GLCD1_PICTO
ID GLCD1_PICTO Reviewed; 352 AA.
AC Q6L1C8;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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}; OrderedLocusNames=PTO0639;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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 Note=Binds 2 Zn(2+) ions per subunit. One of the zinc atoms is
CC essential for catalytic activity while the other has a structural
CC function. {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; AE017261; AAT43224.1; -; Genomic_DNA.
DR RefSeq; WP_011177440.1; NC_005877.1.
DR AlphaFoldDB; Q6L1C8; -.
DR SMR; Q6L1C8; -.
DR STRING; 263820.PTO0639; -.
DR EnsemblBacteria; AAT43224; AAT43224; PTO0639.
DR GeneID; 2844968; -.
DR KEGG; pto:PTO0639; -.
DR PATRIC; fig|263820.9.peg.671; -.
DR eggNOG; arCOG01459; Archaea.
DR HOGENOM; CLU_026673_1_0_2; -.
DR OMA; NWGHEDI; -.
DR OrthoDB; 43162at2157; -.
DR Proteomes; UP000000438; 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; Reference proteome; Zinc.
FT CHAIN 1..352
FT /note="Glucose 1-dehydrogenase 1"
FT /id="PRO_0000414838"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 148
FT /ligand="substrate"
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 204..206
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 264..266
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 292..294
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT BINDING 341
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
SQ SEQUENCE 352 AA; 39284 MW; 057A8271B7178898 CRC64;
MKAIIVHPPG AGVSIEDVNI NGNGPGIKIL ENGICGTDRE IVNGELSAAT SLNGFLVLGH
EALGILEEDT KNLRKGDLVM PINRRGCGRC LNCMLGRPDF CETGEQLEAG ISGMHGFMRE
YINDDERYLV KVPDVIRDIA IMAQPLADLE KSIEEMISIQ KRLHWPCIDG TYNCRKVLIT
GTGTIGILFA MLLKTYGFSV YISNKREPND IESKIFDELS VKYKNLSNKI DESFDAIIEA
SGSGTDVIER TLPLLKNNGF YGIFGFEKTG TLNLTSEFLQ GIVYKSINIT GLINGQKPHM
EMAMNHLIQW KKQFPKTTSM MITEKVSINN ERRLKEVLSK KRPGEIKIKI IW
