GLCDH_THETK
ID GLCDH_THETK Reviewed; 347 AA.
AC Q703W7; G4RN61;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Glucose 1-dehydrogenase;
DE Short=GDH;
DE Short=GlcDH;
DE EC=1.1.1.47;
GN Name=gdh; OrderedLocusNames=TTX_0329;
OS Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS / Kra 1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=768679;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1;
RX PubMed=15028704; DOI=10.1128/jb.186.7.2179-2194.2004;
RA Siebers B., Tjaden B., Michalke K., Doerr C., Ahmed H., Zaparty M.,
RA Gordon P., Sensen C.W., Zibat A., Klenk H.-P., Schuster S.C., Hensel R.;
RT "Reconstruction of the central carbohydrate metabolism of Thermoproteus
RT tenax using genomic and biochemical data.";
RL J. Bacteriol. 186:2179-2194(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1;
RX PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA Hensel R.;
RT "The complete genome sequence of Thermoproteus tenax: a physiologically
RT versatile member of the Crenarchaeota.";
RL PLoS ONE 6:E24222-E24222(2011).
RN [3]
RP PROTEIN SEQUENCE OF 1-29, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1;
RX PubMed=9238103; DOI=10.1007/s002030050477;
RA Siebers B., Wendisch V.F., Hensel R.;
RT "Carbohydrate metabolism in Thermoproteus tenax: in vivo utilization of the
RT non-phosphorylative Entner-Doudoroff pathway and characterization of its
RT first enzyme, glucose dehydrogenase.";
RL Arch. Microbiol. 168:120-127(1997).
CC -!- FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to
CC D-gluconate via gluconolactone. To a lesser extent, is also active with
CC xylose as substrate, but mannose, arabinose, galactose, fructose 6-
CC phosphate, glucose 6-phosphate, glycerinaldehyde 3-phosphate, ribose,
CC sorbitol, ethanol, erythritol, or lactose are not oxidized by the
CC enzyme. Can utilize both NAD(+) and NADP(+) as electron acceptor, with
CC a marked preference for NADP(+). Is involved in the degradation of
CC glucose through a non-phosphorylative variant of the Entner-Doudoroff
CC pathway. {ECO:0000269|PubMed:9238103}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH;
CC Xref=Rhea:RHEA:14293, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16217, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.47;
CC Evidence={ECO:0000269|PubMed:9238103};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH;
CC Xref=Rhea:RHEA:14405, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16217, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.47;
CC Evidence={ECO:0000269|PubMed:9238103};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 mM for glucose (in the presence of NADP(+), at 70 degrees
CC Celsius and pH 7) {ECO:0000269|PubMed:9238103};
CC KM=8 mM for xylose (in the presence of NADP(+), at 70 degrees Celsius
CC and pH 7) {ECO:0000269|PubMed:9238103};
CC KM=0.7 mM for NADP(+) (at 70 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:9238103};
CC KM=86 mM for NAD(+) (at 70 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:9238103};
CC Vmax=40 umol/min/mg enzyme for the oxidation of D-glucose by NADP(+)
CC (at 70 degrees Celsius and pH 7) {ECO:0000269|PubMed:9238103};
CC Vmax=150 umol/min/mg enzyme for the oxidation of D-glucose by NAD(+)
CC (at 70 degrees Celsius and pH 7) {ECO:0000269|PubMed:9238103};
CC Vmax=60 umol/min/mg enzyme for the oxidation of D-xylose by NADP(+)
CC (at 70 degrees Celsius and pH 7) {ECO:0000269|PubMed:9238103};
CC Temperature dependence:
CC Highly thermostable with a half-life of inactivation of 10 minutes at
CC 103 degrees Celsius. {ECO:0000269|PubMed:9238103};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9238103}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Glucose 1-dehydrogenase subfamily. {ECO:0000305}.
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DR EMBL; AJ621346; CAF18527.1; -; Genomic_DNA.
DR EMBL; FN869859; CCC81005.1; -; Genomic_DNA.
DR RefSeq; WP_014126262.1; NC_016070.1.
DR AlphaFoldDB; Q703W7; -.
DR SMR; Q703W7; -.
DR STRING; 768679.TTX_0329; -.
DR EnsemblBacteria; CCC81005; CCC81005; TTX_0329.
DR GeneID; 11263340; -.
DR KEGG; ttn:TTX_0329; -.
DR PATRIC; fig|768679.9.peg.347; -.
DR eggNOG; arCOG01459; Archaea.
DR HOGENOM; CLU_026673_1_0_2; -.
DR OMA; MCRNGRY; -.
DR OrthoDB; 43162at2157; -.
DR Proteomes; UP000002654; Chromosome.
DR GO; GO:0047934; F:glucose 1-dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0047935; F:glucose 1-dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0047936; F:glucose 1-dehydrogenase [NAD(P)] activity; IDA:UniProtKB.
DR GO; GO:0005536; F:glucose binding; IDA:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR GO; GO:0070401; F:NADP+ binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0033222; F:xylose binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019595; P:non-phosphorylated glucose catabolic process; IDA:UniProtKB.
DR HAMAP; MF_02127; Glucose_DH; 1.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR026583; Glc_1-DH_arc.
DR InterPro; IPR031640; Glu_dehyd_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF16912; Glu_dehyd_C; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Metal-binding; NAD;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..347
FT /note="Glucose 1-dehydrogenase"
FT /id="PRO_0000414843"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 178..181
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 260..262
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 289..291
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 347 AA; 37072 MW; C292E175C4ECA071 CRC64;
MRAVTVTPGV PESLRLREVP EPKPGPGQVL LKPLLVGVCG TDKEIIEGRY GKAPEGSDYL
ILGHEALAEV AALGKGVDNV SEGDLVVPTV RRPLDCQLPV DYCPPGKYLE HGIWGLHGHA
AELSITDAAY LVKVPKELRD IAVLTEPLSV VEKGVELGVE SYKARLGSPP KTALVLGAGP
VGLLASMVLR LMGVSITAVA TRPHDSLKAR LVEELGGRYI DAVHERLEGE FDLVIEATGA
PSLAVQGLER LAPGGVEVLL GVYPPTGELK GLGSLLTDAV LKNKLVVGSV NAGLRHFERA
LAHLKEANDS LNGFPKRLIT KVVPLERYQE AYVWTHDDIK VVLQVQT
