ID X7Z3F7_MYCXE Unreviewed; 543 AA.
AC X7Z3F7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:EUA13874.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:EUA13874.1};
GN Name=pgm {ECO:0000313|EMBL:EUA13874.1};
GN ORFNames=I553_6993 {ECO:0000313|EMBL:EUA13874.1};
OS Mycobacterium xenopi 4042.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1299334 {ECO:0000313|EMBL:EUA13874.1};
RN [1] {ECO:0000313|EMBL:EUA13874.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4042 {ECO:0000313|EMBL:EUA13874.1};
RA Brown-Elliot B., Wallace R., Lenaerts A., Ordway D., DeGroote M.A.,
RA Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N.,
RA Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.;
RL Submitted (JAN-2014) 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:EUA13874.1}.
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DR EMBL; JAOB01000081; EUA13874.1; -; Genomic_DNA.
DR AlphaFoldDB; X7Z3F7; -.
DR PATRIC; fig|1299334.3.peg.8757; -.
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:EUA13874.1};
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 40..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 207..313
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 488..537
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 543 AA; 57545 MW; 432D89338E1AF24B CRC64;
MAHPRAGQPA QPEDLVDLPH LVTAYYVNEP DPDDVAQQVV FGTSGHRGSA LDGAFNEAHI
LAITQAIVEY RAAQGTTGPL FLGRDTHALS EPAWVSALEV LAANDVVAMI DSADRYTPTP
AISHAILNYN RDRAGGLADG IVVTPSHNPP ADGGFKYNPP SGGPADSDAT NTIAKRANEI
LRGGLADVKR VTLTRALRTA WRHDYLDAYV DDLPNVVDIR AIRDAGVRIG ADPLGGASVD
YWGVIAERHN LDLTVVNPLV DATFRFMTLD TDGKIRMDCS SADAMASLIA NRDLYHVATG
NDADADRHGI VTPDAGLVNP NHYLAVAIDY LYGHRPSWSA GLAVGKTVVS SSIIDRVVAG
MGRTLLEVPV GFKWFVEPLL AGAIGFGGEE SAGASFLRRD GSVWTTDKDG IIMALLAAEI
SAVTGATPSQ RYRELAAEYG EPSYARIDAP ADREQKARLA KLSADQVSAT ELAGEVITAK
LTAAPGNGAP LGGLKVTTAN AWFAARPSGT EDVYKIYAES FLGPQHLAEV QQAAQEVVDK
VIS
//
