GLCDH_HALSA
ID GLCDH_HALSA Reviewed; 356 AA.
AC Q9HS17;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
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};
GN Name=gdh {ECO:0000255|HAMAP-Rule:MF_02127}; Synonyms=gcd;
GN OrderedLocusNames=VNG_0446G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
CC -!- FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to
CC D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as
CC electron acceptor. Is involved in the degradation of glucose through a
CC modified Entner-Doudoroff pathway. {ECO:0000255|HAMAP-Rule:MF_02127}.
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:0000255|HAMAP-Rule:MF_02127};
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:0000255|HAMAP-Rule:MF_02127};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02127};
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; AE004437; AAG18991.1; -; Genomic_DNA.
DR PIR; C84203; C84203.
DR RefSeq; WP_010902286.1; NC_002607.1.
DR AlphaFoldDB; Q9HS17; -.
DR SMR; Q9HS17; -.
DR STRING; 64091.VNG_0446G; -.
DR PaxDb; Q9HS17; -.
DR EnsemblBacteria; AAG18991; AAG18991; VNG_0446G.
DR GeneID; 5952538; -.
DR GeneID; 62886104; -.
DR KEGG; hal:VNG_0446G; -.
DR PATRIC; fig|64091.14.peg.335; -.
DR HOGENOM; CLU_026673_1_0_2; -.
DR InParanoid; Q9HS17; -.
DR OMA; MCRNGRY; -.
DR OrthoDB; 43162at2157; -.
DR PhylomeDB; Q9HS17; -.
DR Proteomes; UP000000554; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0005536; F:glucose binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070401; F:NADP+ binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019595; P:non-phosphorylated glucose catabolic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Metal-binding; NAD; NADP; Nucleotide-binding;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..356
FT /note="Glucose 1-dehydrogenase"
FT /id="PRO_0000414831"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 180..183
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 205..206
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 270..272
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 300..302
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
SQ SEQUENCE 356 AA; 37510 MW; 115685DF68B84687 CRC64;
MDAIVVSKAD RTPRLVDRPR PDPTPGSVLV RTLRVGVDGT DHEVIAGTHG GFPEDADELV
LGHEAIGVVA DPTDTRFSAG QLVAPTVRRP RGDPTPQFDR GQPDMAAPGT YVERGIDGAD
GFMADYFTSP ADALVALPDS LAAHGFLTEP VSVAEKAIEL ALASRSAFDW RPDSALVLGN
GSLGLLTLAI LAARDDTETL YCLGRRSRPD PTIDIIERLG ATYIDSRTTP VADIPAAHQP
VDMVYEATGH AKHAFDAIDA LAPAGVAALL GVPAAGWTFE VPGSDLHRSL VLENKAVVGS
VNSNARHFRA AADTLAALPD WLCDAIVTGV HDTAAFADAF RDGETSIKTA VQFDTR
