GLMM_ECOL5
ID GLMM_ECOL5 Reviewed; 445 AA.
AC Q0TCT4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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}; OrderedLocusNames=ECP_3263;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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}.
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DR EMBL; CP000247; ABG71245.1; -; Genomic_DNA.
DR RefSeq; WP_000071137.1; NC_008253.1.
DR AlphaFoldDB; Q0TCT4; -.
DR SMR; Q0TCT4; -.
DR STRING; 362663.ECP_3263; -.
DR EnsemblBacteria; ABG71245; ABG71245; ECP_3263.
DR GeneID; 60901972; -.
DR GeneID; 67415990; -.
DR KEGG; ecp:ECP_3263; -.
DR HOGENOM; CLU_016950_7_0_6; -.
DR OMA; PHNPEPL; -.
DR Proteomes; UP000009182; 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; 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; 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 Pfam; PF00408; PGM_PMM_IV; 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_0000301312"
FT ACT_SITE 102
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 102
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 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
SQ SEQUENCE 445 AA; 47517 MW; ECC4102BC1A980EC CRC64;
MSNRKYFGTD GIRGRVGDAP ITPDFVLKLG WAAGKVLARH GSRKIIIGKD TRISGYMLES
ALEAGLAAAG LSALFTGPMP TPAVAYLTRT FRAEAGIVIS ASHNPFYDNG IKFFSIDGTK
LPDAVEEAIE AEMEKEISCV DSAELGKASR IVDAAGRYIE FCKATFPNEL SLSELKIVVD
CANGATYHIA PNVLRELGAN VIAIGCEPNG VNINAEVGAT DVRALQARVL AEKADLGIAF
DGDGDRVIMV DHEGNKVDGD QIMYIIAREG LRQGQLRGGA VGTLMSNMGL ELALKQLGIP
FARAKVGDRY VLEKMQEKGW RIGAENSGHV ILLDKTTTGD GIVAGLQVLA AMARNHMSLH
DLCSGMKMFP QILVNVRYTA GSGDPLEHES VKAVTAEVEA ALGSRGRVLL RKSGTEPLIR
VMVEGEDEAQ VTEFAHRIAD AVKAV