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Database: UniProt
Entry: A0A2A9EMA7_9MICO
LinkDB: A0A2A9EMA7_9MICO
Original site: A0A2A9EMA7_9MICO 
ID   A0A2A9EMA7_9MICO        Unreviewed;       559 AA.
AC   A0A2A9EMA7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:PFG39392.1};
GN   ORFNames=ATJ97_1898 {ECO:0000313|EMBL:PFG39392.1};
OS   Georgenia soli.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC   Georgenia.
OX   NCBI_TaxID=638953 {ECO:0000313|EMBL:PFG39392.1, ECO:0000313|Proteomes:UP000222106};
RN   [1] {ECO:0000313|EMBL:PFG39392.1, ECO:0000313|Proteomes:UP000222106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21838 {ECO:0000313|EMBL:PFG39392.1,
RC   ECO:0000313|Proteomes:UP000222106};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2017) 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:PFG39392.1}.
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DR   EMBL; PDJI01000004; PFG39392.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A9EMA7; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000222106; 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; IPR045244; PGM.
DR   InterPro; IPR005852; PGM_a-D-Glc-sp.
DR   NCBIfam; TIGR01132; pgm; 1.
DR   PANTHER; PTHR22573:SF57; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 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:UP000222106}.
FT   DOMAIN          39..187
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          217..330
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          334..454
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          504..552
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   559 AA;  58995 MW;  21B552CCB1489321 CRC64;
     MHERAGTPAL PEDLIDVGEV VSAYYDRTPD LDDPAQQVVF GTSGHRGSSL DGAFNEAHIV
     ATTAAIVEYR RAQGYDGALY LGRDTHALSE PAWRTALEVL AAAGVDTRID ARDSFTPTPA
     ISHAILRDNG AGTSGGVRTE GPGLADGIVV TPSHNPPRDG GFKYNPPNGG PAGSDATSAI
     AARANEILRE GWEEVGRIPF ERAVAADTTR KNDFITAYVD DLVNVLDLDA IRRAGVRIGA
     DPLGGASVEY WAAIGERHGL DLTVVNPEVD PRWSFMTLDW DGKIRMDCSS PYAMASLREK
     MRGDGGAAPF DVATGNDADS DRHGIVTPDG GLMNPNHYLA VAIEYLFSHR PHWSAEAAVG
     KTLVSSALID RVAAGLGRRL IEVPVGFKYF VPGLLDGSVG FGGEESAGAS FLRKDGTVWT
     TDKDGILLAL LASEIIAVTG KSPSQLHAEL VERYGASSYA RIDAAATKAQ KAKLGKLQPA
     DVAATEIAGE PIVDRLVDAP GNGAAIGGLK VTTSSAWFAA RPSGTEDVYK IYAESFQGDD
     HLAQVQAEAK KVVDEALAE
//
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