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Database: UniProt
Entry: K2MWC4_TRYCR
LinkDB: K2MWC4_TRYCR
Original site: K2MWC4_TRYCR 
ID   K2MWC4_TRYCR            Unreviewed;       525 AA.
AC   K2MWC4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00012363};
DE            EC=4.1.1.49 {ECO:0000256|ARBA:ARBA00012363};
GN   ORFNames=MOQ_009660 {ECO:0000313|EMBL:EKF26641.1};
OS   Trypanosoma cruzi marinkellei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=85056 {ECO:0000313|EMBL:EKF26641.1, ECO:0000313|Proteomes:UP000007350};
RN   [1] {ECO:0000313|EMBL:EKF26641.1, ECO:0000313|Proteomes:UP000007350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B7 {ECO:0000313|EMBL:EKF26641.1,
RC   ECO:0000313|Proteomes:UP000007350};
RX   PubMed=23035642; DOI=10.1186/1471-2164-13-531;
RA   Franzen O., Talavera-Lopez C., Ochaya S., Butler C.E., Messenger L.A.,
RA   Lewis M.D., Llewellyn M.S., Marinkelle C.J., Tyler K.M., Miles M.A.,
RA   Andersson B.;
RT   "Comparative genomic analysis of human infective Trypanosoma cruzi lineages
RT   with the bat-restricted subspecies T. cruzi marinkellei.";
RL   BMC Genomics 13:531-531(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}.
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:EKF26641.1}.
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DR   EMBL; AHKC01020241; EKF26641.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2MWC4; -.
DR   EnsemblProtists; EKF26641; EKF26641; MOQ_009660.
DR   OrthoDB; 3740611at2759; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000007350; Unassembled WGS sequence.
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   CDD; cd00484; PEPCK_ATP; 1.
DR   Gene3D; 3.90.228.20; -; 1.
DR   Gene3D; 3.40.449.10; Phosphoenolpyruvate Carboxykinase, domain 1; 1.
DR   Gene3D; 2.170.8.10; Phosphoenolpyruvate Carboxykinase, domain 2; 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   NCBIfam; TIGR00224; pckA; 1.
DR   PANTHER; PTHR30031:SF0; PHOSPHOENOLPYRUVATE CARBOXYKINASE (ATP); 1.
DR   PANTHER; PTHR30031; PHOSPHOENOLPYRUVATE CARBOXYKINASE ATP; 1.
DR   Pfam; PF01293; PEPCK_ATP; 1.
DR   PIRSF; PIRSF006294; PEP_crbxkin; 1.
DR   SUPFAM; SSF68923; PEP carboxykinase N-terminal domain; 1.
DR   SUPFAM; SSF53795; PEP carboxykinase-like; 1.
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:EKF26641.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyruvate {ECO:0000313|EMBL:EKF26641.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007350};
KW   Transferase {ECO:0000313|EMBL:EKF26641.1}.
SQ   SEQUENCE   525 AA;  58589 MW;  3153CB8DFB992959 CRC64;
     MPPTIHRNLL SPELVQWALK IEKDSCLTAR GALSVMSYAK TGRSPLDKRI VDTDDVRENV
     DWGKVNMKLS EESFARVKKI AKDFLDSREH LFVVDCFAGH DERYRLKVRV ITTRPYHALF
     MRDMLIVPTP EELATFGEPE YVIYNAGECK ADPSIPGLTS TTCVALNFKT REQVILGTEY
     AGEMKKGILT VMFELMPRMN HLCMHASANV GKQGDVSVFF GLSGTGKTTL SADPNRNLIG
     DDEHVWTDRG VFNIEGGCYA KAIGLNPKTE KDIYDAVRFG AVAENCVLDK RTGEIDFYDE
     SICKNTRVAY PLSHIEGALS KALAGHPKNI IFLTNDAFGV MPPVARLTSA QAMFWFVMGY
     TANVPGVEAG GSRTARPIFS SCFGGPFLVR HATFYGEQLA EKMQKHNSRV WLLNTGYAGG
     RADRGAKRMP LRVTRAIIDA IHDGTLDRAE YEEYPGWGLH IPKYVAKVPE HLLNPCKAWK
     DVRQFNATSK ELVAMFQESF NTRFAAKASQ EMKSAVPRYV EPAHL
//
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