ID R4W7U6_9EURY Unreviewed; 362 AA.
AC R4W7U6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Glucose 1-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02127};
DE Short=GDH {ECO:0000256|HAMAP-Rule:MF_02127};
DE Short=GlcDH {ECO:0000256|HAMAP-Rule:MF_02127};
DE EC=1.1.1.47 {ECO:0000256|HAMAP-Rule:MF_02127};
GN Name=gdh {ECO:0000256|HAMAP-Rule:MF_02127};
GN ORFNames=L593_00670 {ECO:0000313|EMBL:AGN00089.1};
OS Salinarchaeum sp. Harcht-Bsk1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Natronoarchaeaceae; Salinarchaeum.
OX NCBI_TaxID=1333523 {ECO:0000313|EMBL:AGN00089.1, ECO:0000313|Proteomes:UP000014072};
RN [1] {ECO:0000313|EMBL:AGN00089.1, ECO:0000313|Proteomes:UP000014072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Harcht-Bsk1 {ECO:0000313|EMBL:AGN00089.1};
RX PubMed=23868130;
RA Dominova I.N., Sorokin D.Y., Kublanov I.V., Patrushev M.V.,
RA Toshchakov S.V.;
RT "Complete Genome Sequence of Salinarchaeum sp. Strain HArcht-Bsk1T,
RT Isolated from Hypersaline Lake Baskunchak, Russia.";
RL Genome Announc. 1:E00505-13(2013).
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_02127};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Glucose 1-dehydrogenase subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_02127}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02127}.
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DR EMBL; CP005962; AGN00089.1; -; Genomic_DNA.
DR RefSeq; WP_020444983.1; NC_021313.1.
DR AlphaFoldDB; R4W7U6; -.
DR STRING; 1333523.L593_00670; -.
DR GeneID; 16180631; -.
DR KEGG; sali:L593_00670; -.
DR PATRIC; fig|1333523.5.peg.136; -.
DR eggNOG; arCOG01459; Archaea.
DR HOGENOM; CLU_026673_1_0_2; -.
DR OrthoDB; 41394at2157; -.
DR Proteomes; UP000014072; 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 CDD; cd08230; glucose_DH; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_02127; Glucose_DH; 1.
DR InterPro; IPR013154; ADH-like_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 PANTHER; PTHR43189:SF2; GLUCOSE 1-DEHYDROGENASE; 1.
DR PANTHER; PTHR43189; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE PROTEIN C1198.01-RELATED; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF16912; Glu_dehyd_C; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_02127}; Metal-binding {ECO:0000256|HAMAP-Rule:MF_02127};
KW NAD {ECO:0000256|HAMAP-Rule:MF_02127};
KW NADP {ECO:0000256|HAMAP-Rule:MF_02127};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02127};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02127}; Reference proteome {ECO:0000313|Proteomes:UP000014072};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02127}.
FT DOMAIN 26..145
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 150..359
FT /note="Glucose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16912"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 188..191
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 212..213
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 277..279
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 306..308
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
SQ SEQUENCE 362 AA; 39339 MW; 5BC9F0C51E8A17AA CRC64;
MRAIAVGRGE TDPTVVEIDE PEPAEGEALI RTLRVGIDGT DHEVIGSNHG GYPEGEDFQV
LGHEAIGVVE DPNGTDLEAG QLVVPTVRRP PGGDAFGSGA EPNEYFERNE PDMAPAGEYV
ERGIAGAHGY MAEYFTSEPR YLVPVPDEFA EIGFLVEPIS NSEKAFDLAE ASRSTFEWDP
ESAIVLGNGP LGLLTLAMLD DRGFDRHYCL GRRDRPDPTI DIIEELGATY VDSRETPVDE
LPGAEEPMDF VYEATGYAPH AFQTIDALAP NGVGVLLGIP GEWEFEIDGG ALHRDFVLEN
KALLGSVNSH VPHFEAAVET LAGMPEWFTD AIVTHVFDPE DVDEAFETGD DRIKVVVEFD
DL
//
