PGK_DROME
ID PGK_DROME Reviewed; 415 AA.
AC Q01604; A5XCG6; Q3KN29; Q9VQF6;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=Pgk; ORFNames=CG3127;
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 [GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=1465095; DOI=10.1007/bf00279363;
RA Roselli-Rehfuss L., Ye F., Lissemore J.L., Sullivan D.T.;
RT "Structure and expression of the phosphoglycerate kinase (Pgk) gene of
RT Drosophila melanogaster.";
RL Mol. Gen. Genet. 235:213-220(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-388.
RC STRAIN=DPF96_10, DPF96_26, DPF96_5.1, DPF96_8.3, HFL97_15e, HFL97_23e,
RC HFL97_3e2, HFL97_61e, HFL97_68e, MA96_24.2, MA96_26.4, MA96_3.5, MA96_4.4,
RC MA96_40.1, MA96_42.4, MA96_49.2, MA96_9.3, Z(H)_26e2, Z(H)_28e2, Z(H)_36e2,
RC Z(H)_38e2, Z(H)_44e2, Z(S)_11e2, Z(S)_28e2, and Z(S)_49e2;
RX PubMed=17379620; DOI=10.1093/molbev/msm057;
RA Flowers J., Sezgin E., Kumagai S., Duvernell D., Matzkin L., Schmidt P.,
RA Eanes W.;
RT "Adaptive evolution of metabolic pathways in Drosophila.";
RL Mol. Biol. Evol. 24:1347-1354(2007).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; Z14029; CAA78404.1; -; Genomic_DNA.
DR EMBL; DQ863952; ABH06587.1; -; Genomic_DNA.
DR EMBL; DQ863953; ABH06588.1; -; Genomic_DNA.
DR EMBL; DQ863954; ABH06589.1; -; Genomic_DNA.
DR EMBL; DQ863955; ABH06590.1; -; Genomic_DNA.
DR EMBL; DQ863956; ABH06591.1; -; Genomic_DNA.
DR EMBL; DQ863957; ABH06592.1; -; Genomic_DNA.
DR EMBL; DQ863958; ABH06593.1; -; Genomic_DNA.
DR EMBL; DQ863959; ABH06594.1; -; Genomic_DNA.
DR EMBL; DQ863960; ABH06595.1; -; Genomic_DNA.
DR EMBL; DQ863961; ABH06596.1; -; Genomic_DNA.
DR EMBL; DQ863962; ABH06597.1; -; Genomic_DNA.
DR EMBL; DQ863963; ABH06598.1; -; Genomic_DNA.
DR EMBL; DQ863964; ABH06599.1; -; Genomic_DNA.
DR EMBL; DQ863965; ABH06600.1; -; Genomic_DNA.
DR EMBL; DQ863966; ABH06601.1; -; Genomic_DNA.
DR EMBL; DQ863967; ABH06602.1; -; Genomic_DNA.
DR EMBL; DQ863968; ABH06603.1; -; Genomic_DNA.
DR EMBL; DQ863969; ABH06604.1; -; Genomic_DNA.
DR EMBL; DQ863970; ABH06605.1; -; Genomic_DNA.
DR EMBL; DQ863971; ABH06606.1; -; Genomic_DNA.
DR EMBL; DQ863972; ABH06607.1; -; Genomic_DNA.
DR EMBL; DQ863973; ABH06608.1; -; Genomic_DNA.
DR EMBL; DQ863974; ABH06609.1; -; Genomic_DNA.
DR EMBL; DQ863975; ABH06610.1; -; Genomic_DNA.
DR EMBL; DQ863976; ABH06611.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF51218.1; -; Genomic_DNA.
DR EMBL; BT023910; ABA81844.1; -; mRNA.
DR PIR; S30111; KIFFPG.
DR RefSeq; NP_001259956.1; NM_001273027.1.
DR RefSeq; NP_001259957.1; NM_001273028.1.
DR RefSeq; NP_001259958.1; NM_001273029.1.
DR RefSeq; NP_001259959.1; NM_001273030.1.
DR RefSeq; NP_476676.1; NM_057328.4.
DR AlphaFoldDB; Q01604; -.
DR SMR; Q01604; -.
DR BioGRID; 59686; 39.
DR IntAct; Q01604; 3.
DR STRING; 7227.FBpp0303562; -.
DR PaxDb; Q01604; -.
DR PRIDE; Q01604; -.
DR DNASU; 33461; -.
DR EnsemblMetazoa; FBtr0077739; FBpp0077419; FBgn0250906.
DR EnsemblMetazoa; FBtr0330716; FBpp0303560; FBgn0250906.
DR EnsemblMetazoa; FBtr0330717; FBpp0303561; FBgn0250906.
DR EnsemblMetazoa; FBtr0330718; FBpp0303562; FBgn0250906.
DR EnsemblMetazoa; FBtr0334162; FBpp0306279; FBgn0250906.
DR GeneID; 33461; -.
DR KEGG; dme:Dmel_CG3127; -.
DR CTD; 33461; -.
DR FlyBase; FBgn0250906; Pgk.
DR VEuPathDB; VectorBase:FBgn0250906; -.
DR eggNOG; KOG1367; Eukaryota.
DR GeneTree; ENSGT00390000008820; -.
DR HOGENOM; CLU_025427_0_0_1; -.
DR InParanoid; Q01604; -.
DR OMA; DMIFDIG; -.
DR OrthoDB; 838642at2759; -.
DR PhylomeDB; Q01604; -.
DR Reactome; R-DME-70171; Glycolysis.
DR Reactome; R-DME-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00185.
DR BioGRID-ORCS; 33461; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Pgk; fly.
DR GenomeRNAi; 33461; -.
DR PRO; PR:Q01604; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0250906; Expressed in adult hindgut (Drosophila) and 27 other tissues.
DR ExpressionAtlas; Q01604; baseline and differential.
DR Genevisible; Q01604; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031430; C:M band; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0030018; C:Z disc; IDA:FlyBase.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IDA:FlyBase.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; ISS:FlyBase.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IGI:FlyBase.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 3.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR PANTHER; PTHR11406; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..415
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145843"
FT BINDING 23..25
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 62..65
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 371..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VARIANT 388
FT /note="S -> A (in strain: HFL97_3e2)"
FT /evidence="ECO:0000269|PubMed:17379620"
FT CONFLICT 410
FT /note="A -> R (in Ref. 1; CAA78404)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 43862 MW; 7D1225FCC81F8B42 CRC64;
MAFNKLSIEN LDLAGKRVLM RVDFNVPIKE GKITSNQRIV AALDSIKLAL SKKAKSVVLM
SHLGRPDGNK NIKYTLAPVA AELKTLLGQD VIFLSDCVGS EVEAACKDPA PGSVILLENV
RFYVEEEGKG LDASGGKVKA DPAKVKEFRA SLAKLGDVYV NDAFGTAHRA HSSMMGDGFE
QRAAGLLLNK ELKYFSQALD KPPNPFLAIL GGAKVADKIQ LIENLLDKVN EMIIGGGMAF
TFLKVLNNMK IGGSLFDEEG SKIVEKLVEK AKKNNVQLHL PVDFVCGDKF AENAAVSEAT
VEAGIPDGHM GLDVGPKTRE LFAAPIARAK LIVWNGPPGV FEFPNFANGT KSIMDGVVAA
TKNGTVSIIG GGDTASCCAK WNTEALVSHV STGGGASLEL LEGKTLPGVA ALTSA
