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Glucose 1-dehydrogenase (GDH) (GlcDH) (EC 1.1.1.47) (Aldose 1-dehydrogenase [NAD(P)( )]) (EC 1.1.1.359) (Galactose 1-dehydrogenase) (EC 1.1.1.120) (EC 1.1.1.48)

 GLCDH_SULSF             Reviewed;         366 AA.
O93715;
25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
25-OCT-2017, entry version 107.
RecName: Full=Glucose 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02127};
Short=GDH {ECO:0000255|HAMAP-Rule:MF_02127};
Short=GlcDH {ECO:0000255|HAMAP-Rule:MF_02127};
EC=1.1.1.47 {ECO:0000255|HAMAP-Rule:MF_02127, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812};
AltName: Full=Aldose 1-dehydrogenase [NAD(P)(+)] {ECO:0000305|PubMed:12824170};
EC=1.1.1.359 {ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812};
AltName: Full=Galactose 1-dehydrogenase {ECO:0000305|PubMed:12824170};
EC=1.1.1.120 {ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812};
EC=1.1.1.48 {ECO:0000269|PubMed:12824170};
Name=gdh {ECO:0000312|EMBL:CAA09918.1};
Sulfolobus solfataricus.
Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
Sulfolobus.
NCBI_TaxID=2287;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, FUNCTION,
CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, AND
SUBUNIT.
STRAIN=ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1;
PubMed=12824170; DOI=10.1074/jbc.M305818200;
Lamble H.J., Heyer N.I., Bull S.D., Hough D.W., Danson M.J.;
"Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus
revealed by studies on glucose dehydrogenase and 2-keto-3-
deoxygluconate aldolase.";
J. Biol. Chem. 278:34066-34072(2003).
[2]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND SUBUNIT.
STRAIN=DSM 5833 / MT-4;
PubMed=3827812; DOI=10.1042/bj2390517;
Giardina P., de Biasi M.G., de Rosa M., Gambacorta A., Buonocore V.;
"Glucose dehydrogenase from the thermoacidophilic archaebacterium
Sulfolobus solfataricus.";
Biochem. J. 239:517-522(1986).
[3]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF WILD-TYPE IN COMPLEXES WITH
NADP AND ZINC AND MUTANT ALA-41 IN COMPLEXES WITH BETA-D-GLUCOSE OR
D-XYLOSE; NADP AND ZINC, SUBUNIT, KINETIC PARAMETERS, COFACTOR,
CATALYTIC MECHANISM, AND MUTAGENESIS OF THR-41.
STRAIN=ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1;
PubMed=16556607; DOI=10.1074/jbc.M601334200;
Milburn C.C., Lamble H.J., Theodossis A., Bull S.D., Hough D.W.,
Danson M.J., Taylor G.L.;
"The structural basis of substrate promiscuity in glucose
dehydrogenase from the hyperthermophilic archaeon Sulfolobus
solfataricus.";
J. Biol. Chem. 281:14796-14804(2006).
-!- FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose
to D-gluconate via gluconolactone. Displays broad substrate
specificity since it is able to catalyze the oxidation of a number
of alternative aldose sugars, such as D-galactose, D-xylose and L-
arabinose, to the corresponding glyconate. Can utilize both NAD(+)
and NADP(+) as electron acceptor. Physiologically, seems to be
involved in the degradation of both glucose and galactose through
a non-phosphorylative variant of the Entner-Doudoroff pathway.
{ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812}.
-!- CATALYTIC ACTIVITY: D-glucose + NAD(P)(+) = D-glucono-1,5-lactone
+ NAD(P)H. {ECO:0000269|PubMed:12824170,
ECO:0000269|PubMed:3827812}.
-!- CATALYTIC ACTIVITY: D-galactose + NAD(+) = D-galactono-1,4-lactone
+ NADH. {ECO:0000269|PubMed:12824170}.
-!- CATALYTIC ACTIVITY: D-galactose + NADP(+) = D-galactono-1,5-
lactone + NADPH. {ECO:0000269|PubMed:12824170,
ECO:0000269|PubMed:3827812}.
-!- CATALYTIC ACTIVITY: An aldopyranose + NAD(P)(+) = an aldono-1,5-
lactone + NAD(P)H. {ECO:0000269|PubMed:12824170,
ECO:0000269|PubMed:3827812}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:16556607};
Note=Binds 2 Zn(2+) ions per subunit. One of the zinc atoms is
essential for catalytic activity while the other has a structural
function. {ECO:0000269|PubMed:16556607};
-!- ENZYME REGULATION: Inhibited by EDTA in vitro.
{ECO:0000269|PubMed:3827812}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=8.0 mM for D-glucose (in the presence of NAD(+), at 70
degrees Celsius and pH 8) {ECO:0000269|PubMed:3827812};
KM=1.50 mM for D-glucose (in the presence of NAD(+), at 70
degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12824170};
KM=0.44 mM for D-glucose (in the presence of NADP(+), at 70
degrees Celsius and pH 8) {ECO:0000269|PubMed:3827812};
KM=1.30 mM for D-glucose (in the presence of NADP(+), at 70
degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12824170};
KM=0.57 mM for D-galactose (in the presence of NAD(+), at 70
degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12824170};
KM=22 mM for D-galactose (in the presence of NADP(+), at 70
degrees Celsius and pH 8) {ECO:0000269|PubMed:3827812};
KM=0.44 mM for D-galactose (in the presence of NADP(+), at 70
degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12824170};
KM=0.25 mM for D-xylose (in the presence of NAD(+), at 70
degrees Celsius and pH 7.5) {ECO:0000269|PubMed:16556607};
KM=0.18 mM for D-xylose (in the presence of NADP(+), at 70
degrees Celsius and pH 7.5) {ECO:0000269|PubMed:16556607};
KM=1.2 mM for NAD(+) (at 70 degrees Celsius and pH 8)
{ECO:0000269|PubMed:3827812};
KM=0.03 mM for NADP(+) (at 70 degrees Celsius and pH 8)
{ECO:0000269|PubMed:3827812};
Vmax=110 umol/min/mg enzyme for the oxidation of D-glucose by
NAD(+) (at 70 degrees Celsius and pH 7.5)
{ECO:0000269|PubMed:12824170};
Vmax=70 umol/min/mg enzyme for the oxidation of D-glucose by
NADP(+) (at 70 degrees Celsius and pH 7.5)
{ECO:0000269|PubMed:12824170};
Vmax=90 umol/min/mg enzyme for the oxidation of D-galactose by
NAD(+) (at 70 degrees Celsius and pH 7.5)
{ECO:0000269|PubMed:12824170};
Vmax=55 umol/min/mg enzyme for the oxidation of D-galactose by
NADP(+) (at 70 degrees Celsius and pH 7.5)
{ECO:0000269|PubMed:12824170};
Vmax=90 umol/min/mg enzyme for the oxidation of D-xylose by
NAD(+) (at 70 degrees Celsius and pH 7.5)
{ECO:0000269|PubMed:16556607};
Vmax=65 umol/min/mg enzyme for the oxidation of D-xylose by
NADP(+) (at 70 degrees Celsius and pH 7.5)
{ECO:0000269|PubMed:16556607};
pH dependence:
Optimum pH is 9. {ECO:0000269|PubMed:3827812};
Temperature dependence:
Optimum temperature is 77 degrees Celsius. At 37 degrees
Celsius, shows about 20% activity as compared with the maximal
value. {ECO:0000269|PubMed:3827812};
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12824170,
ECO:0000269|PubMed:16556607, ECO:0000269|PubMed:3827812}.
-!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
family. Glucose 1-dehydrogenase subfamily. {ECO:0000255|HAMAP-
Rule:MF_02127}.
-----------------------------------------------------------------------
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EMBL; AJ012093; CAA09918.1; -; Genomic_DNA.
PIR; T44937; T44937.
RefSeq; WP_009992653.1; NZ_LT549890.1.
PDB; 2CD9; X-ray; 1.80 A; A/B=1-366.
PDB; 2CDA; X-ray; 2.28 A; A/B=1-366.
PDB; 2CDB; X-ray; 1.60 A; A/B/C/D=1-366.
PDB; 2CDC; X-ray; 1.50 A; A/B/C/D=1-366.
PDBsum; 2CD9; -.
PDBsum; 2CDA; -.
PDBsum; 2CDB; -.
PDBsum; 2CDC; -.
ProteinModelPortal; O93715; -.
SMR; O93715; -.
GeneID; 27429263; -.
eggNOG; arCOG01459; Archaea.
eggNOG; COG1063; LUCA.
BioCyc; MetaCyc:MONOMER-4842; -.
BRENDA; 1.1.1.359; 6163.
BRENDA; 1.1.1.47; 6163.
SABIO-RK; O93715; -.
EvolutionaryTrace; O93715; -.
GO; GO:0047910; F:galactose 1-dehydrogenase (NADP+) activity; IDA:UniProtKB.
GO; GO:0019151; F:galactose 1-dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0005534; F:galactose binding; IDA:UniProtKB.
GO; GO:0047936; F:glucose 1-dehydrogenase [NAD(P)] activity; IDA:UniProtKB.
GO; GO:0005536; F:glucose binding; IDA:UniProtKB.
GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
GO; GO:0070401; F:NADP+ binding; IDA:UniProtKB.
GO; GO:0033222; F:xylose binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0033498; P:galactose catabolic process via D-galactonate; IDA:UniProtKB.
GO; GO:0019595; P:non-phosphorylated glucose catabolic process; IDA:UniProtKB.
GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
HAMAP; MF_02127; Glucose_DH; 1.
InterPro; IPR013154; ADH_N.
InterPro; IPR026583; Glc_1-DH.
InterPro; IPR031640; Glu_dehyd_C.
InterPro; IPR011032; GroES-like.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF08240; ADH_N; 1.
Pfam; PF16912; Glu_dehyd_C; 1.
SUPFAM; SSF50129; SSF50129; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Direct protein sequencing;
Metal-binding; NAD; NADP; Nucleotide-binding; Oxidoreductase; Zinc.
CHAIN 1 366 Glucose 1-dehydrogenase.
/FTId=PRO_0000414839.
NP_BIND 189 192 NADP. {ECO:0000269|PubMed:16556607}.
NP_BIND 211 213 NADP. {ECO:0000269|PubMed:16556607}.
NP_BIND 277 279 NADP. {ECO:0000269|PubMed:16556607}.
NP_BIND 305 307 NADP. {ECO:0000269|PubMed:16556607}.
METAL 39 39 Zinc 1; catalytic.
{ECO:0000269|PubMed:16556607}.
METAL 66 66 Zinc 1; via tele nitrogen; catalytic.
{ECO:0000269|PubMed:16556607}.
METAL 67 67 Zinc 1; catalytic.
{ECO:0000269|PubMed:16556607}.
METAL 93 93 Zinc 2; structural.
{ECO:0000269|PubMed:16556607}.
METAL 96 96 Zinc 2; structural.
{ECO:0000269|PubMed:16556607}.
METAL 99 99 Zinc 2; structural.
{ECO:0000269|PubMed:16556607}.
METAL 107 107 Zinc 2; structural.
{ECO:0000269|PubMed:16556607}.
METAL 150 150 Zinc 1; catalytic.
{ECO:0000269|PubMed:16556607}.
BINDING 41 41 Substrate. {ECO:0000255|HAMAP-
Rule:MF_02127}.
BINDING 89 89 Substrate. {ECO:0000269|PubMed:16556607}.
BINDING 114 114 Substrate. {ECO:0000269|PubMed:16556607}.
BINDING 150 150 Substrate. {ECO:0000269|PubMed:16556607}.
BINDING 154 154 Substrate. {ECO:0000269|PubMed:16556607}.
BINDING 307 307 Substrate. {ECO:0000269|PubMed:16556607}.
BINDING 354 354 NADP. {ECO:0000269|PubMed:16556607}.
MUTAGEN 41 41 T->A: Large decrease in catalytic
activity and substrate affinity.
{ECO:0000269|PubMed:16556607}.
STRAND 2 6 {ECO:0000244|PDB:2CDC}.
STRAND 14 17 {ECO:0000244|PDB:2CDC}.
HELIX 20 22 {ECO:0000244|PDB:2CDC}.
STRAND 27 38 {ECO:0000244|PDB:2CDC}.
HELIX 40 46 {ECO:0000244|PDB:2CDC}.
STRAND 66 72 {ECO:0000244|PDB:2CDC}.
STRAND 84 87 {ECO:0000244|PDB:2CDC}.
STRAND 89 91 {ECO:0000244|PDB:2CDC}.
STRAND 94 96 {ECO:0000244|PDB:2CDC}.
HELIX 97 100 {ECO:0000244|PDB:2CDC}.
HELIX 104 106 {ECO:0000244|PDB:2CDC}.
STRAND 108 110 {ECO:0000244|PDB:2CDC}.
TURN 115 117 {ECO:0000244|PDB:2CDC}.
STRAND 118 120 {ECO:0000244|PDB:2CDC}.
STRAND 125 130 {ECO:0000244|PDB:2CDC}.
HELIX 132 134 {ECO:0000244|PDB:2CDC}.
STRAND 135 138 {ECO:0000244|PDB:2CDC}.
HELIX 140 142 {ECO:0000244|PDB:2CDC}.
TURN 143 145 {ECO:0000244|PDB:2CDC}.
HELIX 146 148 {ECO:0000244|PDB:2CDC}.
HELIX 149 165 {ECO:0000244|PDB:2CDC}.
HELIX 166 168 {ECO:0000244|PDB:2CDC}.
STRAND 177 179 {ECO:0000244|PDB:2CDC}.
STRAND 183 188 {ECO:0000244|PDB:2CDC}.
HELIX 190 203 {ECO:0000244|PDB:2CDC}.
STRAND 206 213 {ECO:0000244|PDB:2CDC}.
HELIX 217 226 {ECO:0000244|PDB:2CDC}.
STRAND 229 232 {ECO:0000244|PDB:2CDC}.
HELIX 238 244 {ECO:0000244|PDB:2CDC}.
STRAND 247 252 {ECO:0000244|PDB:2CDC}.
HELIX 259 264 {ECO:0000244|PDB:2CDC}.
HELIX 265 267 {ECO:0000244|PDB:2CDC}.
STRAND 268 276 {ECO:0000244|PDB:2CDC}.
STRAND 284 288 {ECO:0000244|PDB:2CDC}.
HELIX 289 297 {ECO:0000244|PDB:2CDC}.
STRAND 301 304 {ECO:0000244|PDB:2CDC}.
HELIX 310 326 {ECO:0000244|PDB:2CDC}.
HELIX 328 331 {ECO:0000244|PDB:2CDC}.
STRAND 334 340 {ECO:0000244|PDB:2CDC}.
HELIX 344 352 {ECO:0000244|PDB:2CDC}.
STRAND 360 364 {ECO:0000244|PDB:2CDC}.
SEQUENCE 366 AA; 40891 MW; 59D4AC33B447D3EB CRC64;
MKAIIVKPPN AGVQVKDVDE KKLDSYGKIK IRTIYNGICG TDREIVNGKL TLSTLPKGKD
FLVLGHEAIG VVEESYHGFS QGDLVMPVNR RGCGICRNCL VGRPDFCETG EFGEAGIHKM
DGFMREWWYD DPKYLVKIPK SIEDIGILAQ PLADIEKSIE EILEVQKRVP VWTCDDGTLN
CRKVLVVGTG PIGVLFTLLF RTYGLEVWMA NRREPTEVEQ TVIEETKTNY YNSSNGYDKL
KDSVGKFDVI IDATGADVNI LGNVIPLLGR NGVLGLFGFS TSGSVPLDYK TLQEIVHTNK
TIIGLVNGQK PHFQQAVVHL ASWKTLYPKA AKMLITKTVS INDEKELLKV LREKEHGEIK
IRILWE


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