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   03-AUG-2022, entry version 134.
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; Proteobacteria; 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   PRIDE; P31450; -.
DR   EnsemblBacteria; AYC08251; AYC08251; b3681.
DR   PATRIC; fig|83333.103.peg.4616; -.
DR   EchoBASE; EB1659; -.
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   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; PTHR32092; 1.
DR   Pfam; PF02056; Glyco_hydro_4; 1.
DR   PRINTS; PR00732; GLHYDRLASE4.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 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