ID E9AZ83_LEIMU Unreviewed; 525 AA.
AC E9AZ83;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00012363};
DE EC=4.1.1.49 {ECO:0000256|ARBA:ARBA00012363};
GN ORFNames=LMXM_27_1810 {ECO:0000313|EMBL:CBZ28283.1};
OS Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ28283.1, ECO:0000313|Proteomes:UP000007259};
RN [1] {ECO:0000313|EMBL:CBZ28283.1, ECO:0000313|Proteomes:UP000007259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|EMBL:CBZ28283.1,
RC ECO:0000313|Proteomes:UP000007259};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
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 ---------------------------------------------------------------------------
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; FR799580; CBZ28283.1; -; Genomic_DNA.
DR RefSeq; XP_003876755.1; XM_003876706.1.
DR AlphaFoldDB; E9AZ83; -.
DR GeneID; 13449737; -.
DR KEGG; lmi:LMXM_27_1810; -.
DR VEuPathDB; TriTrypDB:LmxM.27.1810; -.
DR OMA; GRNDNKP; -.
DR OrthoDB; 3740611at2759; -.
DR PhylomeDB; E9AZ83; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000007259; Chromosome 27.
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:CBZ28283.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:CBZ28283.1};
KW Transferase {ECO:0000313|EMBL:CBZ28283.1}.
SQ SEQUENCE 525 AA; 58380 MW; C866073080442A85 CRC64;
MAPIIHRNLT APELVQWALK LEKDSKLSAR GALCVLSYAK TGRSPRDKRV VDTDDVRENV
DWGSVNVKLS EESFAKVKKR AMDFLNSRDH LFIVDCFAGH DERYRLKVRA ITARPYHALF
MHNMLIRPTQ QELENFGEPQ YTIYNAGEHS ADPSVPGVTS TTSVSLNFKT GEEVILGTEY
AGEMKKGILT VMFELMPRQG HLCMHASANV GKRGDVTVFF GLSGTGKTTL SADPKRMLIG
DDEHVWTDRG VFNIEGGCYA KAIGLNPKTE EEIYNAVRFG SVAENCTLEK LKHEIDFNDE
SISKNTRVAY PLEHIPGALT HAVAGHPSNV IFLTNDAFGV MPPVARLTPE QAMFWFIMGY
TANVPGVEVG STPVAKPIFS SCFAGPFLVR HATFYGEQLA KKMTEHNARV WLLNTGYAGG
RADRGAKRMP LKVTRAVIDA IHNGSLDKEE YGVYPGWGLQ IPKRCARVPE QLLDPRKAWK
DVKAFNKTTE ELVLMFQASF QKRFAAKASE ALKSAVPKYV ETAHL
//
