ID   A0A2W1Y9Y5_9MICO        Unreviewed;       540 AA.
AC   A0A2W1Y9Y5;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:PZF48081.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:PZF48081.1};
GN   ORFNames=DEI94_09040 {ECO:0000313|EMBL:PZF48081.1};
OS   Curtobacterium sp. MCBD17_040.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Curtobacterium.
OX   NCBI_TaxID=2175674 {ECO:0000313|EMBL:PZF48081.1};
RN   [1] {ECO:0000313|EMBL:PZF48081.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCBD17_040 {ECO:0000313|EMBL:PZF48081.1};
RA   Chase A.B., Gomez-Lunar Z., Lopez A.E., Li J., Allison S.D., Martiny A.C.,
RA   Martiny J.B.H.;
RT   "Emergence of Soil Bacterial Ecotypes Along a Climate Gradient.";
RL   Submitted (JUN-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:PZF48081.1}.
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DR   EMBL; QKTL01000009; PZF48081.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2W1Y9Y5; -.
DR   OrthoDB; 9806956at2; -.
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; 2.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:PZF48081.1};
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          39..178
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          203..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..533
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   540 AA;  57745 MW;  6320DD89A2CA11DD CRC64;
     MNDRAGTPAT AEDLVDLQEL VDAYYSRVPD ASNPEQMVVF GTSGHRGSSL DTAFNDAHIA
     AITQAIVEYR AQQGTTGPLF IGRDTHALSG PAERTALEVL AANGVTVLAD KDNGYVPTPA
     LSHAIIRYNR EGHDDTADGI VITPSHNPPR DGGFKYNPPH GGPADSDATK WIADRANAII
     AGGLVDVQRQ EQASPGRYDF LDTYVHDLAD IIDIAAIKRA GVRIGADPLG GASLPYWNRI
     RDHYGLDLTV VNPDVDPTWS FMTLDWDGKI RMDPSSPSAM ASVLAHKDEF DVLTGNDADS
     DRHGIVTPDG GLMNPNHYLA VAIEYLYSHR PHWRQDAAIG KTLVSSSIID RVAESLGRTL
     WEVPVGFKWF VPGLIDGSVG FGGEESAGAS FLRMDGTAWT TDKDGIILAL LASEIIAVTG
     KTPSQLYREL TERFGDPVYQ RVDAAATKAQ KAALGKLDGD AIQADTLAGD PIVAKLSKAP
     GNGAAVGGVK VVTDRAWFAA RPSGTEDVYK IYAESFVGQE HLEQVQREAK EIVDAALGGA
//