ID L1LFR2_THEEQ Unreviewed; 196 AA.
AC L1LFR2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
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 ORFNames=BEWA_041520 {ECO:0000313|EMBL:EKX74114.1};
OS Theileria equi strain WA.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=1537102 {ECO:0000313|EMBL:EKX74114.1, ECO:0000313|Proteomes:UP000031512};
RN [1] {ECO:0000313|EMBL:EKX74114.1, ECO:0000313|Proteomes:UP000031512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WA {ECO:0000313|EMBL:EKX74114.1,
RC ECO:0000313|Proteomes:UP000031512};
RX PubMed=23137308; DOI=10.1186/1471-2164-13-603;
RA Kappmeyer L.S., Thiagarajan M., Herndon D.R., Ramsay J.D., Caler E.,
RA Djikeng A., Gillespie J.J., Lau A.O., Roalson E.H., Silva J.C., Silva M.G.,
RA Suarez C.E., Ueti M.W., Nene V.M., Mealey R.H., Knowles D.P., Brayton K.A.;
RT "Comparative genomic analysis and phylogenetic position of Theileria
RT equi.";
RL BMC Genomics 13:603-603(2012).
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|RuleBase:RU000532}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|RuleBase:RU000696}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000256|ARBA:ARBA00008982, ECO:0000256|RuleBase:RU000532}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKX74114.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACOU01000002; EKX74114.1; -; Genomic_DNA.
DR AlphaFoldDB; L1LFR2; -.
DR STRING; 1537102.L1LFR2; -.
DR EnsemblProtists; EKX74114; EKX74114; BEWA_041520.
DR VEuPathDB; PiroplasmaDB:BEWA_041520; -.
DR eggNOG; KOG1367; Eukaryota.
DR OrthoDB; 5488671at2759; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000031512; Unassembled WGS sequence.
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 Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
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 PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000031512};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
SQ SEQUENCE 196 AA; 21103 MW; B3F733D8B814B238 CRC64;
MLDGLLDHSP ILGHSSLGKR SVEGLARLLR RHSMIKSYAH SVCQLSDKDR DSWPTSRYGF
WSSFGYWCKC GCRGLYTSIP KLLTFDMRTT LAHKDDLNFV NGTHPRETLN GLKTAPFSPI
PKVNEIKACI CEQGKVSLGS TKGGATSIIG GGDTAALAEQ TGRAKFFSHV STGGGASLEL
LEGKVLPGVS CLTQKS
//