位置:首页 > 蛋白库 > GLCDH_METS5
GLCDH_METS5
ID   GLCDH_METS5             Reviewed;         358 AA.
AC   A4YGA7;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Msed_1301;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000682; ABP95459.1; -; Genomic_DNA.
DR   RefSeq; WP_012021246.1; NC_009440.1.
DR   AlphaFoldDB; A4YGA7; -.
DR   SMR; A4YGA7; -.
DR   STRING; 399549.Msed_1301; -.
DR   EnsemblBacteria; ABP95459; ABP95459; Msed_1301.
DR   GeneID; 5104552; -.
DR   GeneID; 59457592; -.
DR   KEGG; mse:Msed_1301; -.
DR   eggNOG; arCOG01459; Archaea.
DR   HOGENOM; CLU_026673_1_0_2; -.
DR   OMA; NWGHEDI; -.
DR   Proteomes; UP000000242; 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..358
FT                   /note="Glucose 1-dehydrogenase"
FT                   /id="PRO_0000414835"
FT   BINDING         38
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         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   BINDING         65
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         66
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         92
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         95
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         98
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         106
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         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   BINDING         149
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         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   BINDING         187..190
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   BINDING         209..211
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   BINDING         268..270
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   BINDING         296..298
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
FT   BINDING         342
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02127"
SQ   SEQUENCE   358 AA;  39611 MW;  AF162547645D9F6C CRC64;
     MKAIIVRPPN EGVEVKDITL RESTDGKIVV RTRLSGLCGT DRGLVTGRLT FARPPPGYDF
     LILGHETLGE VVKGNGEFSP GDLVVPVVRR GCGSCLNCML GRQDFCETGR FTEIGIRGAH
     GTMREEFLED PKYLVRVPRE LGDEGVLLEP LSNVVKALTE MEYLQRRSWW RCDDSTYSCR
     TAVVLGSGPI GLLFSMALRS MGFRVIVANR RPPSQVESEI TRDIGATFLN TSEHEDLEPD
     LIVDTSGHPS AVVPLLPRIR KNGAVILFGT TGLERYELTA EEITMLVENN ILIFGSVNAS
     KADFQAGVNL LVEWKARYPG VLQRMITKRV SVEEAPQVLK EKVPGEIKTV IDWTARES
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024