GLMM_HELPY
ID GLMM_HELPY Reviewed; 445 AA.
AC P25177; Q6V395;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Phosphoglucosamine mutase;
DE EC=5.4.2.10;
GN Name=glmM; Synonyms=ureC; OrderedLocusNames=HP_0075;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=85P;
RX PubMed=2001995; DOI=10.1128/jb.173.6.1920-1931.1991;
RA Labigne A., Cussac V., Courcoux P.;
RT "Shuttle cloning and nucleotide sequences of Helicobacter pylori genes
RT responsible for urease activity.";
RL J. Bacteriol. 173:1920-1931(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487;
RA She F.F., Zhang J., Ding H.;
RT "Gene cloning and expression of glmM in E. coli.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [4]
RP FUNCTION AS A PHOSPHOGLUCOSAMINE MUTASE.
RX PubMed=9171391; DOI=10.1128/jb.179.11.3488-3493.1997;
RA De Reuse H., Labigne A., Mengin-Lecreulx D.;
RT "The Helicobacter pylori ureC gene codes for a phosphoglucosamine mutase.";
RL J. Bacteriol. 179:3488-3493(1997).
RN [5]
RP PHOSPHORYLATION AT SER-99.
RX PubMed=10671448; DOI=10.1128/jb.182.5.1280-1285.2000;
RA Jolly L., Pompeo F., van Heijenoort J., Fassy F., Mengin-Lecreulx D.;
RT "Autophosphorylation of phosphoglucosamine mutase from Escherichia coli.";
RL J. Bacteriol. 182:1280-1285(2000).
CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC glucosamine-1-phosphate. {ECO:0000269|PubMed:9171391}.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PTM: Activated by phosphorylation. Can autophosphorylate in vitro using
CC ATP. {ECO:0000269|PubMed:10671448}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; M60398; AAA25018.1; -; Genomic_DNA.
DR EMBL; AY353251; AAQ57666.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07146.1; -; Genomic_DNA.
DR PIR; C38537; C38537.
DR RefSeq; NP_206875.1; NC_000915.1.
DR RefSeq; WP_000688400.1; NC_018939.1.
DR AlphaFoldDB; P25177; -.
DR SMR; P25177; -.
DR DIP; DIP-3160N; -.
DR MINT; P25177; -.
DR STRING; 85962.C694_00365; -.
DR iPTMnet; P25177; -.
DR PaxDb; P25177; -.
DR DNASU; 900169; -.
DR EnsemblBacteria; AAD07146; AAD07146; HP_0075.
DR KEGG; hpy:HP_0075; -.
DR PATRIC; fig|85962.47.peg.79; -.
DR eggNOG; COG1109; Bacteria.
DR OMA; PHNPEPL; -.
DR PhylomeDB; P25177; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IBA:GO_Central.
DR GO; GO:0004615; F:phosphomannomutase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Isomerase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..445
FT /note="Phosphoglucosamine mutase"
FT /id="PRO_0000147899"
FT ACT_SITE 99
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 99
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:10671448"
FT CONFLICT 124
FT /note="K -> R (in Ref. 1; AAA25018)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="E -> G (in Ref. 1; AAA25018)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="V -> I (in Ref. 2; AAQ57666)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="A -> V (in Ref. 2; AAQ57666)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="D -> E (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="S -> T (in Ref. 2; AAQ57666)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="V -> I (in Ref. 1; AAA25018)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="N -> S (in Ref. 2; AAQ57666)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="Q -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="Q -> L (in Ref. 1; AAA25018)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="A -> R (in Ref. 1; AAA25018)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="S -> N (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="S -> N (in Ref. 1; AAA25018)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="S -> L (in Ref. 2; AAQ57666)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 49086 MW; C0A52D904FFDAF20 CRC64;
MKIFGTDGVR GKAGVKLTPM FVMRLGIAAG LYFKKHSQTN KILIGKDTRK SGYMVENALV
SALTSIGYNV IQIGPMPTPA IAFLTEDMRC DAGIMISASH NPFEDNGIKF FNSYGYKLKE
EEEKAIEEIF HDEELLHSSY KVGESVGSAK RIDDVIGRYI AHLKHSFPKH LNLQSLRIVL
DTANGAAYKV APVVFSELGA DVLVINDEPN GCNINDQCGA LHPNQLSQEV KKYRADLGFA
FDGDADRLVV VDNLGNIVHG DKLLGVLGVY QKSKNALSSQ AVVATNMSNL ALKEYLKSQD
LELKHCAIGD KFVSECMQLN KANFGGEQSG HIIFSDYAKT GDGLVCALQV SALVLESKQV
SSVALNPFEL YPQSLVNLNV QKKPPLESLK GYSALLKELD KLEIRHLIRY SGTENKLRIL
LEAKDEKLLE SKMQELKEFF EGHLC
