ID GLVG_ECOLI Reviewed; 212 AA.
AC P31450; A0A385XMQ3;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 28-JUN-2023, entry version 139.
DE RecName: Full=Putative inactive 6-phospho-alpha-glucosidase;
GN Name=glvG {ECO:0000303|PubMed:8019415}; OrderedLocusNames=b4556;
GN ORFNames=b3681;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
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 DISCUSSION OF SEQUENCE.
RX PubMed=8019415; DOI=10.1002/pro.5560030309;
RA Reizer J., Michotey V., Reizer A., Saier M.H. Jr.;
RT "Novel phosphotransferase system genes revealed by bacterial genome
RT analysis: unique, putative fructose- and glucoside-specific systems.";
RL Protein Sci. 3:440-450(1994).
RN [4]
RP LACK OF GLUCOSIDASE ACTIVITY, AND CROSS-REACTIVITY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9209025; DOI=10.1128/jb.179.13.4129-4137.1997;
RA Bouma C.L., Reizer J., Reizer A., Robrish S.A., Thompson J.;
RT "6-phospho-alpha-D-glucosidase from Fusobacterium mortiferum: cloning,
RT expression, and assignment to family 4 of the glycosylhydrolases.";
RL J. Bacteriol. 179:4129-4137(1997).
CC -!- MISCELLANEOUS: The GlvG polypeptide of 212 residues cross-reacts with
CC antibodies prepared against the full-length 6-phospho-alpha-D-
CC glucosidase (MalH) from Fusobacterium mortiferum. This operon may be
CC cryptic in wild-type K12 strains (Probable).
CC {ECO:0000305|PubMed:8019415}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. Lacks the C-terminal
CC half of the catalytic domain found in other members of this family.
CC This truncated polypeptide does not display phospho-alpha- or phospho-
CC beta-glucosidase activity (PubMed:9209025).
CC {ECO:0000305|PubMed:9209025}.
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DR EMBL; L10328; AAA62033.1; -; Genomic_DNA.
DR EMBL; U00096; AYC08251.1; -; Genomic_DNA.
DR PIR; B65170; B65170.
DR AlphaFoldDB; P31450; -.
DR SMR; P31450; -.
DR DIP; DIP-9813N; -.
DR IntAct; P31450; 7.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR EnsemblBacteria; AYC08251; AYC08251; b3681.
DR PATRIC; fig|83333.103.peg.4616; -.
DR EchoBASE; EB1659; -.
DR InParanoid; P31450; -.
DR PhylomeDB; P31450; -.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1820.10; AglA-like glucosidase; 1.
DR InterPro; IPR019802; GlycHydrolase_4_CS.
DR InterPro; IPR001088; Glyco_hydro_4.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR PANTHER; PTHR32092:SF14; MALTOSE-6'-PHOSPHATE GLUCOSIDASE; 1.
DR Pfam; PF02056; Glyco_hydro_4; 1.
DR PRINTS; PR00732; GLHYDRLASE4.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1.
PE 5: Uncertain;
KW Manganese; Metal-binding; NAD; Reference proteome.
FT CHAIN 1..212
FT /note="Putative inactive 6-phospho-alpha-glucosidase"
FT /id="PRO_0000169860"
FT BINDING 4..70
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
SQ SEQUENCE 212 AA; 23724 MW; 43FAD27B6D83FD1C CRC64;
MTKFSVVVAG GGSTFTPGIV LMLLANQDRF PLRALKFYDN DGARQEVIAE ACKVILKEKA
PDIAFSYTTD PEVAFSDVDF VMAHIRVGKY PMRELDEKIP LRHGVVGQET CGPGGIAYGM
RSIGGVLELV DYMEKYSPNA WMLNYSNPAA IVAEATRRLR PNAKILNICD MPIGIESRMA
QIVGLQDRKQ MRVRYYGLNH WWSAISRSFR KG
//
