ID C1IPN3_9GAMM Unreviewed; 505 AA.
AC C1IPN3;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
DE Flags: Fragment;
GN Name=pgm {ECO:0000313|EMBL:ACG63441.1};
OS Francisella philomiragia.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=28110 {ECO:0000313|EMBL:ACG63441.1};
RN [1] {ECO:0000313|EMBL:ACG63441.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCUG 19701 {ECO:0000313|EMBL:ACG63441.1};
RX PubMed=19187160; DOI=10.1111/j.1365-2672.2008.04092.x;
RA Ottem K.F., Nylund A., Karlsbakk E., Friis-Moller A., Kamaishi T.;
RT "Elevation of Francisella philomiragia subsp. noatunensis Mikalsen et al.
RT (2007) to Francisella noatunensis comb. nov. [syn. Francisella piscicida
RT Ottem et al. (2008) syn. nov.] and characterization of Francisella
RT noatunensis subsp. orientalis subsp. nov., two important fish pathogens.";
RL J. Appl. Microbiol. 106:1231-1243(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
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}.
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DR EMBL; EU682976; ACG63441.1; -; Genomic_DNA.
DR AlphaFoldDB; C1IPN3; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03085; PGM1; 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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573:SF2; 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 PRINTS; PR00509; PGMPMM.
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 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 1..135
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 168..269
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 278..390
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACG63441.1"
FT NON_TER 505
FT /evidence="ECO:0000313|EMBL:ACG63441.1"
SQ SEQUENCE 505 AA; 55139 MW; 9FC4556589DD6CCD CRC64;
SGLRNKVTAF QQPGYLENFV QSIFNSLDDI QGKTLVVGGD GRYYNDVAVQ IIVRMAAANG
FGKIIVGQNG IFSTPAVSCV IRKYQAFGGI VLSASHNPGG PKGDFGIKYN VSNGGPAPEK
ITDRIFSETK KIDQYLISDA PKDSVNLNKI GTYKIENTTV EVINSVTDYA ELMQQIFDFD
KIRELFANGF KVRFDSMSAV SGPYAKYIFE TLLQAPAGTV VNAEPLEDFG GFHPDPNPVN
AEDLVKHMRS GKYDFGAASD GDADRNMIVG KQIDVSPSDS LAIMAANAHL IPAYSKGIKG
VARSMPTSTA VDRVAESLGL PCFETPTGWK FFGNLLDAQK ITLCGEESYG TGSDHIREKD
GVWAVLFWLN LVAATGKQID QLVEEHWQKF GRNFYSRHDY EAIDTVIANS IMSSLRDKLS
SLAGTQLNGE KVAKADDFSY TDPIDDSVSN HQGIRIIFED GSRIVFRLSG TGTQGATLRI
YLEKYESDSS KFNIPTQQAL ASLID
//
