ID S8FGK3_9BACT Unreviewed; 462 AA.
AC S8FGK3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:EPT34067.1};
DE EC=5.4.2.10 {ECO:0000313|EMBL:EPT34067.1};
GN Name=glmM {ECO:0000313|EMBL:EPT34067.1};
GN ORFNames=HMPREF9012_0996 {ECO:0000313|EMBL:EPT34067.1};
OS Bacteroidetes bacterium oral taxon 272 str. F0290.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=888054 {ECO:0000313|EMBL:EPT34067.1, ECO:0000313|Proteomes:UP000015345};
RN [1] {ECO:0000313|EMBL:EPT34067.1, ECO:0000313|Proteomes:UP000015345}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0290 {ECO:0000313|EMBL:EPT34067.1,
RC ECO:0000313|Proteomes:UP000015345};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (JUL-2013) 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:EPT34067.1}.
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DR EMBL; AUTU01000011; EPT34067.1; -; Genomic_DNA.
DR AlphaFoldDB; S8FGK3; -.
DR PATRIC; fig|888054.3.peg.756; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000015345; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR024086; GlmM_arc-type.
DR NCBIfam; TIGR03990; Arch_GlmM; 1.
DR PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:EPT34067.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000015345}.
FT DOMAIN 8..142
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 171..264
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 271..375
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 397..458
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 462 AA; 50728 MW; 552B59FA65204AA2 CRC64;
MTLIKSISGI RGTIGGQVGE SLNPLDIVKF TSAYATLMRK NTHMTTNKIV VGRDARISGE
MVKNVVCGTL MGMGFDVVNI GLATTPTTEL AVTMEEACGG IILTASHNPR QWNALKLLNE
KGEFLNREEG DEVLRIAEVE DFEFADVDHI GHYREDSTYD QKHIDRVLAL KLVDVAAIRK
ANFRVALDTV NSVGGIILPE LLERLGVKTV KTLYGEPTGD FRHNPEPLEK NLGDIMGLMT
KGGYDVAFVC DPDVDRLAII CEDGKMYGEE YTLVTVADYV LQHTPGNTVS NLSSTRALRD
VTRKYGGEYA AAAVGEVNVV TKMKETHAVI GGEGNGGVIY PECHYGRDAL VGIALFLSYL
SKKQMRVSEL RASYPSYFMA KNRIDLAPGT NVEAILSKVK ALYKQEEIDD TDGVKIDFPD
KWVHLRKSNT EPIIRIYSEA STVEAADEIG QEIMELVKSL VG
//
