ID   A0A1H8V9D2_9ACTN        Unreviewed;       544 AA.
AC   A0A1H8V9D2;
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:SEP11857.1};
GN   ORFNames=SAMN05660991_03349 {ECO:0000313|EMBL:SEP11857.1};
OS   Trujillella endophytica.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Trujillonella.
OX   NCBI_TaxID=673521 {ECO:0000313|EMBL:SEP11857.1, ECO:0000313|Proteomes:UP000198960};
RN   [1] {ECO:0000313|EMBL:SEP11857.1, ECO:0000313|Proteomes:UP000198960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45413 {ECO:0000313|EMBL:SEP11857.1,
RC   ECO:0000313|Proteomes:UP000198960};
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; FOEE01000011; SEP11857.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8V9D2; -.
DR   STRING; 673521.SAMN05660991_03349; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000198960; 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}.
FT   DOMAIN          40..179
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          208..315
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          319..439
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          484..538
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   544 AA;  57059 MW;  CD377F5C1F0BE1BA CRC64;
     MSDVRAGQPA EPSDLVDVAA LVTAYYTLDP DPTEPAQQVA FGTSGHRGSS LDAAFNEAHI
     LATTQAICEY RAAQGVDGPL FLGRDTHALS EPAWASALEV LAANDVTVLV DAADRYTPTP
     AVSHAILRAN RGKNGGRADG IVVTPSHNPP RDGGFKYNPP HGGPADSDAT KAIADRANEL
     LRAGLDGVRR IPFARARAAA SAYDFTGTYV EDLPSVLDLD AVRAAGVRIG ADPLGGASVD
     YWGAIAERHR LDLTVVNPLV DPTWRFMTLD WDGKIRMDCS SPSAMASLIG KRADYAIATG
     NDADADRHGI VTPDGGLMNP NAFLAVAISH LFSSRPEWGA QTAVGKTLVS SSLIDRVVAG
     LGRRLVEVPV GFKWFVPGLL DGSVGFGGEE SAGASFLRRD GGVWTTDKDG MLLALLAAEI
     QAVTGRSPSQ LHGELTERYG ESAYARVDAP ATREQKAALA KLSPEAVTAT ELAGEPIVAK
     LTRAPGNDAP IGGLKVVTEN AWFAARPSGT EDVYKIYAES FAGPDHLARV QEEARAVVTA
     ALAG
//