GLMM_CAMJJ
ID GLMM_CAMJJ Reviewed; 445 AA.
AC A1VY80;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Phosphoglucosamine mutase {ECO:0000255|HAMAP-Rule:MF_01554};
DE EC=5.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01554};
GN Name=glmM {ECO:0000255|HAMAP-Rule:MF_01554};
GN OrderedLocusNames=CJJ81176_0383;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC glucosamine-1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01554}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate;
CC Xref=Rhea:RHEA:23424, ChEBI:CHEBI:58516, ChEBI:CHEBI:58725;
CC EC=5.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01554};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01554};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01554};
CC -!- PTM: Activated by phosphorylation. {ECO:0000255|HAMAP-Rule:MF_01554}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000255|HAMAP-Rule:MF_01554}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAQ73397.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000538; EAQ73397.2; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_002857318.1; NC_008787.1.
DR AlphaFoldDB; A1VY80; -.
DR SMR; A1VY80; -.
DR STRING; 354242.CJJ81176_0383; -.
DR EnsemblBacteria; EAQ73397; EAQ73397; CJJ81176_0383.
DR KEGG; cjj:CJJ81176_0383; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_0_7; -.
DR Proteomes; UP000000646; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05802; GlmM; 1.
DR HAMAP; MF_01554_B; GlmM_B; 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; IPR006352; GlmM_bact.
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; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR TIGRFAMs; TIGR01455; glmM; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase; Magnesium; Metal-binding; Phosphoprotein.
FT CHAIN 1..445
FT /note="Phosphoglucosamine mutase"
FT /id="PRO_0000305635"
FT ACT_SITE 99
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
SQ SEQUENCE 445 AA; 48769 MW; 982EB20165FB0692 CRC64;
MKLFGTDGVR GKAGEFLDSF LAMRLAMAAG IYFKDKSITN NILVGKDTRR SGYMIENAIV
SGLTSIGYNV IQIGPMPTPA IAFLTEDMRC DAGIMISASH NPYYDNGIKF FDAHGNKLSE
DIEKKIEEIY FDDKLIQASK VDMEKIGQAK RIDDVIGRYI VSIKNSFPKD LTLKSLRVVL
DVAHGAAYKV APTVFKELGA EVIVMSDKPN GLNINENCGA LHPANLAAEV KRLRADVGFA
FDGDADRLVV VDEKGEVANG DSLLGVLALY LKEQGKLQSS VVATIMSNGA LKEFLNKHGI
ELDTCNVGDK YVLEKLKANG GNFGGEQSGH IIFSDYAKTG DGLIAALQFS ALMLSKKKSA
SSILGQVKPY PQLLTNLKIA EKKDLDKIKG LKELKKDLEN KNINTLFRYS GTENLIRLLL
EAKDIKLLEK EMKNVVEFFK KALNG
