PCKA_TRYCR
ID PCKA_TRYCR Reviewed; 472 AA.
AC P51058;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Phosphoenolpyruvate carboxykinase (ATP), glycosomal;
DE EC=4.1.1.49;
GN Name=PEPCK;
OS Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8294043; DOI=10.1016/0378-1119(93)90449-d;
RA Linss J., Goldenberg S., Urbina J.A., Amzel L.M.;
RT "Cloning and characterization of the gene encoding ATP-dependent phospho-
RT enol-pyruvate carboxykinase in Trypanosoma cruzi: comparison of primary and
RT predicted secondary structure with host GTP-dependent enzyme.";
RL Gene 136:69-77(1993).
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;
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Glycosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC family. {ECO:0000305}.
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; M91163; AAA50780.1; -; mRNA.
DR PDB; 1II2; X-ray; 2.00 A; A/B=2-457.
DR PDBsum; 1II2; -.
DR AlphaFoldDB; P51058; -.
DR SMR; P51058; -.
DR VEuPathDB; TriTrypDB:BCY84_02917; -.
DR VEuPathDB; TriTrypDB:C3747_111g98; -.
DR VEuPathDB; TriTrypDB:C4B63_9g285; -.
DR VEuPathDB; TriTrypDB:Tc_MARK_9661; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0071790; -.
DR VEuPathDB; TriTrypDB:TcCL_ESM11520; -.
DR VEuPathDB; TriTrypDB:TcCLB.507547.90; -.
DR VEuPathDB; TriTrypDB:TcCLB.508441.20; -.
DR VEuPathDB; TriTrypDB:TCDM_05454; -.
DR VEuPathDB; TriTrypDB:TcG_04606; -.
DR VEuPathDB; TriTrypDB:TCSYLVIO_007781; -.
DR VEuPathDB; TriTrypDB:TcYC6_0076530; -.
DR BRENDA; 4.1.1.49; 6524.
DR SABIO-RK; P51058; -.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P51058; -.
DR GO; GO:0020015; C:glycosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; 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 Gene3D; 3.40.449.10; -; 1.
DR Gene3D; 3.90.228.20; -; 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; PTHR30031; 1.
DR Pfam; PF01293; PEPCK_ATP; 1.
DR PIRSF; PIRSF006294; PEP_crbxkin; 1.
DR SUPFAM; SSF68923; SSF68923; 1.
DR PROSITE; PS00532; PEPCK_ATP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Decarboxylase; Gluconeogenesis; Glycosome;
KW Lyase; Nucleotide-binding; Peroxisome.
FT CHAIN 1..472
FT /note="Phosphoenolpyruvate carboxykinase (ATP), glycosomal"
FT /id="PRO_0000203868"
FT BINDING 221..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1II2"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1II2"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:1II2"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:1II2"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1II2"
FT HELIX 71..86
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 88..98
FT /evidence="ECO:0007829|PDB:1II2"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:1II2"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:1II2"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:1II2"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:1II2"
FT HELIX 182..198
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:1II2"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:1II2"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:1II2"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:1II2"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:1II2"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:1II2"
FT HELIX 349..358
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:1II2"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:1II2"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:1II2"
FT HELIX 392..406
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:1II2"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:1II2"
FT HELIX 431..442
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:1II2"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:1II2"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:1II2"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:1II2"
SQ SEQUENCE 472 AA; 52585 MW; ECD918DB3882CFE0 CRC64;
MPPTIHRNLL SPELVQWALK IEKDSRLTAR GALAVMSYAK TGRSPLDKRI VDTDDVRENV
DWGKVNMKLS EESFARVRKI AKEFLDTREH LFVVDCFAGH DERYRLKVRV FTTRPYHALF
MRDMLIVPTP EELATFGEPD YVIYNAGECK ADPSIPGLTS TTCVALNFKT REQVILGTEY
AGEMKKGILT VMFELMPQMN HLCMHASANV GKQGDVTVFF GLSGTGKTTL SADPHRNLIG
DDEHVWTDRG VFNIEGGCYA KAIGLNPKTE KDIYDAVRFG AVAENCVLDK RTGEIDFYDE
SICKNTRVAY PLSHIEGALS KAIAGHPKNV IFLTNDAFGV MPPVARLTSA QAMFWFVMGY
TANVPGVEAG GTRTARPIFS SCFGGPFLVR HATFYGEQLA EKMQKHNSRV WLLNTGYAGG
RADRGAKRMP LRVTRAIIDA IHDGTLDRTE YEEYPGWACT SRSTSPKCRS IC
