ID A0A1I7FIU5_9BURK Unreviewed; 543 AA.
AC A0A1I7FIU5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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};
GN ORFNames=SAMN05216552_100268 {ECO:0000313|EMBL:SFU36074.1};
OS Pseudoduganella namucuonensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Pseudoduganella.
OX NCBI_TaxID=1035707 {ECO:0000313|EMBL:SFU36074.1, ECO:0000313|Proteomes:UP000199391};
RN [1] {ECO:0000313|Proteomes:UP000199391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11014 {ECO:0000313|Proteomes:UP000199391};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FPBO01000002; SFU36074.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7FIU5; -.
DR STRING; 1035707.SAMN05216552_100268; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000199391; Unassembled WGS sequence.
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|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000199391}.
FT DOMAIN 14..153
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 184..286
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 295..407
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 543 AA; 57843 MW; DE6D6585ED4F2990 CRC64;
MAIQTVATHP IPGQRPGTSG LRKKVEVFRQ PHYLENFVQS VFDTLGDCAG KTLVVGGDGR
YHNRAAIQTI LRMAAAHGYA QVLVGQGGIL STPAVSCVIR KRQASGGIIL SASHNPGGPD
GDFGIKYNIA AGGPAPEGVT EAIYRRSESI AQYRLSDAPE VDIDRLGVTQ VEQTRVEVID
SVADYAELMR GLFDFDAIRK LFAGGFTMRF DGMHAVSGPY AKTIIEGMLG APEGTVINCV
PLEDFGGLHP DPNPVNAAQL IELMGGADAP DFGAASDGDG DRNMIVGRDF DVTPSDSLAI
LAANATLAPG YRQGLKGIAR SMPTSRAADR VAEALGIPCH ETPTGWKFFG TLLDAGMATL
CGEESYGTGS DHIREKDGVW AVLFWLNLLA ATGKPVERIV GEHWERFGRN YYSRHDYEAI
DTAAANLLMA DLRVKLPALA GQVLNGHTVD FADDFSYTDP VDGSTVTGQG IRIVMTDGSR
IVYRLSGTGT EGATLRVYIE LYEPDPSQHH RPTQQALASL IAAADSVANI AMQTGRASPS
VIT
//
