YCJS_ECOLI
ID YCJS_ECOLI Reviewed; 351 AA.
AC P77503;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=D-glucoside 3-dehydrogenase {ECO:0000305|PubMed:30742415};
DE EC=1.1.1.- {ECO:0000269|PubMed:30742415};
GN Name=ycjS; OrderedLocusNames=b1315, JW1308;
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, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=30742415; DOI=10.1021/acs.biochem.8b01278;
RA Mukherjee K., Huddleston J.P., Narindoshvili T., Nemmara V.V.,
RA Raushel F.M.;
RT "Functional Characterization of the ycjQRS Gene Cluster from Escherichia
RT coli: A Novel Pathway for the Transformation of D-Gulosides to D-
RT Glucosides.";
RL Biochemistry 58:1388-1399(2019).
CC -!- FUNCTION: Catalyzes the NADH-dependent reduction of the oxo group at C3
CC of 3-dehydro-D-glucosides leading to D-glucosides. Probably functions
CC in a metabolic pathway that transforms D-gulosides to D-glucosides. Can
CC use 3-dehydro-D-glucose, methyl alpha-3-dehydro-D-glucoside and methyl
CC beta-3-dehydro-D-glucoside as substrates in vitro. However, the actual
CC specific physiological substrates for this metabolic pathway are
CC unknown. To a lesser extent, is also able to catalyze the reverse
CC reactions, i.e. the NAD(+)-dependent oxidation of the hydroxyl group at
CC C3 of D-glucosides leading to 3-dehydro-D-glucosides. Cannot act on
CC UDP-glucose, UDP-N-acetyl-D-glucosamine, D-glucosamine, N-acetyl-D-
CC glucosamine, or UDP-D-galactose. {ECO:0000269|PubMed:30742415}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-glucoside + NAD(+) = a 3-dehydro-D-glucoside + H(+) +
CC NADH; Xref=Rhea:RHEA:61724, ChEBI:CHEBI:15378, ChEBI:CHEBI:35436,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:145017;
CC Evidence={ECO:0000269|PubMed:30742415};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.2 mM for D-glucose (at pH 8.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:30742415};
CC KM=8.9 mM for D-glucose (at pH 9.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:30742415};
CC KM=5.6 mM for methyl alpha-D-glucoside (at pH 8.0 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:30742415};
CC KM=5.9 mM for methyl alpha-D-glucoside (at pH 9.0 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:30742415};
CC KM=2.0 mM for methyl beta-D-glucoside (at pH 8.0 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:30742415};
CC KM=1.6 mM for methyl beta-D-glucoside (at pH 9.0 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:30742415};
CC KM=2.1 mM for 1,5-anhydro-D-glucitol (at pH 8.0 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:30742415};
CC KM=3.9 mM for 1,5-anhydro-D-glucitol (at pH 9.0 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:30742415};
CC KM=0.5 mM for 3-dehydro-D-glucose (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:30742415};
CC KM=0.95 mM for methyl alpha-3-dehydro-D-glucoside (at pH 7.0 and 30
CC degrees Celsius) {ECO:0000269|PubMed:30742415};
CC KM=1.2 mM for methyl alpha-3-dehydro-D-glucoside (at pH 8.0 and 30
CC degrees Celsius) {ECO:0000269|PubMed:30742415};
CC KM=0.80 mM for methyl beta-3-dehydro-D-glucoside (at pH 7.0 and 30
CC degrees Celsius) {ECO:0000269|PubMed:30742415};
CC KM=0.92 mM for methyl beta-3-dehydro-D-glucoside (at pH 8.0 and 30
CC degrees Celsius) {ECO:0000269|PubMed:30742415};
CC Note=kcat is 0.65 sec(-1) for the NAD(+)-dependent oxidation of D-
CC glucose (at pH 8.0 and 30 degrees Celsius). kcat is 1.14 sec(-1) for
CC the NAD(+)-dependent oxidation of D-glucose (at pH 9.0 and 30 degrees
CC Celsius). kcat is 0.58 sec(-1) for the NAD(+)-dependent oxidation of
CC methyl alpha-D-glucoside (at pH 8.0 and 30 degrees Celsius). kcat is
CC 1.2 sec(-1) for the NAD(+)-dependent oxidation of methyl alpha-D-
CC glucoside (at pH 9.0 and 30 degrees Celsius). kcat is 0.4 sec(-1) for
CC the NAD(+)-dependent oxidation of methyl beta-D-glucoside (at pH 8.0
CC and 30 degrees Celsius). kcat is 0.3 sec(-1) for the NAD(+)-dependent
CC oxidation of methyl beta-D-glucoside (at pH 9.0 and 30 degrees
CC Celsius). kcat is 0.17 sec(-1) for the NAD(+)-dependent oxidation of
CC 1,5-anhydro-D-glucitol (at pH 8.0 and 30 degrees Celsius). kcat is
CC 0.4 sec(-1) for the NAD(+)-dependent oxidation of 1,5-anhydro-D-
CC glucitol (at pH 9.0 and 30 degrees Celsius). kcat is 4.7 sec(-1) for
CC the NADH-dependent reduction of 3-dehydro-D-glucose (at pH 6.5 and 30
CC degrees Celsius). kcat is 22 sec(-1) for the NADH-dependent reduction
CC of methyl alpha-3-dehydro-D-glucoside (at pH 7.0 and 30 degrees
CC Celsius). kcat is 18 sec(-1) for the NADH-dependent reduction of
CC methyl alpha-3-dehydro-D-glucoside (at pH 8.0 and 30 degrees
CC Celsius). kcat is 19 sec(-1) for the NADH-dependent reduction of
CC methyl beta-3-dehydro-D-glucoside (at pH 7.0 and 30 degrees Celsius).
CC kcat is 12.5 sec(-1) for the NADH-dependent reduction of methyl beta-
CC 3-dehydro-D-glucoside (at pH 8.0 and 30 degrees Celsius).
CC {ECO:0000269|PubMed:30742415};
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; U00096; AAC74397.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14890.1; -; Genomic_DNA.
DR PIR; F64880; F64880.
DR RefSeq; NP_415831.1; NC_000913.3.
DR RefSeq; WP_001395397.1; NZ_LN832404.1.
DR AlphaFoldDB; P77503; -.
DR SMR; P77503; -.
DR BioGRID; 4263193; 12.
DR IntAct; P77503; 1.
DR STRING; 511145.b1315; -.
DR PaxDb; P77503; -.
DR PRIDE; P77503; -.
DR EnsemblBacteria; AAC74397; AAC74397; b1315.
DR EnsemblBacteria; BAA14890; BAA14890; BAA14890.
DR GeneID; 948589; -.
DR KEGG; ecj:JW1308; -.
DR KEGG; eco:b1315; -.
DR PATRIC; fig|1411691.4.peg.964; -.
DR EchoBASE; EB3675; -.
DR eggNOG; COG0673; Bacteria.
DR HOGENOM; CLU_023194_1_4_6; -.
DR InParanoid; P77503; -.
DR OMA; PDKPWFY; -.
DR PhylomeDB; P77503; -.
DR BioCyc; EcoCyc:G6653-MON; -.
DR BioCyc; MetaCyc:G6653-MON; -.
DR PRO; PR:P77503; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:EcoCyc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..351
FT /note="D-glucoside 3-dehydrogenase"
FT /id="PRO_0000091779"
SQ SEQUENCE 351 AA; 38652 MW; 3410735BAA0A756D CRC64;
MKSAMTSSPL RVAIIGAGQV ADKVHASYYC TRNDLELVAV CDSRLSQAQA LAEKYGNASV
WDDPQAMLLA VKPDVVSVCS PNRFHYEHTL MALEAGCHVM CEKPPAMTPE QAREMCDTAR
KLGKVLAYDF HHRFALDTQQ LREQVTNGVL GEIYVTTARA LRRCGVPGWG VFTNKELQGG
GPLIDIGIHM LDAAMYVLGF PAVKSVNAHS FQKIGTQKSC GQFGEWDPAT YSVEDSLFGT
IEFHNGGILW LETSFALNIR EQSIMNVSFC GDKAGATLFP AHIYTDNNGE LMTLMQREIA
DDNRHLRSME AFINHVQGKP VMIADAEQGY IIQQLVAALY QSAETGTRVE L
