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Database: UniProt
Entry: Q8GKM1_HELPX
LinkDB: Q8GKM1_HELPX
Original site: Q8GKM1_HELPX 
ID   Q8GKM1_HELPX            Unreviewed;       197 AA.
AC   Q8GKM1;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:AAN74080.1};
DE   Flags: Fragment;
GN   Name=glmM {ECO:0000313|EMBL:AAN74080.1};
OS   Helicobacter pylori (Campylobacter pylori).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=210 {ECO:0000313|EMBL:AAN74080.1};
RN   [1] {ECO:0000313|EMBL:AAN74080.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PS207A {ECO:0000313|EMBL:AAN74080.1};
RX   PubMed=15516562; DOI=10.1128/JB.186.22.7508-7520.2004;
RA   Kalia A., Mukhopadhyay A.K., Dailide G., Ito Y., Azuma T., Wong B.C.,
RA   Berg D.E.;
RT   "Evolutionary dynamics of insertion sequences in Helicobacter pylori.";
RL   J. Bacteriol. 186:7508-7520(2004).
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; AY152905; AAN74080.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8GKM1; -.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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; 2.
DR   InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR   InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR42946:SF1; PHOSPHOGLUCOSAMINE MUTASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 2.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
FT   DOMAIN          2..108
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAN74080.1"
FT   NON_TER         197
FT                   /evidence="ECO:0000313|EMBL:AAN74080.1"
SQ   SEQUENCE   197 AA;  21736 MW;  4095FD87973708E9 CRC64;
     IAAGLYFKKH SQTNKILIGK DTRKSGYMVE NALVSALTSI GYNVIQIGPM PTPAIAFLTE
     DMRCDAGIMI SASHNPFEDN GIKFFNSYGY KLKEEEEKAI EEIFHDERLL HSSYKVGESV
     GSAKRIDDVI GRYIVHLKHS FPKHLNLQSL RIVLDTANGA AYKVAPVVFS ELGADVLVIN
     DEPNGCNINE QCGALHP
//
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