ID   GLCD1_HALTV             Reviewed;         365 AA.
AC   D2RW30;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   28-JAN-2026, entry version 74.
DE   RecName: Full=Glucose 1-dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_02127};
DE            Short=GDH 1 {ECO:0000255|HAMAP-Rule:MF_02127};
DE            Short=GlcDH 1 {ECO:0000255|HAMAP-Rule:MF_02127};
DE            EC=1.1.1.47 {ECO:0000255|HAMAP-Rule:MF_02127};
GN   Name=gdh1 {ECO:0000255|HAMAP-Rule:MF_02127};
GN   OrderedLocusNames=Htur_2582;
OS   Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS   13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Halobacteria; Halobacteriales; 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 /
RC   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 + NADH + H(+);
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 + NADPH + H(+);
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; Evidence={ECO:0000255|HAMAP-
CC         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; CP001860; ADB61459.1; -; Genomic_DNA.
DR   RefSeq; WP_012943735.1; NC_013743.1.
DR   AlphaFoldDB; D2RW30; -.
DR   SMR; D2RW30; -.
DR   STRING; 543526.Htur_2582; -.
DR   GeneID; 8743195; -.
DR   KEGG; htu:Htur_2582; -.
DR   eggNOG; arCOG01459; Archaea.
DR   HOGENOM; CLU_026673_1_0_2; -.
DR   OrthoDB; 41394at2157; -.
DR   Proteomes; UP000001903; Chromosome.
DR   GO; GO:0005536; F:D-glucose binding; IEA:UniProtKB-UniRule.
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: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; Metal-binding; NAD; NADP; Nucleotide-binding;
KW   Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN           1..365
FT                   /note="Glucose 1-dehydrogenase 1"
FT                   /id="PRO_0000414833"
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         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
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         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   BINDING         182..185
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   BINDING         207..208
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   BINDING         272..274
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   365 AA;  39125 MW;  E9EF59BDFAE1B581 CRC64;
     MKAIAVEPGA GTPTLIDLPV PEPAPGEALV RTLRVGVDGT DDEVIAGAHG GVPDGDDRLV
     LGHEAVGVVE DANGTDLEEG QYVVPTVRRP PPGVETNVYF ERGEPDMAPE GEYVERGIVG
     AHGFMAEYFT SPADCLVPIS ADLAPVGFLV EPISITEKAI EHAAATRSAF DWRPESVFVL
     GNGSLGLLTA AMFRTTMGYD RVYCLGRRDR PHPSIDILDE LGVTYIDSRE TPVPEVPEVY
     EPMDLVYEAT GYAKHAFESI EALAPNGVAA LLGVPNDWSF EVDGGRLHRE MVLHNKAIVG
     SVNSNRDQFA SAVDTLAGLP SWVIEDVVSG VYGLEEYERA FSDPTDDATA DDDTTIKTAV
     EFSNI
//