GLCD2_HALTV
ID GLCD2_HALTV Reviewed; 356 AA.
AC D2S1F7;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 56.
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=Htur_4392;
OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OG Plasmid pHTUR01.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=543526;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 / 4k;
RX PubMed=21304683; DOI=10.4056/sigs.681272;
RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL Stand. Genomic Sci. 2:107-116(2010).
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; CP001861; ADB63204.1; -; Genomic_DNA.
DR RefSeq; WP_012945448.1; NC_013744.1.
DR AlphaFoldDB; D2S1F7; -.
DR SMR; D2S1F7; -.
DR PRIDE; D2S1F7; -.
DR EnsemblBacteria; ADB63204; ADB63204; Htur_4392.
DR GeneID; 8745020; -.
DR KEGG; htu:Htur_4392; -.
DR HOGENOM; CLU_026673_1_0_2; -.
DR OrthoDB; 43162at2157; -.
DR Proteomes; UP000001903; Plasmid pHTUR01.
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; Plasmid; Reference proteome; Zinc.
FT CHAIN 1..356
FT /note="Glucose 1-dehydrogenase 2"
FT /id="PRO_0000414834"
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 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 114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 181..184
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 206..207
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 301..303
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
SQ SEQUENCE 356 AA; 37871 MW; E87CCCCCAD0494D0 CRC64;
MRAVALFPDE PELRVIEKPK PTPENGEALI RTVAVGIDGS DRRIAAGEIG GDVPDGEDHL
VIGHEAVGVV EEPNGTDLAR GDVVAPLVRR PVGDGSRFAA NGELDMAPPG SFHECGITGA
HGYMSEFFTA RPGYLVPIPE SRAAYGFFVE PASLVEKALD QTEAARSGFD WRPSSAFVLG
NGNLGLLALT RLETGDEFER TYCLGRRDRP DPTIDVIENV GGTYVDSREL SLDEFPAVHE
PVDFAFETTG HPAHAVEAVD ALAPNGVVTL QGIPGSSSTV EIDGGAFHTD LVVTNKAILG
VVNARRSHFR AAAEWLAETP ESVLDALVTG VYGPDEIDEA FADSAETIKT VVSFDR
