位置:首页 > 蛋白库 > PGM_NEIMB
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024