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PCKG_DROME
ID   PCKG_DROME              Reviewed;         647 AA.
AC   P20007; A1ZB97; Q53YF8; Q9V8J0;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase [GTP];
DE            Short=PEPCK;
DE            EC=4.1.1.32;
GN   Name=Pepck; Synonyms=ZDF4; ORFNames=CG17725;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Canton-S; TISSUE=Head;
RX   PubMed=3114718; DOI=10.1093/nar/15.16.6745;
RA   Gundelfinger E.D., Hermans-Borgmeyer I., Grenningloh G., Zopf D.;
RT   "Nucleotide and deduced amino acid sequence of the phosphoenolpyruvate
RT   carboxykinase (GTP) from Drosophila melanogaster.";
RL   Nucleic Acids Res. 15:6745-6745(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to
CC       phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic
CC       pathway that produces glucose from lactate and other precursors derived
CC       from the citric acid cycle. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate;
CC         Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC       family. {ECO:0000305}.
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DR   EMBL; Y00402; CAA68463.1; -; mRNA.
DR   EMBL; AE013599; AAF57676.1; -; Genomic_DNA.
DR   EMBL; BT003447; AAO39450.1; -; mRNA.
DR   PIR; A26809; QYFFGM.
DR   RefSeq; NP_523784.2; NM_079060.3.
DR   AlphaFoldDB; P20007; -.
DR   SMR; P20007; -.
DR   BioGRID; 62806; 7.
DR   DIP; DIP-22737N; -.
DR   STRING; 7227.FBpp0085880; -.
DR   PaxDb; P20007; -.
DR   PRIDE; P20007; -.
DR   DNASU; 37131; -.
DR   EnsemblMetazoa; FBtr0086701; FBpp0085880; FBgn0003067.
DR   GeneID; 37131; -.
DR   KEGG; dme:Dmel_CG17725; -.
DR   CTD; 37131; -.
DR   FlyBase; FBgn0003067; Pepck.
DR   VEuPathDB; VectorBase:FBgn0003067; -.
DR   eggNOG; KOG3749; Eukaryota.
DR   GeneTree; ENSGT00390000001912; -.
DR   HOGENOM; CLU_028872_1_1_1; -.
DR   InParanoid; P20007; -.
DR   OMA; GPTNNWV; -.
DR   PhylomeDB; P20007; -.
DR   Reactome; R-DME-70263; Gluconeogenesis.
DR   UniPathway; UPA00138; -.
DR   BioGRID-ORCS; 37131; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; Pepck; fly.
DR   GenomeRNAi; 37131; -.
DR   PRO; PR:P20007; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0003067; Expressed in arthropod fat body and 41 other tissues.
DR   Genevisible; P20007; DM.
DR   GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR   GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; ISS:FlyBase.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IBA:GO_Central.
DR   GO; GO:0006094; P:gluconeogenesis; ISS:FlyBase.
DR   GO; GO:0046327; P:glycerol biosynthetic process from pyruvate; IBA:GO_Central.
DR   GO; GO:0019543; P:propionate catabolic process; IBA:GO_Central.
DR   GO; GO:0033993; P:response to lipid; IBA:GO_Central.
DR   GO; GO:0042594; P:response to starvation; IBA:GO_Central.
DR   CDD; cd00819; PEPCK_GTP; 1.
DR   Gene3D; 3.40.449.10; -; 1.
DR   Gene3D; 3.90.228.20; -; 1.
DR   HAMAP; MF_00452; PEPCK_GTP; 1.
DR   InterPro; IPR018091; PEP_carboxykin_GTP_CS.
DR   InterPro; IPR013035; PEP_carboxykinase_C.
DR   InterPro; IPR008209; PEP_carboxykinase_GTP.
DR   InterPro; IPR035077; PEP_carboxykinase_GTP_C.
DR   InterPro; IPR035078; PEP_carboxykinase_GTP_N.
DR   InterPro; IPR008210; PEP_carboxykinase_N.
DR   PANTHER; PTHR11561; PTHR11561; 1.
DR   Pfam; PF00821; PEPCK_GTP; 1.
DR   Pfam; PF17297; PEPCK_N; 1.
DR   PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR   SUPFAM; SSF68923; SSF68923; 1.
DR   PROSITE; PS00505; PEPCK_GTP; 1.
PE   2: Evidence at transcript level;
KW   Decarboxylase; Gluconeogenesis; GTP-binding; Lyase; Manganese;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..647
FT                   /note="Phosphoenolpyruvate carboxykinase [GTP]"
FT                   /id="PRO_0000103635"
FT   ACT_SITE        314
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         261..263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         270
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         290
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         313..318
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         337
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         429..431
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         431
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         462
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         554..557
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   CONFLICT        302
FT                   /note="E -> V (in Ref. 1; CAA68463)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        408
FT                   /note="Q -> R (in Ref. 1; CAA68463)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   647 AA;  71129 MW;  0DB81B3D9E1B1FBB CRC64;
     MPELIEQSKI ISGNVCGLPQ LHKLRQDNCG LYSHIRGIPI SYGNVDLLTT GVRAFVEEGI
     ALCQPDQVHI CDGSEQENKV LIKSLLEAGT IVPLPKYDNC WLARTNPADV ARVESRTFIC
     TERREETIPT PVEGVKGTLG NWISPSDMDA AVQQRFPGCM KGRTMYVVPF SMGPVGSPLS
     KIGIELTDSA YVVASMRIMT RMGAAVLRQL AKKEEFVRAL HSVGAPANGQ VEQPSWPCDP
     ERTIILHKPA ENLIVSYGSG YGGNSLLGKK CFALRIGSTI AKQEGWLAEH MLILGITDPK
     GEKKYITAAF PSACGKTNLA MLNPSLANYK VECVGDDIAW MKFDSQGVLR AINPENGFFG
     VAPGTSMETN PIAMNTVFKN TIFTNVASTS DGGVFWEGME SSLAPNVQIT DWLGKPWTKD
     SGKPAAHPNS RFCTPAAQCP IIDEAWEDPA GVPISAMLFG GRRPAGVPLI YEARDWTHGV
     FIGAAMRSEA TAAAEHKGKV IMHDPFAMRP FFGYNFGDYV AHWLSMEKRG QVPKIFHVNW
     FRKSAEGKFM WPGYGENSRV LEWILRRVNG ESCYVDSAIG HIPAEGALNL DGMKDKVDVK
     EIFSLPKEFW SQEVKDIRTY FESQVGADLP ASIYQQLDEL SSRVDNL
 
 
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