ID   A0A3P1VAR9_9ACTO        Unreviewed;       575 AA.
AC   A0A3P1VAR9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Phospho-sugar mutase {ECO:0000313|EMBL:RRD30600.1};
GN   ORFNames=EII10_00260 {ECO:0000313|EMBL:RRD30600.1};
OS   Actinomyces bowdenii.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=131109 {ECO:0000313|EMBL:RRD30600.1, ECO:0000313|Proteomes:UP000271272};
RN   [1] {ECO:0000313|EMBL:RRD30600.1, ECO:0000313|Proteomes:UP000271272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OH5050 {ECO:0000313|EMBL:RRD30600.1,
RC   ECO:0000313|Proteomes:UP000271272};
RA   Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA   Eisen J.A., Holcombe L.J., O'Flynn C.;
RT   "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT   for Automated Genome-Based Taxonomic Assignment.";
RL   Submitted (NOV-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:RRD30600.1}.
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DR   EMBL; RQZC01000001; RRD30600.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P1VAR9; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000271272; 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; cd05799; PGM2; 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; 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:UP000271272}.
FT   DOMAIN          56..198
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          221..321
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          335..445
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          517..540
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   575 AA;  60693 MW;  F8570B06785F00B4 CRC64;
     MTQSPEQDLD AVVTSWIAED PDPVTRAELD GLLQAHRSGQ GEATAALADA FGSTLAFGTA
     GLRGRLGGGP ARMNRVVVIR AAAGLAAYLR ERVGEGFTAV IGYDARHGSA QFARDTASVI
     TGAGGRALLF DSHCPTPVLA FALRHLGADA GVMVTASHNP PQDNGYKVYL GGRAVSDWGQ
     GAQIVPPHDE RIAAAIEAVG PISDVPMPEQ GWEAVDPGIR EEYLERVTQT ACSRRLAPVR
     IVLTAMHGVG GPLCRQALER AGFDDIVEVA EQFQPDPDFP TVPFPNPEEP GALDLSMALA
     RKVDADLIIA NDPDADRCSA AIPDPTAEGG WRQLTGDEVG ALLGEQAAEL AAFAGTGVLA
     NSIVSSRLLR RIAQSHGLGH RQTLTGFKWI SRVPDLVFGY EEALGYCVDP TAVRDKDGIS
     ASVCLASLAS VLKQQGRSIP DLLDRLARDH GLHATSPLSL RVEDLSIITR AMERLRSGGA
     PARLAGSPVV EELDLLDGAP DCTGGTLPPT NGLVWTTAAD DRVIIRPSGT EPKLKCYCEV
     ILPVGKQDDM AALRRAAAQR LEQIKSDLRG VLGMG
//