ID A5XCI1_DROSI Unreviewed; 415 AA.
AC A5XCI1;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 03-MAY-2023, entry version 62.
DE RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
DE EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
DE Flags: Fragment;
GN Name=Pgk {ECO:0000313|EMBL:ABH06617.1};
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240 {ECO:0000313|EMBL:ABH06617.1};
RN [1] {ECO:0000313|EMBL:ABH06617.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HFL97_2.1 {ECO:0000313|EMBL:ABH06617.1};
RA Flowers J.M., Sezgin E., Kumagai S., Duvernell D.D., Matzkin L.M.,
RA Schmidt P.S., Eanes W.F.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABH06617.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HFL97_2.1 {ECO:0000313|EMBL:ABH06617.1};
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).
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 Evidence={ECO:0000256|RuleBase:RU000532};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000256|ARBA:ARBA00004838,
CC ECO:0000256|RuleBase:RU000532}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC ECO:0000256|RuleBase:RU000696}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000256|ARBA:ARBA00008982, ECO:0000256|RuleBase:RU000532}.
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DR EMBL; DQ863982; ABH06617.1; -; Genomic_DNA.
DR AlphaFoldDB; A5XCI1; -.
DR UniPathway; UPA00109; UER00185.
DR ChiTaRS; Pgk; fly.
DR GO; GO:0031430; C:M band; IEA:EnsemblMetazoa.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0030018; C:Z disc; IEA:EnsemblMetazoa.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:EnsemblMetazoa.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:EnsemblMetazoa.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000724-
KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT BINDING 23..25
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 62..65
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 371..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT NON_TER 415
FT /evidence="ECO:0000313|EMBL:ABH06617.1"
SQ SEQUENCE 415 AA; 43820 MW; 5A74599763CC25D1 CRC64;
MAFNNLSIEN LDLAGKRVLM RVDFNVPIKE GKITSNQRIV AALDSVKLAL 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 ALSSA
//
