位置:首页 > 蛋白库 > 6PGD_CAEEL
6PGD_CAEEL
ID   6PGD_CAEEL              Reviewed;         484 AA.
AC   Q17761; Q22772;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE            EC=1.1.1.44;
GN   ORFNames=T25B9.9;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate
CC       to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP
CC       to NADPH. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate
CC         + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58121, ChEBI:CHEBI:58349, ChEBI:CHEBI:58759; EC=1.1.1.44;
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       3/3.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC       {ECO:0000305}.
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; Z70311; CAA94380.1; -; Genomic_DNA.
DR   EMBL; Z70306; CAA94380.1; JOINED; Genomic_DNA.
DR   PIR; T19020; T19020.
DR   RefSeq; NP_501998.1; NM_069597.5.
DR   AlphaFoldDB; Q17761; -.
DR   SMR; Q17761; -.
DR   BioGRID; 43072; 20.
DR   STRING; 6239.T25B9.9; -.
DR   EPD; Q17761; -.
DR   PaxDb; Q17761; -.
DR   PeptideAtlas; Q17761; -.
DR   EnsemblMetazoa; T25B9.9.1; T25B9.9.1; WBGene00012015.
DR   GeneID; 177971; -.
DR   KEGG; cel:CELE_T25B9.9; -.
DR   UCSC; T25B9.9.1; c. elegans.
DR   CTD; 177971; -.
DR   WormBase; T25B9.9; CE06508; WBGene00012015; -.
DR   eggNOG; KOG2653; Eukaryota.
DR   GeneTree; ENSGT00390000009023; -.
DR   HOGENOM; CLU_024540_4_2_1; -.
DR   InParanoid; Q17761; -.
DR   OMA; VIMVKAG; -.
DR   OrthoDB; 847823at2759; -.
DR   PhylomeDB; Q17761; -.
DR   Reactome; R-CEL-71336; Pentose phosphate pathway.
DR   UniPathway; UPA00115; UER00410.
DR   PRO; PR:Q17761; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00012015; Expressed in adult organism and 4 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR   GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR   GO; GO:0046177; P:D-gluconate catabolic process; IBA:GO_Central.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006114; 6PGDH_C.
DR   InterPro; IPR006113; 6PGDH_Gnd/GntZ.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR006184; 6PGdom_BS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006183; Pgluconate_DH.
DR   PANTHER; PTHR11811; PTHR11811; 1.
DR   Pfam; PF00393; 6PGD; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000109; 6PGD; 1.
DR   PRINTS; PR00076; 6PGDHDRGNASE.
DR   SMART; SM01350; 6PGD; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00873; gnd; 1.
DR   PROSITE; PS00461; 6PGD; 1.
PE   3: Inferred from homology;
KW   Gluconate utilization; NADP; Oxidoreductase; Pentose shunt;
KW   Reference proteome.
FT   CHAIN           1..484
FT                   /note="6-phosphogluconate dehydrogenase, decarboxylating"
FT                   /id="PRO_0000090067"
FT   ACT_SITE        183
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        190
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         10..15
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         33..35
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         75..77
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         129..131
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         186..187
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         448
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         454
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   484 AA;  53196 MW;  D3CF6F1065F17535 CRC64;
     MAEADIAVIG LAVMGQNLIL NMNDHGFTVC AFNRTVKLVD DFLANEAKGT KIIGAHSIEE
     MCKKLKRPRR VMMLIKAGTP VDMMIDAIVP HLEEGDIIID GGNSEYTDSN RRSEQLAAKG
     IMFVGCGVSG GEEGARFGPS LMPGGNPKAW PHLKDIFQKI AAKSNGEPCC DWVGNAGSGH
     FVKMVHNGIE YGDMQLIAEA YHLLSKAVEL NHDQMAEVLD DWNKGELESF LIEITANILK
     YRDEQGEPIV PKIRDSAGQK GTGKWTCFAA LEYGLPVTLI GEAVFARCLS ALKDERVRAS
     KQLPRPQVSP DTVVQDKRVF IKQISKALYA SKIVSYAQGF MLLAEASKQF NWNLNFGAIA
     LMWRGGCIIR SRFLGDIEHA FQKNKQLSNL LLDDFFTKAI TEAQDSWRVV VCAAVRLGIP
     VPAFSSALAF YDGYTSEVVP ANLLQAQRDY FGAHTYELLA KPGTWVHTNW TGTGGRVTSN
     AYNA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025