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Database: UniProt
Entry: L1LFR2_THEEQ
LinkDB: L1LFR2_THEEQ
Original site: L1LFR2_THEEQ 
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}.
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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
//
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