PCKA_TRYBB
ID PCKA_TRYBB Reviewed; 472 AA.
AC P13735;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Phosphoenolpyruvate carboxykinase (ATP), glycosomal;
DE EC=4.1.1.49;
DE AltName: Full=Glycosomal protein p60;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2925689; DOI=10.1016/s0021-9258(18)83719-x;
RA Kueng V., Schlaeppi K., Schneider A., Seebeck T.;
RT "A glycosomal protein (p60) which is predominantly expressed in procyclic
RT Trypanosoma brucei. Characterization and DNA sequence.";
RL J. Biol. Chem. 264:5203-5209(1989).
RN [2]
RP FUNCTION.
RX PubMed=2671940; DOI=10.1093/nar/17.15.6411;
RA Parsons M., Smith J.M.;
RT "Trypanosome glycosomal protein P60 is homologous to phosphoenolpyruvate
RT carboxykinase (ATP).";
RL Nucleic Acids Res. 17:6411-6411(1989).
CC -!- FUNCTION: P60 has the capability to bind to microtubules and membrane
CC vesicles in vitro. {ECO:0000269|PubMed:2671940}.
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.
CC -!- SUBCELLULAR LOCATION: Glycosome.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC family. {ECO:0000305}.
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DR EMBL; M20570; AAA30199.1; -; Genomic_DNA.
DR PIR; A33275; A33275.
DR AlphaFoldDB; P13735; -.
DR SMR; P13735; -.
DR PRIDE; P13735; -.
DR UniPathway; UPA00138; -.
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 3: Inferred from homology;
KW ATP-binding; Decarboxylase; Gluconeogenesis; Glycosome; Lyase;
KW Nucleotide-binding; Peroxisome.
FT CHAIN 1..472
FT /note="Phosphoenolpyruvate carboxykinase (ATP), glycosomal"
FT /id="PRO_0000203867"
FT BINDING 221..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 472 AA; 52457 MW; 82768661A5A04786 CRC64;
MAPIIHKNLT APELVEWALK LEKDSQLTAR GALSVRSYAK TGRSPRDKRI VNTTDVTDNV
DWGSVNMKLT EESFEKLKTI AKDYFATCKH LFVMDCFAGH DERYRLKVRV YTTRPYHALF
MRNMLIVPTL EELQSFGEPD YVIYNAGEAK ADPTVPGVTS TTSVALNFKT REQVILGTEY
AGEMKKGILT VMFELMPRMG HLCMHASANV GKSGDVTVFF GLSGTGKTTL SADPRRNLIG
DDEHVWTDRG VFNIEGGCYA KAIGLNPETE KDIYEAVRFG AVAENCTLDR RTHEIDFNDE
SICKNTRVAY PLMHIDGALS KAVAGHPKNI IFLTNDAFGV MPPVARLTSA QAMFWFVMGY
TANVPGVEAG SARVARPIFS SCFGGPFLVR HATHYGQQLA EKMEKHNSRV WLLNTGYAGG
RADRGAKRMP LRVTRAIIDA IHDGTLDQAD YEVYPGWAFT FLRGLRTCPQ AC