(data stored in ACNUC10043 zone)

SWISSPROT: GLCDH_METPS

ID   GLCDH_METPS             Reviewed;         358 AA.
AC   D1YUK8;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 52.
DE   RecName: Full=Glucose 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02127};
DE            Short=GDH {ECO:0000255|HAMAP-Rule:MF_02127};
DE            Short=GlcDH {ECO:0000255|HAMAP-Rule:MF_02127};
DE            EC=1.1.1.47 {ECO:0000255|HAMAP-Rule:MF_02127};
GN   Name=gdh {ECO:0000255|HAMAP-Rule:MF_02127}; OrderedLocusNames=MCP_0058;
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE;
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(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}.
DR   EMBL; AP011532; BAI60130.1; -; Genomic_DNA.
DR   SMR; D1YUK8; -.
DR   STRING; 304371.MCP_0058; -.
DR   PRIDE; D1YUK8; -.
DR   EnsemblBacteria; BAI60130; BAI60130; MCP_0058.
DR   KEGG; mpd:MCP_0058; -.
DR   eggNOG; arCOG01459; Archaea.
DR   eggNOG; COG1063; LUCA.
DR   HOGENOM; HOG000022008; -.
DR   KO; K22969; -.
DR   OMA; MCRNGRY; -.
DR   Proteomes; UP000001882; Chromosome.
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; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR026583; Glc_1-DH.
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.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YUK8.
DR   SWISS-2DPAGE; D1YUK8.
KW   Carbohydrate metabolism; Metal-binding; NAD; NADP; Nucleotide-binding;
KW   Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN           1..358
FT                   /note="Glucose 1-dehydrogenase"
FT                   /id="PRO_0000414836"
FT   NP_BIND         183..186
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   METAL           39
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   METAL           64
FT                   /note="Zinc; via tele nitrogen; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   METAL           65
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   METAL           152
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   BINDING         41
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   BINDING         116
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   BINDING         152
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
SQ   SEQUENCE   358 AA;  39443 MW;  D38A683189A0E516 CRC64;
     MKAVVCTPGQ KDSVRVIDME RPRCGPGEVL VRVHSIGVDG TDEEINEGLY GEAPEGCDFL
     VIGHEAVGIV EESGAGVRCT RPGDVVVATV RRPCPERCLN CRNHQPDFCL TGDYLERGIK
     GLHGFMAEYY TESMDYVIQL PRELLDTGSL LEPLSVVEKG IRESLRVQQR MLWEPRRALV
     LGAGPLGLLA TFILRDMGLD VYTLATRERT SPKARVAEVS GARYIDVGEE PLDTLPEKHG
     PFDIIVEATG YSPYAFRAME LVNRNGVVCL AGLSPKKKDH ALCTDCINMS MVLDNKAALG
     TVSASRRDFE KGVDRMLSIR NKWPGLLESL FTKKESLDSA PRALRRTKED IKAVVVAT
//

If you have problems or comments...

PBIL Back to PBIL home page