YCJQ_ECOLI
ID YCJQ_ECOLI Reviewed; 350 AA.
AC P76043; P78306;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=D-guloside 3-dehydrogenase {ECO:0000305|PubMed:30742415};
DE EC=1.1.1.- {ECO:0000269|PubMed:30742415};
GN Name=ycjQ; OrderedLocusNames=b1313, JW1306;
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], AND SEQUENCE REVISION TO
RP 234-243.
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, COFACTOR, SUBSTRATE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12;
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 NAD(+)-dependent oxidation of the hydroxyl
CC group at C3 of D-gulosides leading to 3-dehydro-D-gulosides. Probably
CC functions in a metabolic pathway that transforms D-gulosides to D-
CC glucosides. Is also able to catalyze the reverse reactions, i.e. the
CC NADH-dependent reduction of the oxo group at C3 of 3-dehydro-D-
CC gulosides leading to D-gulosides. In vitro, can oxidize D-gulose and
CC methyl beta-D-guloside, and reduce methyl alpha-3-dehydro-D-guloside
CC and methyl beta-3-dehydro-D-guloside. However, the actual specific
CC physiological substrates for this metabolic pathway are unknown.
CC {ECO:0000269|PubMed:30742415}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-guloside + NAD(+) = a 3-dehydro-D-guloside + H(+) + NADH;
CC Xref=Rhea:RHEA:61720, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:145014, ChEBI:CHEBI:145016;
CC Evidence={ECO:0000269|PubMed:30742415};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:30742415};
CC Note=Binds 1 Zn(2+) ions per subunit. {ECO:0000269|PubMed:30742415};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.1 mM for D-gulose (at pH 8.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:30742415};
CC KM=5.6 mM for D-gulose (at pH 9.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:30742415};
CC KM=12.5 mM for methyl beta-D-guloside (at pH 8.0 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:30742415};
CC KM=12.0 mM for methyl beta-D-guloside (at pH 9.0 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:30742415};
CC KM=9.4 mM for methyl alpha-3-dehydro-D-guloside (at pH 7.0 and 30
CC degrees Celsius) {ECO:0000269|PubMed:30742415};
CC KM=1.5 mM for methyl alpha-3-dehydro-D-guloside (at pH 8.0 and 30
CC degrees Celsius) {ECO:0000269|PubMed:30742415};
CC KM=2.3 mM for methyl beta-3-dehydro-D-guloside (at pH 7.0 and 30
CC degrees Celsius) {ECO:0000269|PubMed:30742415};
CC KM=7.0 mM for methyl beta-3-dehydro-D-guloside (at pH 8.0 and 30
CC degrees Celsius) {ECO:0000269|PubMed:30742415};
CC Note=kcat is 0.18 sec(-1) for the NAD(+)-dependent oxidation of D-
CC gulose (at pH 8.0 and 30 degrees Celsius). kcat is 0.23 sec(-1) for
CC the NAD(+)-dependent oxidation of D-gulose (at pH 9.0 and 30 degrees
CC Celsius). kcat is 0.35 sec(-1) for the NAD(+)-dependent oxidation of
CC methyl beta-D-guloside (at pH 8.0 and 30 degrees Celsius). kcat is
CC 1.2 sec(-1) for the NAD(+)-dependent oxidation of methyl beta-D-
CC guloside (at pH 9.0 and 30 degrees Celsius). kcat is 18.5 sec(-1) for
CC the NADH-dependent reduction of methyl alpha-3-dehydro-D-guloside (at
CC pH 7.0 and 30 degrees Celsius). kcat is 3.8 sec(-1) for the NADH-
CC dependent reduction of methyl alpha-3-dehydro-D-guloside (at pH 8.0
CC and 30 degrees Celsius). kcat is 7.0 sec(-1) for the NADH-dependent
CC reduction of methyl beta-3-dehydro-D-guloside (at pH 7.0 and 30
CC degrees Celsius). kcat is 9.7 sec(-1) for the NADH-dependent
CC reduction of methyl beta-3-dehydro-D-guloside (at pH 8.0 and 30
CC degrees Celsius). {ECO:0000269|PubMed:30742415};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; U00096; AAC74395.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14889.2; -; Genomic_DNA.
DR PIR; D64880; D64880.
DR RefSeq; NP_415829.1; NC_000913.3.
DR RefSeq; WP_000737347.1; NZ_SSZK01000012.1.
DR AlphaFoldDB; P76043; -.
DR SMR; P76043; -.
DR BioGRID; 4263191; 8.
DR DIP; DIP-11608N; -.
DR STRING; 511145.b1313; -.
DR PaxDb; P76043; -.
DR PRIDE; P76043; -.
DR EnsemblBacteria; AAC74395; AAC74395; b1313.
DR EnsemblBacteria; BAA14889; BAA14889; BAA14889.
DR GeneID; 66674859; -.
DR GeneID; 945971; -.
DR KEGG; ecj:JW1306; -.
DR KEGG; eco:b1313; -.
DR PATRIC; fig|1411691.4.peg.966; -.
DR EchoBASE; EB3673; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_9_0_6; -.
DR InParanoid; P76043; -.
DR OMA; QLGNMIV; -.
DR PhylomeDB; P76043; -.
DR BioCyc; EcoCyc:G6651-MON; -.
DR BioCyc; MetaCyc:G6651-MON; -.
DR PRO; PR:P76043; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Zinc.
FT CHAIN 1..350
FT /note="D-guloside 3-dehydrogenase"
FT /id="PRO_0000160890"
SQ SEQUENCE 350 AA; 38217 MW; A539943AF7A9ECB7 CRC64;
MKKLVATAPR VAALVEYEDR AILANEVKIR VRFGAPKHGT EVVDFRAASP FIDEDFNGEW
QMFTPRPADA PRGIEFGKFQ LGNMVVGDII ECGSDVTDYA VGDSVCGYGP LSETVIINAV
NNYKLRKMPQ GSSWKNAVCY DPAQFAMSGV RDANVRVGDF VVVVGLGAIG QIAIQLAKRA
GASVVIGVDP IAHRCDIARR HGADFCLNPI GTDVGKEIKT LTGKQGADVI IETSGYADAL
QSALRGLAYG GTISYVAFAK PFAEGFNLGR EAHFNNAKIV FSRACSEPNP DYPRWSRKRI
EETCWELLMN GYLNCEDLID PVVTFANSPE SYMQYVDQHP EQSIKMGVTF
