PGMB_ECOLI
ID PGMB_ECOLI Reviewed; 219 AA.
AC P77366;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Beta-phosphoglucomutase;
DE Short=Beta-PGM;
DE EC=5.4.2.6 {ECO:0000269|PubMed:29684280};
GN Name=ycjU; Synonyms=pgmB; OrderedLocusNames=b1317, JW1310;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION AS A BETA-PHOSPHOGLUCOMUTASE, AND COFACTOR.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=16990279; DOI=10.1074/jbc.m605449200;
RA Kuznetsova E., Proudfoot M., Gonzalez C.F., Brown G., Omelchenko M.V.,
RA Borozan I., Carmel L., Wolf Y.I., Mori H., Savchenko A.V., Arrowsmith C.H.,
RA Koonin E.V., Edwards A.M., Yakunin A.F.;
RT "Genome-wide analysis of substrate specificities of the Escherichia coli
RT haloacid dehalogenase-like phosphatase family.";
RL J. Biol. Chem. 281:36149-36161(2006).
RN [5]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=DM4100;
RX PubMed=20128927; DOI=10.1186/1471-2180-10-35;
RA Han X., Dorsey-Oresto A., Malik M., Wang J.Y., Drlica K., Zhao X., Lu T.;
RT "Escherichia coli genes that reduce the lethal effects of stress.";
RL BMC Microbiol. 10:35-35(2010).
RN [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12 / MDS42;
RX PubMed=25848029; DOI=10.1073/pnas.1423570112;
RA Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L.,
RA Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D.,
RA Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D.,
RA Allen K.N., Farelli J.D.;
RT "Panoramic view of a superfamily of phosphatases through substrate
RT profiling.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113, and K12 / MG1655 / ATCC 47076;
RX PubMed=29684280; DOI=10.1021/acs.biochem.8b00392;
RA Mukherjee K., Narindoshvili T., Raushel F.M.;
RT "Discovery of a kojibiose phosphorylase in Escherichia coli K-12.";
RL Biochemistry 57:2857-2867(2018).
RN [8] {ECO:0007744|PDB:4G9B}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.
RA Vetting M.W., Toro R., Bhosle R., Al Obaidi N.F., Morisco L.L.,
RA Wasserman S.R., Sojitra S., Washington E., Scott Glenn A., Chowdhury S.,
RA Evans B., Hammonds J., Hillerich B., Love J., Seidel R.D., Imker H.J.,
RA Dunaway-Mariano D., Allen K.N., Gerlt J.A., Almo S.C.;
RT "Crystal structure of beta-phosphoglucomutase homolog from Escherichia
RT coli, target efi-501172, with bound mg, open lid.";
RL Submitted (JUL-2012) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the conversion of beta D-glucose 1-phosphate (G1P)
CC to D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-
CC (bis)phosphate (beta-G16P) as an intermediate (PubMed:16990279,
CC PubMed:29684280) (Probable). Phosphatase activity with the reaction
CC intermediate beta-G16P has been measured (PubMed:25848029). In vitro
CC interconverts beta D-glucose 1-phosphate, beta-D-allose 1-phosphate,
CC beta-D-galactose 1-phosphate and beta-D-mannose 1-phosphate to their
CC corresponding sugar 6-phosphate product. The beta-D-glucose 1-phosphate
CC substrate may be furnished by YcjT (AC P77154), the apparent upstream
CC enzyme in the putative biochemical pathway encoded in this locus (yjcM
CC to ycjW) (PubMed:29684280). It may play a key role in the regulation of
CC the flow of carbohydrate intermediates in glycolysis and the formation
CC of the sugar nucleotide UDP-glucose. {ECO:0000269|PubMed:16990279,
CC ECO:0000269|PubMed:25848029, ECO:0000269|PubMed:29684280,
CC ECO:0000305|PubMed:25848029}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucose 1-phosphate = beta-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:20113, ChEBI:CHEBI:57684, ChEBI:CHEBI:58247;
CC EC=5.4.2.6; Evidence={ECO:0000269|PubMed:29684280};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16990279, ECO:0000269|PubMed:29684280,
CC ECO:0000269|Ref.8};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000250|UniProtKB:P71447};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18.5 uM for beta-D-glucose 1-phosphate (using beta-D-glucose 1,6-
CC (bis)phosphate as an activator, at pH 8.0, 30 degrees Celsius)
CC {ECO:0000269|PubMed:29684280};
CC KM=1.19 mM for beta-D-glucose 6-phosphate (using beta-D-glucose 1,6-
CC (bis)phosphate as an activator, at pH 8.0, 30 degrees Celsius)
CC {ECO:0000269|PubMed:29684280};
CC KM=11 uM for beta-D-glucose 1,6-(bis)phosphate
CC {ECO:0000269|PubMed:25848029};
CC Note=kcat is 21 sec(-1) for conversion of G1P to G6P, kcat is 0.5
CC sec(-1) for conversion of G6P to G1P. {ECO:0000269|PubMed:29684280};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P71447}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:20128927}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P71447}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are only slightly more
CC susceptible to nalidixic acid, but are more sensitive to UV irradiation
CC than the wild-type (PubMed:20128927). No visible phenotype when grown
CC on glucose (PubMed:29684280). {ECO:0000269|PubMed:20128927,
CC ECO:0000269|PubMed:29684280}.
CC -!- MISCELLANEOUS: The catalysis proceeds via a phosphoenzyme formed by
CC reaction of an active-site nucleophile with the cofactor glucose 1,6-
CC diphosphate (G1,6-diP). The phosphorylated mutase binds either G1P or
CC G6P and transfers the phosphoryl group to the C(6)OH or C(1)OH,
CC respectively (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH 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; U00096; AAC74399.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14892.1; -; Genomic_DNA.
DR PIR; H64880; H64880.
DR RefSeq; NP_415833.1; NC_000913.3.
DR RefSeq; WP_000775794.1; NZ_SSZK01000012.1.
DR PDB; 4G9B; X-ray; 1.70 A; A=1-219.
DR PDBsum; 4G9B; -.
DR AlphaFoldDB; P77366; -.
DR SMR; P77366; -.
DR BioGRID; 4263195; 16.
DR IntAct; P77366; 1.
DR STRING; 511145.b1317; -.
DR PaxDb; P77366; -.
DR DNASU; 945891; -.
DR EnsemblBacteria; AAC74399; AAC74399; b1317.
DR EnsemblBacteria; BAA14892; BAA14892; BAA14892.
DR GeneID; 945891; -.
DR KEGG; ecj:JW1310; -.
DR KEGG; eco:b1317; -.
DR PATRIC; fig|1411691.4.peg.962; -.
DR EchoBASE; EB3677; -.
DR eggNOG; COG0637; Bacteria.
DR HOGENOM; CLU_045011_13_3_6; -.
DR InParanoid; P77366; -.
DR OMA; TQTAKVH; -.
DR PhylomeDB; P77366; -.
DR BioCyc; EcoCyc:G6655-MON; -.
DR BioCyc; MetaCyc:G6655-MON; -.
DR BRENDA; 5.4.2.6; 2026.
DR PRO; PR:P77366; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008801; F:beta-phosphoglucomutase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:EcoCyc.
DR GO; GO:0009294; P:DNA-mediated transformation; IMP:EcoCyc.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR CDD; cd02598; HAD_BPGM; 1.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR010976; B-phosphoglucomutase_hydrolase.
DR InterPro; IPR010972; Beta-phosphoglucomutase.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01990; bPGM; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR TIGRFAMs; TIGR02009; PGMB-YQAB-SF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Isomerase; Magnesium;
KW Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..219
FT /note="Beta-phosphoglucomutase"
FT /id="PRO_0000108052"
FT ACT_SITE 11
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 9..11
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:4G9B"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:4G9B"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 44..49
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 116..120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:4G9B"
FT SITE 116
FT /note="Important for catalytic activity and assists the
FT phosphoryl transfer reaction to Asp8 by balancing charge
FT and orienting the reacting groups"
FT /evidence="ECO:0000250"
FT SITE 147
FT /note="Important for catalytic activity and assists the
FT phosphoryl transfer reaction to Asp8 by balancing charge
FT and orienting the reacting groups"
FT /evidence="ECO:0000250"
FT MOD_RES 9
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000250"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:4G9B"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:4G9B"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:4G9B"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:4G9B"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:4G9B"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:4G9B"
FT HELIX 68..87
FT /evidence="ECO:0007829|PDB:4G9B"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4G9B"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:4G9B"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:4G9B"
FT HELIX 121..127
FT /evidence="ECO:0007829|PDB:4G9B"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:4G9B"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:4G9B"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:4G9B"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:4G9B"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:4G9B"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:4G9B"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:4G9B"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:4G9B"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:4G9B"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:4G9B"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:4G9B"
SQ SEQUENCE 219 AA; 23565 MW; 1FE8C3CAE4EAE717 CRC64;
MKLQGVIFDL DGVITDTAHL HFQAWQQIAA EIGISIDAQF NESLKGISRD ESLRRILQHG
GKEGDFNSQE RAQLAYRKNL LYVHSLRELT VNAVLPGIRS LLADLRAQQI SVGLASVSLN
APTILAALEL REFFTFCADA SQLKNSKPDP EIFLAACAGL GVPPQACIGI EDAQAGIDAI
NASGMRSVGI GAGLTGAQLL LPSTESLTWP RLSAFWQNV
