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G6PD_CERCA
ID   G6PD_CERCA              Reviewed;         526 AA.
AC   P41571;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE            Short=G6PD;
DE            EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413};
DE   AltName: Full=Zwischenferment;
GN   Name=ZW;
OS   Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC   Tephritidae; Ceratitis; Ceratitis.
OX   NCBI_TaxID=7213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8269100; DOI=10.1111/j.1365-2583.1993.tb00094.x;
RA   Scott M.J., Kriticou D., Robinson A.S.;
RT   "Isolation of cDNAs encoding 6-phosphogluconate dehydrogenase and glucose-
RT   6-phosphate dehydrogenase from the mediterranean fruit fly Ceratitis
RT   capitata: correlating genetic and physical maps of chromosome 5.";
RL   Insect Mol. Biol. 1:213-222(1993).
CC   -!- FUNCTION: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes
CC       the first and rate-limiting step of the oxidative branch within the
CC       pentose phosphate pathway/shunt, an alternative route to glycolysis for
CC       the dissimilation of carbohydrates and a major source of reducing power
CC       and metabolic intermediates for fatty acid and nucleic acid
CC       biosynthetic processes. {ECO:0000250|UniProtKB:P11413}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC         lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:61548; EC=1.1.1.49;
CC         Evidence={ECO:0000250|UniProtKB:P11413};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15842;
CC         Evidence={ECO:0000250|UniProtKB:P11413};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       1/3. {ECO:0000250|UniProtKB:P11413}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P11413}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; S67872; AAB29395.1; -; mRNA.
DR   RefSeq; NP_001266304.1; NM_001279375.1.
DR   AlphaFoldDB; P41571; -.
DR   SMR; P41571; -.
DR   PRIDE; P41571; -.
DR   GeneID; 101453374; -.
DR   KEGG; ccat:101453374; -.
DR   CTD; 32974; -.
DR   OrthoDB; 383995at2759; -.
DR   UniPathway; UPA00115; UER00408.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006739; P:NADP metabolic process; ISS:UniProtKB.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00966; G6PD; 1.
DR   InterPro; IPR001282; G6P_DH.
DR   InterPro; IPR019796; G6P_DH_AS.
DR   InterPro; IPR022675; G6P_DH_C.
DR   InterPro; IPR022674; G6P_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23429; PTHR23429; 1.
DR   Pfam; PF02781; G6PD_C; 1.
DR   Pfam; PF00479; G6PD_N; 1.
DR   PIRSF; PIRSF000110; G6PD; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00871; zwf; 1.
DR   PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cytoplasm; Glucose metabolism; NADP;
KW   Oxidoreductase.
FT   CHAIN           1..526
FT                   /note="Glucose-6-phosphate 1-dehydrogenase"
FT                   /id="PRO_0000068090"
FT   ACT_SITE        276
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         50..57
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         214..218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         370
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         373
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         378
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         379
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         383
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         406
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         408
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         414..416
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         434..436
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         500
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         516
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         522
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   526 AA;  60592 MW;  4047EBF7444C4917 CRC64;
     MATQHFTNGS ATDDGETALE HIIKSLETPT MKCEGTHFDS HVPHTFVIFG ASGDLAKKKI
     YPTLWWLYRD NLLPKSTKFC GYARSKLTIE ELRAKCHQYM KVQPDEQAKY EEFWQNHDYA
     AGSYDQRSDF VALKERLSSL ESCNCSCNRI FYLALPPSVF ERVTVNIKDI CLAERGWNRV
     IIEKPFGRDD VTSKKLSDHL ASLFHEDQLY RIDHYLGKEM VQNLMTIRFA NKILNSTWNR
     ENIASVLITF KEPFGTQGRG GYFDEFGIIR DVMQNHLLQI LSLVAMEKPT SCQPDDIRDE
     KVKVLKSIPA LTLDDMVLGQ YVGNPNGVGE QREGYLDDPT VSNDSNTPTY AQGVLRINNE
     RWDGVPFILR CGKALDERKA VVRIQYRDVP GDIFEGNSKR NELVIRVQPG EALYFKMMTK
     SPGITFDIEE TELDLTYEHR YKNSYLPDAY ERLILDVFCG SQMHFVRSDE LSEAWRIFTP
     VLNEIENNKV KPIPYVFGSR GPKEADQKTS ENNFKYYGSY KWIGKK
 
 
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