ID A0A177QSH8_9PROT Unreviewed; 457 AA.
AC A0A177QSH8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:OAI50518.1};
GN ORFNames=AYO46_09915 {ECO:0000313|EMBL:OAI50518.1};
OS Betaproteobacteria bacterium SCGC AG-212-J23.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1799662 {ECO:0000313|EMBL:OAI50518.1, ECO:0000313|Proteomes:UP000077532};
RN [1] {ECO:0000313|Proteomes:UP000077532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC AG-212-J23 {ECO:0000313|Proteomes:UP000077532};
RA Choi J., Stepanauskas R., Howe A.;
RL Submitted (FEB-2016) 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}.
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:OAI50518.1}.
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DR EMBL; LSTF01000092; OAI50518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177QSH8; -.
DR Proteomes; UP000077532; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000077532}.
FT DOMAIN 6..137
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 152..249
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 255..356
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 382..446
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 457 AA; 49341 MW; F5C1CCB8B923FC97 CRC64;
MTVPAEIFRA YDIRGIVGKT LTPAIVRDIG RALGSVGKER GAATFAIGRD GRLSGPEFAK
ALAEGLNAVG ADVIDIGMAP TPVAYFAAHH LGCGSCVAIT GSHNPPDYNG LKIVVGGSTL
YGDEIQDLRK RIESGKFATG QGKRSEANVL QAYVDRITSD VKLARKMRIA VDCGNGVAGM
LAPKLYRALG CEVEELYCEV DGRFPNHHPD PSVPKNLQEL ISTVKNSSCE LGIAFDGDGD
RLGLVTKDGE IIFADRQLML LAKDVLSRNP GAQIIYDVKS TRLLAPWIEK HGGRPLIWKT
GHSLIKAKLR ETGALLAGEM SGHTFFKERW YGFDDALYGG ARLLEILSKE KDANPVLKSL
PNAPSTPELH WGLSEGEPHA LVAKLQASKP FPGAERVVTI DGVRVEYADG FGLARASNTT
PVIVLRFEAD SNIALERIKR DFRNALQPLK PDAPLPY
//
