PGKC_CRIFA
ID PGKC_CRIFA Reviewed; 455 AA.
AC P08967;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Phosphoglycerate kinase, glycosomal;
DE Short=Phosphoglycerate kinase C;
DE EC=2.7.2.3;
GN Name=PGKC; Synonyms=PGK-C;
OS Crithidia fasciculata.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Crithidia.
OX NCBI_TaxID=5656;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3402434; DOI=10.1002/j.1460-2075.1988.tb02926.x;
RA Swinkels B.W., Evers R., Borst P.;
RT "The topogenic signal of the glycosomal (microbody) phosphoglycerate kinase
RT of Crithidia fasciculata resides in a carboxy-terminal extension.";
RL EMBO J. 7:1159-1165(1988).
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: Glycosome.
CC -!- DOMAIN: This glycosomal PGK has a C-terminal extension of 38 AA which
CC is not present in the cytosolic isoenzyme. This domain most likely
CC serves as topogenic signal to direct the glycosomal PKG to the
CC glycosome.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; X07459; CAA30342.1; -; Genomic_DNA.
DR PIR; S00487; TVCRGG.
DR AlphaFoldDB; P08967; -.
DR SMR; P08967; -.
DR PRIDE; P08967; -.
DR VEuPathDB; TriTrypDB:CFAC1_180006900; -.
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..455
FT /note="Phosphoglycerate kinase, glycosomal"
FT /id="PRO_0000145850"
FT REGION 417..455
FT /note="Topogenic signal"
FT /evidence="ECO:0000255"
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 455 AA; 47843 MW; D8BF53AE5A0E1BFE CRC64;
MSLVPKKSID DAVVKGKKVL IRVDFNVPVK NGEITNDFRI RSALPTIQKV LKEGGSCILM
SHLGRPKGAK MSDPKPAKSV RGYEEAATLR PVAARLSELL GQKVEFAPDC LDAASYAAKL
KGGDVLLLEN VRFYAEEGSK KEEERDAMAK VLAAYGDVYV SDAFGTAHRD SADMTGIPKV
LGAGYAGYLM EKEINYFAQV LNNPPRPLVA IVGGAKVSDK IQLLDNMLGR INYLVIGGAM
AYTFQKAQGH AIGISMCEED KLDLAKSLLK KAQERNVEVL LPVDHVCNKE FQGVDAPLVT
KDVEIPEGYM ALDIGPKTIK IYEDVIAKCK STIWNGPMGV FEMPCYSKGT FAVAKAMGNG
TQKNGLMSII GGGDTASAAE LSGEAKNMSH VSTGGGASLE LLEGKSLPGV TVLTNKDAKA
PAAAAAAGGD CPCGSGCAAV PAAATATVSM VLASP