ID A0A444PYE7_9MICO Unreviewed; 538 AA.
AC A0A444PYE7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Alpha-D-glucose phosphate-specific phosphoglucomutase {ECO:0000313|EMBL:RWZ52863.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:RWZ52863.1};
GN ORFNames=ELQ90_02680 {ECO:0000313|EMBL:RWZ52863.1};
OS Labedella phragmitis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Labedella.
OX NCBI_TaxID=2498849 {ECO:0000313|EMBL:RWZ52863.1, ECO:0000313|Proteomes:UP000288547};
RN [1] {ECO:0000313|EMBL:RWZ52863.1, ECO:0000313|Proteomes:UP000288547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11W25H-1 {ECO:0000313|EMBL:RWZ52863.1,
RC ECO:0000313|Proteomes:UP000288547};
RA Li F.;
RL Submitted (DEC-2018) 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:RWZ52863.1}.
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DR EMBL; RZNB01000001; RWZ52863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444PYE7; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000288547; 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; 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, ECO:0000313|EMBL:RWZ52863.1};
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..178
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 202..310
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 314..434
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 485..531
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 538 AA; 57397 MW; A4DD47DCFD5E69C4 CRC64;
MTDRAGTPAT ESDLVDLDAL HEAYYALKPD VSVPEQRVVF GTSGHRGSSL STSFNEDHIA
ATTQAIVEYR AAQGITGPLF IGADTHALSR PALTTALEVL VGNDVRVLTD QYDDFVPTPA
LSLAIITYNN AGNDDEADGI VVTPSHNPPA DGGFKYNPPH GGPADSDATS WIANRANELI
ADGLRDVKLA EPSAVETYDF RKAYVDDLAN IIDFDVIKQA GLHIGADPLG GASVHYWQAI
ADTYGLDLTV VNPDVDPTWR FMTLDWDGKI RMDPSSANAM ASVLEHRSEY DILTGNDADA
DRHGIVTPDG GLMNPNHYLA VAIEYLYANR PGWKDDAAIG KTLVSSSMID RVAESLGRRL
WEVPVGFKWF VPGLIDGSVG FGGEESAGAS FLRFDGTAWT TDKDGILLCL LASEITAKTG
KTPSQLYAEL TERFGSPAYE RVDAAASKEQ KAKLGKLDGD AITATELAGE PIIAKLSAAP
GNGAAVGGLK VVTENAWFAA RPSGTEDVYK IYAESFKGAE HLRQVQAEAK QIVDAAIA
//
