ID   A0A1C5JQR0_9ACTN        Unreviewed;       547 AA.
AC   A0A1C5JQR0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:SCG72847.1};
GN   ORFNames=GA0070614_5084 {ECO:0000313|EMBL:SCG72847.1};
OS   Micromonospora coxensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=356852 {ECO:0000313|EMBL:SCG72847.1, ECO:0000313|Proteomes:UP000198215};
RN   [1] {ECO:0000313|EMBL:SCG72847.1, ECO:0000313|Proteomes:UP000198215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45161 {ECO:0000313|EMBL:SCG72847.1,
RC   ECO:0000313|Proteomes:UP000198215};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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; LT607753; SCG72847.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5JQR0; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000198215; Chromosome i.
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}.
FT   DOMAIN          40..180
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          489..540
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
FT   REGION          29..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   547 AA;  57933 MW;  E688D2A1F50A5179 CRC64;
     MAHPRAGQPA EPADLVDVPR LVTAYYAEHP DPDDPAQQVS FGTSGHRGSS LRTAFNSDHI
     LAVTQALCDY RREQGVDGPL FLARDTHALS APAAVDALEV LAANDVTVLV DSRDGYTPTP
     ALSHAVLTHN RGRTSGLADG IVITPSHNPP DDGGFKYNPT HGGPADSDVT TWIQDRANAI
     LAAGLKEVRR IPYARARAAD TTGTYDFLAR YVDDLPAAID IDAIRDAGVR IGADPLGGAS
     VAYWGEIAER HRLDLTVLNP TVDPTWRFMT LDGDGKIRMD CSSPNAMASL IAARADYQVS
     TGNDADADRH GIVTPDGGLM NPNHYLAVAI GHLFRTREQW GPAAAVGKTL VSSSMIDRIA
     ADLERPLLEV PVGFKWFVPG LLDGAVGFGG EESAGASFLR RDGSTWTTDK DGILLCLLAS
     EIIATTGRTP SQHYAELTER FGAPAYARID APADRRQKAV LGKLSPEQVG ATELAGEPIT
     ATLTAAPGNG AAIGGLKVTT ASGWFAARPS GTEDVYKIYA ESFQGPEHLA RIQEEAKALV
     DGVLAKA
//