ID A0A1H9NNB8_9EURY Unreviewed; 353 AA.
AC A0A1H9NNB8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN04489841_3664 {ECO:0000313|EMBL:SER37247.1};
OS Natrinema salaciae.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1186196 {ECO:0000313|EMBL:SER37247.1, ECO:0000313|Proteomes:UP000199114};
RN [1] {ECO:0000313|Proteomes:UP000199114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25055 {ECO:0000313|Proteomes:UP000199114};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOFD01000005; SER37247.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9NNB8; -.
DR STRING; 1186196.SAMN04489841_3664; -.
DR OrthoDB; 41394at2157; -.
DR Proteomes; UP000199114; Unassembled WGS sequence.
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}; Zinc {ECO:0000256|HAMAP-Rule:MF_02127}.
FT DOMAIN 25..137
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 144..350
FT /note="Glucose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16912"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 180..183
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 203..204
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 268..270
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 297..299
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
SQ SEQUENCE 353 AA; 38403 MW; 428CF1C943A810CC CRC64;
MRAIAVERDG SQPRLIEKPR PEPDPGEALV RTLRVGIDGT DFEVIDGNHG GFPAESDHQV
LGHEAVGVVE ESNGTALEEG QLVVPTVRRP PDTANEYFRR GEPDMAPPDE CLERGIDGEH
GFMADYVTSP EAFLVPVPPA FEATGILIEP MSNTEKALEH AYASRSAFDW QRDAALVLGN
GPLGLLTLAR LQSEFERTYC LGRRDRPDPT IDLIERLGAT YVDSRETPVA AVPAEYEPMD
LVYEATGYAK HAFETIDALD QNGVGVLLGL PGDAAFDVAG GRLHRTLVQG NRALVGSVNS
HVEHFEAACE TLSALPDWFS DALVTDVFEP AAVDDAFSRS PDRIKTVIEF DSR
//
