PGM_NEIMB
ID PGM_NEIMB Reviewed; 460 AA.
AC P40391;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Phosphoglucomutase;
DE Short=PGM;
DE EC=5.4.2.2;
DE AltName: Full=Glucose phosphomutase;
GN Name=pgm; OrderedLocusNames=NMB0790;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NMB / Serogroup B;
RX PubMed=8157643; DOI=10.1016/s0021-9258(19)78105-8;
RA Zhou D., Stephens D.S., Gibson B.W., Engstrom J.J., McAllister C.F.,
RA Lee F.K.N., Apicella M.A.;
RT "Lipooligosaccharide biosynthesis in pathogenic Neisseria. Cloning,
RT identification, and characterization of the phosphoglucomutase gene.";
RL J. Biol. Chem. 269:11162-11169(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
CC -!- FUNCTION: This enzyme participates in both the breakdown and synthesis
CC of glucose.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2;
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; U02490; AAA20589.1; -; Genomic_DNA.
DR EMBL; AE002098; AAF41203.1; -; Genomic_DNA.
DR PIR; B53614; B53614.
DR PIR; C81159; C81159.
DR RefSeq; NP_273832.1; NC_003112.2.
DR RefSeq; WP_010980847.1; NC_003112.2.
DR AlphaFoldDB; P40391; -.
DR SMR; P40391; -.
DR STRING; 122586.NMB0790; -.
DR PaxDb; P40391; -.
DR EnsemblBacteria; AAF41203; AAF41203; NMB0790.
DR KEGG; nme:NMB0790; -.
DR PATRIC; fig|122586.8.peg.1002; -.
DR HOGENOM; CLU_016950_9_1_4; -.
DR OMA; KCSQVMY; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
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 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 PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Isomerase;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..460
FT /note="Phosphoglucomutase"
FT /id="PRO_0000147812"
FT ACT_SITE 103
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 103..104
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 243..244
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 322..324
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT CONFLICT 140
FT /note="A -> R (in Ref. 1; AAA20589)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="K -> E (in Ref. 1; AAA20589)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="V -> A (in Ref. 1; AAA20589)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="K -> E (in Ref. 1; AAA20589)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="L -> V (in Ref. 1; AAA20589)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="S -> T (in Ref. 1; AAA20589)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 49476 MW; BAA17FD8C6A4A298 CRC64;
MASIARDIFK AYDIRGIVGK TLTDEAAYLI GKAIAAKAAE KGITRIALGR DGRLSGPELM
EHIRRGFTDS GINVLNVGMV ATPMLYFAAV NECGGSGVMI TGSHNPPDYN GFKMMLGGDT
LAGEAIQELL SIIEKDGFAA AGKQGSVTEK DISGEYLKHI TGHIRLKRPM NIAIDAGNGV
GGAFAGKLYK GLGNKVTELF CDVDGTFPNH HPDPSKPKNL QDLIAALKNG DAEIGLAFDG
DADRLGVVTK DGNIIYPDRQ LMLFAQDVLN RNPGAKVIFD VKSTRLLAPW IKEHGGKAIM
EKTGHSFIKS AMKETGAPVA GEMSGHIFFK ERWFGFDDGL YAGARLLEIL SASDNPSEVL
NNLPQSISTP ELNIALPEGS NGHQVIDELA AKAEFEGATE IITIDGLRVE FPDGFGLMRA
SNTTPILVLR FEADTQEAIE RIQNQFKAVI ESNPNLIWPL
