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Database: UniProt
Entry: J1H6M3_9ACTO
LinkDB: J1H6M3_9ACTO
Original site: J1H6M3_9ACTO 
ID   J1H6M3_9ACTO            Unreviewed;       558 AA.
AC   J1H6M3;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:EJF40943.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:EJF40943.1};
GN   Name=pgm {ECO:0000313|EMBL:EJF40943.1};
GN   ORFNames=HMPREF1317_1486 {ECO:0000313|EMBL:EJF40943.1};
OS   Schaalia georgiae F0490.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Schaalia.
OX   NCBI_TaxID=1125717 {ECO:0000313|EMBL:EJF40943.1, ECO:0000313|Proteomes:UP000004578};
RN   [1] {ECO:0000313|EMBL:EJF40943.1, ECO:0000313|Proteomes:UP000004578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0490 {ECO:0000313|EMBL:EJF40943.1,
RC   ECO:0000313|Proteomes:UP000004578};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (MAY-2012) 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:EJF40943.1}.
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DR   EMBL; AKFS01000239; EJF40943.1; -; Genomic_DNA.
DR   RefSeq; WP_005871392.1; NZ_AKFS01000239.1.
DR   AlphaFoldDB; J1H6M3; -.
DR   PATRIC; fig|1125717.3.peg.1486; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000004578; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:EJF40943.1};
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          38..184
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          216..330
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          333..453
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          495..551
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   558 AA;  58858 MW;  8B157F140E12BADE CRC64;
     MHERAGTPAL PEDLINVDDV ISAYYDVEPD PANVDQRVVF GTSGHRGSSL DGKFNEAHIV
     AITAAIVEYR ASQGVNGPLF IGRDTHALSE PAWRTALEVL AGAGVDARID SRGSYTPTPA
     VSVAILGANG APGQLRTSGD GLADGIVVTP SHNPPRDGGF KYNPPHGGPA DTDATSVIAA
     RANELLESGQ WREVPRVVGS DLLHHPSITP FDYLDFYVGQ LDQIVDIEAI RAAGVRIGAD
     PLGGASIDYW AAIGERYGLD LTVVNPKVDP AWPFMTLDWD GKIRMDCSSP YAMASLRQAM
     TPDAEGNTPY DIATGNDADS DRHGIVTPDG LMNPNHFLAV AIEYLFSHRP GWGEDCAVGK
     TLVSSALIDR VVASLGRKLV EVPVGFKHFV PGLLSGTVGF GGEESAGASF LRKDGTVWST
     DKDGIIMALL ASEILAVTGK TPSQLHAEQV ERFGASAYAR IDAAASREEK AKLAALSADD
     VTATELAGDP ITAKLVRAPG NDAPIGGLKV ATEYAWFAAR PSGTEDVYKI YAESFKGAEH
     LAEVQEAAKK LVSDALGA
//
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