ID   A0A1I2BXR5_9ACTN        Unreviewed;       546 AA.
AC   A0A1I2BXR5;
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:SFE60907.1};
GN   ORFNames=SAMN05216251_10460 {ECO:0000313|EMBL:SFE60907.1};
OS   Actinacidiphila alni.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=380248 {ECO:0000313|EMBL:SFE60907.1, ECO:0000313|Proteomes:UP000199323};
RN   [1] {ECO:0000313|EMBL:SFE60907.1, ECO:0000313|Proteomes:UP000199323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3510 {ECO:0000313|EMBL:SFE60907.1,
RC   ECO:0000313|Proteomes:UP000199323};
RA   de Groot N.N.;
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; FONG01000004; SFE60907.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2BXR5; -.
DR   STRING; 380248.SAMN05216251_10460; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000199323; 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:UP000199323}.
FT   DOMAIN          39..179
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          210..317
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          321..441
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          492..540
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   546 AA;  58324 MW;  5D0FF7CF97042521 CRC64;
     MPHERAGTPA RPDDLVDVPR LITAYYALHP DPGETGQRVA FGTSGHRGSS LRTAFNEDHI
     AATSQAICDY RTRQGTTGPL FLGADTHALS EPARVTALEV FAANEVTVLI DEHDGWTPTP
     AVSHAILAYN RGRTDHVADG VVVTPSHNPP ADGGFKYNPP SGGPAASDAT GWIQDRANEL
     IADGLKGVRR IPYARALAAD TTGRYDFLGR YVDDLPAVLD LETVRREGVR IGADPLGGAS
     VAYWGRIAEW HGLDLTVVNP VADPTWRFMT LDWDGKIRMD CSSPYAMASL IARKDEYRIA
     TGNDADADRH GIVTPDGGLM NPNHYLAVAI SYLSRHREQW APDLAIGKTL VSSSMIDKVV
     ADLGRPLTEV PVGFKWFVDG LLGGTLAFGG EESAGASFLR RDGAAWTTDK DGILLALLAA
     EITAVTGRTP SEHYADLTAK FGAPSYARID APATPEEKAV LAKLSPKQVP AADLAGERVT
     SVLTEAPGNG AALGGIKVST ENAWFAARPS GTEDVYKIYA ESFLGDDHLA RVQEEARDIV
     SQALSD
//