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   27-MAR-2024, entry version 169.
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,
RC   MA96_4.4, MA96_40.1, MA96_42.4, MA96_49.2, MA96_9.3, Z(H)_26e2,
RC   Z(H)_28e2, Z(H)_36e2, Z(H)_38e2, Z(H)_44e2, Z(S)_11e2, Z(S)_28e2, and
RC   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.FBpp0306279; -.
DR   PaxDb; 7227-FBpp0303562; -.
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   AGR; FB:FBgn0250906; -.
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; 5477183at2759; -.
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 cell types or tissues.
DR   ExpressionAtlas; Q01604; baseline and differential.
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; Phosphoglycerate kinase, N-terminal domain; 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; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF0; PHOSPHOGLYCERATE KINASE; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
DR   Genevisible; Q01604; DM.
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
//