ID M0MRR3_9EURY Unreviewed; 356 AA.
AC M0MRR3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=C449_01746 {ECO:0000313|EMBL:EMA47429.1};
OS Halococcus saccharolyticus DSM 5350.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=1227455 {ECO:0000313|EMBL:EMA47429.1, ECO:0000313|Proteomes:UP000011669};
RN [1] {ECO:0000313|EMBL:EMA47429.1, ECO:0000313|Proteomes:UP000011669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5350 {ECO:0000313|EMBL:EMA47429.1,
RC ECO:0000313|Proteomes:UP000011669};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMA47429.1}.
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DR EMBL; AOMD01000005; EMA47429.1; -; Genomic_DNA.
DR RefSeq; WP_006076151.1; NZ_AOMD01000005.1.
DR AlphaFoldDB; M0MRR3; -.
DR STRING; 1227455.C449_01746; -.
DR PATRIC; fig|1227455.4.peg.363; -.
DR InParanoid; M0MRR3; -.
DR OrthoDB; 41394at2157; -.
DR Proteomes; UP000011669; 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}; Reference proteome {ECO:0000313|Proteomes:UP000011669};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02127}.
FT DOMAIN 25..136
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 142..353
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 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 206..207
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 271..273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 300..302
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02127"
SQ SEQUENCE 356 AA; 38727 MW; E1A955346C012B51 CRC64;
MKAVVVQQGE TEPTVVEIDE PTPDPGEALL RTLRVGIDGT DHEVIEGNHG GFPDGDDYQV
LGHEAVAVVA DANGTDLNEG QLVVPTVRRP REEGNEYFER GEPDMAPDGQ YVERGIVGAH
GYMAEYFTSA PRYLVPVPDA FAESGFLVEP ISNTEKALEH AHATRSAFEW TPETGLVLGN
GPLGLLTLAM LEGGRTDFSR TYCLGRRDRP DPTIDIIERL GATYVDSRET PVSVISEVHE
PMDFVYEATG YAKHAFETVH ALRSNGVGAL LGIPEDWTFE IDGGALHREL VLQNKALFGS
VNSNVRHYEA AIDSLSAFPD WLVDDLVTGV HEPAAAPAAF ETNDETIKTV VEFDTV
//
