GLCDH_THEAC
ID GLCDH_THEAC Reviewed; 361 AA.
AC P13203;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Glucose 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02127};
DE Short=GDH {ECO:0000255|HAMAP-Rule:MF_02127};
DE Short=GlcDH {ECO:0000255|HAMAP-Rule:MF_02127};
DE EC=1.1.1.47 {ECO:0000255|HAMAP-Rule:MF_02127, ECO:0000269|PubMed:8436115};
DE AltName: Full=Galactose 1-dehydrogenase {ECO:0000305|PubMed:2803257};
DE EC=1.1.1.120 {ECO:0000269|PubMed:2803257};
DE EC=1.1.1.48 {ECO:0000269|PubMed:2803257};
GN Name=gdh {ECO:0000255|HAMAP-Rule:MF_02127}; OrderedLocusNames=Ta0897;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-18, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=8436115; DOI=10.1111/j.1432-1033.1993.tb17581.x;
RA Bright J.R., Byrom D., Danson M.J., Hough D.W., Towner P.;
RT "Cloning, sequencing and expression of the gene encoding glucose
RT dehydrogenase from the thermophilic archaeon Thermoplasma acidophilum.";
RL Eur. J. Biochem. 211:549-554(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [3]
RP PROTEIN SEQUENCE OF 2-25, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=2803257; DOI=10.1042/bj2610973;
RA Smith L.D., Budgen N., Bungard S.J., Danson M.J., Hough D.W.;
RT "Purification and characterization of glucose dehydrogenase from the
RT thermoacidophilic archaebacterium Thermoplasma acidophilum.";
RL Biochem. J. 261:973-977(1989).
CC -!- FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to
CC D-gluconate via gluconolactone. Is also significantly active with
CC galactose as substrate, but not with mannose or glucose 6-phosphate.
CC Can utilize both NAD(+) and NADP(+) as electron acceptor, with a marked
CC preference for NADP(+). Physiologically, may be involved in the
CC degradation of both glucose and galactose through a non-phosphorylative
CC variant of the Entner-Doudoroff pathway. {ECO:0000269|PubMed:2803257,
CC ECO:0000269|PubMed:8436115}.
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:2803257, ECO:0000269|PubMed:8436115};
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:2803257, ECO:0000269|PubMed:8436115};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose + NAD(+) = D-galactono-1,4-lactone + H(+) + NADH;
CC Xref=Rhea:RHEA:21296, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15895, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.48;
CC Evidence={ECO:0000269|PubMed:2803257};
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=1.1.1.120; Evidence={ECO:0000269|PubMed:2803257};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02127};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 mM for glucose {ECO:0000269|PubMed:2803257};
CC KM=0.113 mM for NADP(+) {ECO:0000269|PubMed:2803257};
CC Note=The KM value for NAD(+) is superior to 30 mM, it could not be
CC defined precisely as it was impossible to reach saturation of the
CC enzyme.;
CC Temperature dependence:
CC Thermostable. Retains full catalytic activity after 9 hours at 55
CC degrees Celsius, and at 75 degrees Celsius the half-life is
CC approximately 3 hours. {ECO:0000269|PubMed:2803257};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:2803257}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Glucose 1-dehydrogenase subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_02127}.
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DR EMBL; X59788; CAA42450.1; -; Genomic_DNA.
DR EMBL; AL445065; CAC12026.1; -; Genomic_DNA.
DR PIR; S29788; S29788.
DR RefSeq; WP_010901307.1; NC_002578.1.
DR AlphaFoldDB; P13203; -.
DR SMR; P13203; -.
DR STRING; 273075.Ta0897; -.
DR EnsemblBacteria; CAC12026; CAC12026; CAC12026.
DR GeneID; 1456433; -.
DR KEGG; tac:Ta0897; -.
DR eggNOG; arCOG01459; Archaea.
DR HOGENOM; CLU_026673_1_0_2; -.
DR OMA; MCRNGRY; -.
DR OrthoDB; 43162at2157; -.
DR BioCyc; MetaCyc:MON-4889; -.
DR BRENDA; 1.1.1.359; 6324.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0047910; F:galactose 1-dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0019151; F:galactose 1-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005534; F:galactose binding; IDA:UniProtKB.
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: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; Direct protein sequencing; Metal-binding; NAD;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2803257,
FT ECO:0000269|PubMed:8436115"
FT CHAIN 2..361
FT /note="Glucose 1-dehydrogenase"
FT /id="PRO_0000079889"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 216..218
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 275..277
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 304..306
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 349
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT VARIANT 2
FT /note="T -> S"
FT CONFLICT 338..361
FT /note="AKPSETNIFFQKPHGEIKTVIKWQ -> RSRPKPTYSSRNHTER (in
FT Ref. 1; CAA42450)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 40250 MW; 4852179202F15208 CRC64;
MTEQKAIVTD APKGGVKYTT IDMPEPEHYD AKLSPVYIGI CGTDRGEVAG ALSFTYNPEG
ENFLVLGHEA LLRVDDARDN GYIKKGDLVV PLVRRPGKCI NCRIGRQDNC SIGDPDKHEA
GITGLHGFMR DVIYDDIEYL VKVEDPELGR IAVLTEPLKN VMKAFEVFDV VSKRSIFFGD
DSTLIGKRMV IIGSGSEAFL YSFAGVDRGF DVTMVNRHDE TENKLKIMDE FGVKFANYLK
DMPEKIDLLV DTSGDPTTTF KFLRKVNNNG VVILFGTNGK APGYPVDGED IDYIVERNIT
IAGSVDAAKI HYVQALQSLS NWNRRHPDAM KSIITYEAKP SETNIFFQKP HGEIKTVIKW
Q
