GLCD2_PICTO
ID GLCD2_PICTO Reviewed; 359 AA.
AC Q6L047;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Glucose/galactose 1-dehydrogenase;
DE EC=1.1.1.360;
DE AltName: Full=Galactose 1-dehydrogenase [NADP(+)];
DE AltName: Full=Glucose 1-dehydrogenase 2;
DE Short=GDH 2;
DE Short=GlcDH 2;
GN Name=gdh2; Synonyms=gdhA; OrderedLocusNames=PTO1070;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15691337; DOI=10.1111/j.1742-4658.2004.04539.x;
RA Angelov A., Futterer O., Valerius O., Braus G.H., Liebl W.;
RT "Properties of the recombinant glucose/galactose dehydrogenase from the
RT extreme thermoacidophile, Picrophilus torridus.";
RL FEBS J. 272:1054-1062(2005).
CC -!- FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to
CC D-gluconate via gluconolactone. Is also significantly active with D-
CC galactose as substrate, but not with D-xylose, L-arabinose, D-ribose,
CC D-mannose, D-allose, D-glucosamine, 2-deoxy-D-glucose, or glucose-6-
CC phosphate. Can utilize both NAD(+) and NADP(+) as electron acceptor,
CC with a marked preference for NADP(+) (20-fold higher activity).
CC Physiologically, may be involved in the degradation of both glucose and
CC galactose through a non-phosphorylative variant of the Entner-Doudoroff
CC pathway. {ECO:0000269|PubMed:15691337}.
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;
CC EC=1.1.1.360; Evidence={ECO:0000269|PubMed:15691337};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose + NADP(+) = D-galactono-1,5-lactone + H(+) +
CC NADPH; Xref=Rhea:RHEA:18625, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15945, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.360; Evidence={ECO:0000269|PubMed:15691337};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Zn(2+) is of critical importance for the stability of the enzyme.
CC {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 mM for D-glucose {ECO:0000269|PubMed:15691337};
CC KM=4.5 mM for D-galactose {ECO:0000269|PubMed:15691337};
CC KM=1.12 mM for NADP(+) {ECO:0000269|PubMed:15691337};
CC pH dependence:
CC Optimum pH is 6.5 for the oxidation of D-glucose by NADP(+). At the
CC physiological pH of 4.6 found in the cytoplasm of Picrophilus cells,
CC the enzyme shows merely 10% of its maximal activity.
CC {ECO:0000269|PubMed:15691337};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius for the oxidation of D-
CC glucose by NADP(+). {ECO:0000269|PubMed:15691337};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15691337}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Glucose 1-dehydrogenase subfamily. {ECO:0000305}.
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DR EMBL; AE017261; AAT43655.1; -; Genomic_DNA.
DR RefSeq; WP_011177871.1; NC_005877.1.
DR AlphaFoldDB; Q6L047; -.
DR SMR; Q6L047; -.
DR STRING; 263820.PTO1070; -.
DR EnsemblBacteria; AAT43655; AAT43655; PTO1070.
DR GeneID; 2844646; -.
DR KEGG; pto:PTO1070; -.
DR eggNOG; arCOG01459; Archaea.
DR HOGENOM; CLU_026673_1_0_2; -.
DR OMA; MCRNGRY; -.
DR OrthoDB; 43162at2157; -.
DR BRENDA; 1.1.1.360; 7518.
DR Proteomes; UP000000438; Chromosome.
DR GO; GO:0047910; F:galactose 1-dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0005534; F:galactose binding; IDA:UniProtKB.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0070401; F:NADP+ binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0033498; P:galactose catabolic process via D-galactonate; IDA:UniProtKB.
DR GO; GO:0019595; P:non-phosphorylated glucose catabolic process; IDA:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; 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; Metal-binding; NAD; NADP; Nucleotide-binding;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..359
FT /note="Glucose/galactose 1-dehydrogenase"
FT /id="PRO_0000414837"
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 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213..215
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 273..275
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 302..304
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 359 AA; 40463 MW; 7CAC2E1480E4B7C7 CRC64;
MVRAIITNAP NGGVKIENVN INEPEHYEVK LRPVYTGLCG TDRGEVLGNL SFAYNEPGYN
YLVLGHEAIC QVIEASENPY KIKPGDYVVP VVRRPGKCVN CRIGREDDCS DGDKHEAGIT
GLHGFMRDYF YDEAKNLVKI NDKNMVKVAV LTEPTKNVMK AFEVFDTVSK RSIFQGDDST
NLTKNCLIIG TGSEAFLYAF MAREYRFNVF MTNRHPVGEE KLSIISRINA DFYDYTREDP
LKGIDLLIDT SGDPGTIFRF VRKMNYNGVV ILFGTNGRAP ATSIDGEDID YIIERNISLV
GSVDGAKRHY LRAVEYLEKW NYSEGSVINR LITGVFEPED VSIFTKKPEN EIKSVIKWS
