRAI ADYVKSNSTR RNSPPKIIIG YDTRFNSKEF
     ALSAANILAS NGIKVFLTNR DTPTPVISFQ IIDKMADGGI NITASHNPPE YNGLKFSPSH
     GGPAAPAVTK AIEKHVAKIK GEVEEMPLSC FKYPIEEFNP KARYIERIKK LICLTAIRRA
     KLKVIVDLMH GTGRGYLDEI LKDAGCKIEV LNKNLDPLFG GHPPEPAKEN LDKLIAEVKK
     RRANLGLALD GDADRFGIAD EKGRFYTPNE VISLLFKHLV DTRERLGQVA RTHSTTTLID
     RIAHRYGIEV IETPIGFKYI GEVLSKKDCI IGGEESGGLS IANHLPEKDG ILACLLVVEM
     VAMQRKKLSR ILKDLYREFG KSYPGKLNFT LTEDEKSRLL NMLDKHPPKK IAGLKISESN
     RVDGYKFILE DSSWVLIRPS GTEPLVRCHF EGTSHNKAKK LATYCQNLIR LFKLPLKIAT
     PPEED
//
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