ID J4C2M8_THEOR Unreviewed; 698 AA.
AC J4C2M8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00012363};
DE EC=4.1.1.49 {ECO:0000256|ARBA:ARBA00012363};
GN ORFNames=TOT_010000431 {ECO:0000313|EMBL:BAM38966.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM38966.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM38966.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM38966.1,
RC ECO:0000313|Proteomes:UP000003786};
RX PubMed=22951932;
RA Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT "Comparative genome analysis of three eukaryotic parasites with differing
RT abilities to transform leukocytes reveals key mediators of Theileria-
RT induced leukocyte transformation.";
RL MBio 3:e00204-e00212(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18617, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=4.1.1.49; Evidence={ECO:0000256|ARBA:ARBA00001389};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC family. {ECO:0000256|ARBA:ARBA00006052}.
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DR EMBL; AP011946; BAM38966.1; -; Genomic_DNA.
DR RefSeq; XP_009689267.1; XM_009690972.1.
DR AlphaFoldDB; J4C2M8; -.
DR STRING; 869250.J4C2M8; -.
DR EnsemblProtists; BAM38966; BAM38966; TOT_010000431.
DR GeneID; 20713344; -.
DR KEGG; tot:TOT_010000431; -.
DR VEuPathDB; PiroplasmaDB:TOT_010000431; -.
DR eggNOG; ENOG502QQI5; Eukaryota.
DR OrthoDB; 3740611at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000003786; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.90.228.20; -; 3.
DR Gene3D; 3.40.449.10; Phosphoenolpyruvate Carboxykinase, domain 1; 1.
DR HAMAP; MF_00453; PEPCK_ATP; 1.
DR InterPro; IPR001272; PEP_carboxykinase_ATP.
DR InterPro; IPR013035; PEP_carboxykinase_C.
DR InterPro; IPR008210; PEP_carboxykinase_N.
DR InterPro; IPR015994; PEPCK_ATP_CS.
DR PANTHER; PTHR30031:SF0; PHOSPHOENOLPYRUVATE CARBOXYKINASE (ATP); 1.
DR PANTHER; PTHR30031; PHOSPHOENOLPYRUVATE CARBOXYKINASE ATP; 1.
DR Pfam; PF01293; PEPCK_ATP; 2.
DR SUPFAM; SSF68923; PEP carboxykinase N-terminal domain; 1.
DR SUPFAM; SSF53795; PEP carboxykinase-like; 2.
DR PROSITE; PS00532; PEPCK_ATP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW Kinase {ECO:0000313|EMBL:BAM38966.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:BAM38966.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003786};
KW Transferase {ECO:0000313|EMBL:BAM38966.1}.
SQ SEQUENCE 698 AA; 77033 MW; 42B4B78746D2D44D CRC64;
MAKVTVNTNV PHYNVLLDKV NGLNISGPKN PDLTQGVSDK KENQLVPEKL ETSAEDFLAP
VKTTLKTSED GPYGKIDESK VLHNSCIPLL YHHALRFEAH TELTSTGALS CLSEDRLTIF
DRYMASLGWL IHEIVGEKTG RSPLDKRTVL DDNTRDTVWW DSVNIPIDLE SFNMNKKLAV
DFINTNERIY VTDAFAGWDP DHRLKVRVVS IRAYHALFMH NLLIVPSQDE LKDFKPDFTI
YNAGPCDAKP SIPGVTSNTS ICINYTSMEM IILGSEYAGE MKKGILTLMM YILPQKGLLP
LHSSCNVDAS GNVTLFFGLS GTGKTTLSTE PNRLLIGDDE HVWTDRGVFN IEGGCYAKCK
DLSKDHEPEI FDAIKFGSVL ENVVLDETNK VVDYKDVSIT ENTRCAYPLE FIKNVKLPAL
VNNHPNNVIF LTCDAFGALP PVSLLNTSQA IYHFVSGYTT KMVGTEIGVN KPTATFSACY
AGPFLALSPL VYADLLYEKL SGGKTKEVPA GVSSGPEEVL GADAANLDGM NLDKASLGAD
SVGGNDDPGR VNNIDNKANF ENPSNPGANN SSLDFSGFNG NIRVWLLNTG WIGGSIDSPN
GRRIPLKYSR RIVDAINNDE ISRDPKDFDV MPYFGILVPR NVNGVPREVL NQQLSWPDRE
HYLQQVETVA AKFVKNFNQY RSRANSLILR GEPKLTQA
//
