ID E9AGT9_LEIIN Unreviewed; 479 AA.
AC E9AGT9; A0A2K4YSQ7; A0A381MG46;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 72.
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};
GN Name=PGKC {ECO:0000313|EMBL:CBZ08601.1};
GN ORFNames=LINJ_20_0110 {ECO:0000313|EMBL:CBZ08601.1};
OS Leishmania infantum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5671 {ECO:0000313|EMBL:CBZ08601.1, ECO:0000313|Proteomes:UP000008153};
RN [1] {ECO:0000313|EMBL:CBZ08601.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CBZ08601.1,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
RN [2] {ECO:0000313|EMBL:CBZ08601.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CBZ08601.1,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JPCM5;
RA Hilley J.D., Rogers M., Wilkes J., Dickens N.J., Bates P., Depledge D.P.,
RA Harris D., Her Y., Herzyk P., Imamura H., Otto T.D., Saad W., Seeger K.,
RA Berriman M., Smith D.F., Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow genomic structural
RT differences between species and strains of Leishmania.";
RL Submitted (FEB-2011) 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 Evidence={ECO:0000256|ARBA:ARBA00000642,
CC 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; FR796452; CBZ08601.1; -; Genomic_DNA.
DR RefSeq; XP_003392440.1; XM_003392392.1.
DR AlphaFoldDB; E9AGT9; -.
DR SMR; E9AGT9; -.
DR STRING; 5671.E9AGT9; -.
DR GeneID; 10966714; -.
DR KEGG; lif:LINJ_20_0110; -.
DR VEuPathDB; TriTrypDB:LINF_200006000; -.
DR eggNOG; KOG1367; Eukaryota.
DR InParanoid; E9AGT9; -.
DR OrthoDB; 5477183at2759; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000008153; Chromosome 20.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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; 2.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR027250; Pgk_euglenozoa.
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:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PIRSF; PIRSF500126; Pgk_euglenozoa; 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 Reference proteome {ECO:0000313|Proteomes:UP000008153};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 39
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 132
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 220
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 372..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
SQ SEQUENCE 479 AA; 51377 MW; 1C7C9B9874F68107 CRC64;
MSLVLKKSID DATFRDKKVL IRVDFNVPVK NGKITNDFRI RSALPTIQKV LKEGGSCILM
SHLGRPKGAR MSDPRPEKGV RGYEEAASLR PVAARIAELL GQKVEFAPDC LDAAVYASKL
KSGDVLLLEN VRFYAEEGSK KEEERDAMAK VLASYADLYV SDAFGTAHRD SATMTGIPKV
LGAGYAGYLM EKEINYFSRV LNNPPRPLVA IVGGAKVSDK IELLDNMLGR INYLVIGGAM
AYTFQKAQGR KIGISMCEED KLDLAKSLLK KAQERGVQVF LPVDHVCNKE FKAADSPLVT
ENVDVPDGYM ALDIGPKTIH LYEEVIGRCK SAIWNGPMGV FEMPCYSKGT FAVAKAMGTG
TQKSGLLSII GGGDSASAAE LSGEAKNMSH VSTGGGASLE LLEGKTLPGV AILTDKDVKE
RGSSCKFAFG GGAPSREVCP RGSGHIFGGA SIVTEIVKLV GALLMGIFIG RRMSTKLIR
//