GLCD2_VULM7
ID GLCD2_VULM7 Reviewed; 348 AA.
AC F0QYK7;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Glucose 1-dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_02127};
DE Short=GDH 2 {ECO:0000255|HAMAP-Rule:MF_02127};
DE Short=GlcDH 2 {ECO:0000255|HAMAP-Rule:MF_02127};
DE EC=1.1.1.47 {ECO:0000255|HAMAP-Rule:MF_02127};
GN Name=gdh2 {ECO:0000255|HAMAP-Rule:MF_02127}; OrderedLocusNames=VMUT_1235;
OS Vulcanisaeta moutnovskia (strain 768-28).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Vulcanisaeta.
OX NCBI_TaxID=985053;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=768-28;
RX PubMed=21398550; DOI=10.1128/jb.00237-11;
RA Gumerov V.M., Mardanov A.V., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of 'Vulcanisaeta moutnovskia' strain 768-28, a
RT novel member of the hyperthermophilic crenarchaeal genus vulcanisaeta.";
RL J. Bacteriol. 193:2355-2356(2011).
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 non-phosphorylative variant of the Entner-Doudoroff pathway.
CC {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADY01440.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP002529; ADY01440.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048056918.1; NC_015151.1.
DR AlphaFoldDB; F0QYK7; -.
DR SMR; F0QYK7; -.
DR STRING; 985053.VMUT_1235; -.
DR PRIDE; F0QYK7; -.
DR EnsemblBacteria; ADY01440; ADY01440; VMUT_1235.
DR GeneID; 10288887; -.
DR KEGG; vmo:VMUT_1235; -.
DR eggNOG; arCOG01459; Archaea.
DR HOGENOM; CLU_026673_1_0_2; -.
DR OrthoDB; 43162at2157; -.
DR Proteomes; UP000007485; 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; Zinc.
FT CHAIN 1..348
FT /note="Glucose 1-dehydrogenase 2"
FT /id="PRO_0000414846"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 41
FT /ligand="substrate"
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 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 178..181
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 260..262
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 289..291
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
SQ SEQUENCE 348 AA; 37449 MW; 1AEA94B9DA99A1D5 CRC64;
MKAVTVIPGI PESLRLMDVS KPNPNKGQVL LKPIRVGVCG TDKEIIEGRY GKAPEGNQYL
ILGHEAVAEV VEIGDGVDNA GVGDIVVPTV RRPLNCDLPV DFCPVGHYLE HGIWGLHGHA
AEYSVTDAKY LVKVPKEIVD VAVLTEPLSV VEKGIDMAMR IGQARFDWKP RTALVLGAGP
VGLLATMVLR LMGLSTVTTA TRPPDSLKAK LVKELGGTYV DSAVGQISGE FDIVVEATGS
PQVINEGLGH IAPNGVYVLL GVYPSGGSLN NLGELMTSVV LNNKVIVGSV NAGIKHFEMA
LEHLRRAKDE FNNWPAKLIT KRANLSNYQE AYTWTHDDIK TVLEIIQS
