ID F2L7W7_BURGS Unreviewed; 464 AA.
AC F2L7W7;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:AEA59496.1};
GN OrderedLocusNames=bgla_1g08080 {ECO:0000313|EMBL:AEA59496.1};
OS Burkholderia gladioli (strain BSR3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA59496.1, ECO:0000313|Proteomes:UP000008316};
RN [1] {ECO:0000313|EMBL:AEA59496.1, ECO:0000313|Proteomes:UP000008316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSR3 {ECO:0000313|EMBL:AEA59496.1,
RC ECO:0000313|Proteomes:UP000008316};
RX PubMed=21478339; DOI=10.1128/JB.00420-11;
RA Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., Choi I.Y.,
RA Moon J.S., Kim J., Hwang I.;
RT "Complete genome sequence of Burkholderia gladioli BSR3.";
RL J. Bacteriol. 193:3149-3149(2011).
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}.
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DR EMBL; CP002599; AEA59496.1; -; Genomic_DNA.
DR RefSeq; WP_013696851.1; NC_015381.1.
DR AlphaFoldDB; F2L7W7; -.
DR STRING; 999541.bgla_1g08080; -.
DR GeneID; 66456695; -.
DR KEGG; bgd:bgla_1g08080; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_9_1_4; -.
DR Proteomes; UP000008316; Chromosome 1.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03089; PMM_PGM; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 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 PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 5..143
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 159..256
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 261..365
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 375..453
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 464 AA; 50241 MW; 613CFB8938EC9731 CRC64;
MISQSIFKAY DIRGVIGKTL DASVARSIGQ AFGSEVRAQG GDAVVVARDG RLSGPELIAA
LADGLRAAGV DVVDVGMVPT PVGYFAASVP LPLASGERRV DSCIVVTGSH NPPDYNGFKM
VLRGAAIYGE QIQALYRRIV AQDYAEGSGS YQQHDVADAY LQRIVGDIKL ARPLKIVVDT
GNGVAGELAP RLFKALGCEL VELFTEIDGN FPNHHPDPAH PENLQDVIRA LKETDAEIGF
AFDGDGDRLG VVTKDGQIIY PDRQMMLFAE EVLSRNPGAQ IIYDVKCTRN LAPWIREKGG
EPLMWKTGHS LVKAKLRETG APLAGEMSGH VFFKDRWYGF DDGLYTGARL LEILARVADP
SALLNGLPNA ESTPELQLKL EEGENVALIE KLRQDAKFEG ADEVITIDGL RVEYPDGFGL
ARSSNTTPVV VLRFEANSAE ALERIKGEFR RALTAAKPDA KLPF
//
