PGKC_LEIME
ID PGKC_LEIME Reviewed; 479 AA.
AC Q27685;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Phosphoglycerate kinase, glycosomal;
DE Short=Phosphoglycerate kinase C;
DE EC=2.7.2.3;
GN Name=PGKC;
OS Leishmania mexicana.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5665;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MHOM/BZ/84/BEL46;
RX PubMed=9497040; DOI=10.1016/s0166-6851(97)00152-7;
RA Adje C.A., Opperdoes F.R., Michels P.A.M.;
RT "Organization, sequence and stage-specific expression of the
RT phosphoglycerate kinase genes of Leishmania mexicana mexicana.";
RL Mol. Biochem. Parasitol. 90:155-168(1997).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Glycosome.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; X98487; CAA67113.1; -; Genomic_DNA.
DR AlphaFoldDB; Q27685; -.
DR SMR; Q27685; -.
DR VEuPathDB; TriTrypDB:LmxM.20.0100; -.
DR UniPathway; UPA00109; UER00185.
DR GO; GO:0020015; C:glycosome; IEA:UniProtKB-SubCell.
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 CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 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; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PIRSF; PIRSF500126; Pgk_euglenozoa; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycolysis; Glycosome; Kinase; Nucleotide-binding; Peroxisome;
KW Transferase.
FT CHAIN 1..479
FT /note="Phosphoglycerate kinase, glycosomal"
FT /id="PRO_0000145856"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 62..65
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 220
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 372..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 479 AA; 51499 MW; 03C3B8B12DF7DAB4 CRC64;
MSLVLKKSID DVALKDKKVL IRVDFNVPVK NGEITNDFRI RSALPTIQKV LKEGGSCILM
SHLGRPKGAR MSDPKPEKGV RGYEEAATLR PVAAALSELL EKKVAFAPDC LNASIYVSKL
KRGDVLLLEN VRFYTEEGSK KEEEADAMAK VLASYADLYV SDAFGTAHRD SATMTGIPKV
LGSGYAGYLM EKEINYFSRV LNNPPRPLVA IVGGAKVSDK IELLDNMLGR INYLVIGGAM
AYTFQKAQGR KIGISMCEED KLDLAKSLLK KAQERGVQVL LPVDHVCNKE FKAVDSPLVT
EDVDVPDGYM ALDIGPKTIH MYEEVIGRCK SAIWNGPMGV FEMPCYSKGT FAVAKAMGTG
TQKDGLLSII GGGDTASAAE LSGEAKNMSH VSTGGGASLE LLEGKTLPGV AILTDKEVKG
RGPLLKCACG GASPSNESCP RRREGIWGGG FIVTEIVKLV GALLIGIFIG RRLNTKLIR