ID   PCKA_CANAX              Reviewed;         553 AA.
AC   O13434;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase (ATP);
DE            EC=4.1.1.49;
GN   Name=PCK1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SGY243;
RX   PubMed=9224895; DOI=10.1016/s0378-1119(97)00069-3;
RA   Leuker C.E., Sonneborn A., Delbruck S., Ernst J.F.;
RT   "Sequence and promoter regulation of the PCK1 gene encoding
RT   phosphoenolpyruvate carboxykinase of the fungal pathogen Candida
RT   albicans.";
RL   Gene 192:235-240(1997).
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   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC       family. {ECO:0000305}.
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DR   EMBL; U70473; AAC49763.1; -; Genomic_DNA.
DR   VEuPathDB; FungiDB:CAWG_01381; -.
DR   VEuPathDB; FungiDB:CR_00200W_A; -.
DR   UniPathway; UPA00138; -.
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   CDD; cd00484; PEPCK_ATP; 1.
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   TIGRFAMs; TIGR00224; pckA; 1.
DR   PROSITE; PS00532; PEPCK_ATP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Decarboxylase; Gluconeogenesis; Lyase; Nucleotide-binding.
FT   CHAIN           1..553
FT                   /note="Phosphoenolpyruvate carboxykinase (ATP)"
FT                   /id="PRO_0000203870"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         255..262
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   553 AA;  60802 MW;  DF61449D2302CA7D CRC64;
     MAPPTAVGSS INFEGHPTIK STQDPLVQKL SLNTDTVIRH NAPPPTLYED GLLEKGTTIS
     STGALMAYSG NKTGRSPKDK RIVDESTSSH NIWWGPVNKQ VGELTWEISR SRALDYLRTR
     EKLFVVDAYA GWDPSYRIKV RIICARAYHA LFMTNMLIRP TEEELKNFGE PDFTIYNAGQ
     FPANIHTKGM TSATSVEINF KDMEMVILGT EYAGEMKKGI FTVMFYLMPI KHKVLTLHSS
     CNQGVEKGDV TLFFGLSGTG KTTLSADPQR KLIGDDEHCW SDNGVFNIEG GCYAKCLDLS
     AEKEPEIFNS IKFGAILENV VYXXITKVVD YGDSSITENT RCAYPIDFIP SAKIPCLPTP
     IPQYYLLTCD ASGVLATVSK LTNAQVMYHF ISGYTSKMAG SEEGVTEPHA TFSACFGQPF
     LVLHPMKYAQ QLADKISEHN ANAWLLNTGW VGSSVAQGGG KRCPLKYTRA ILDAIHSGEL
     SKVEYEKVPV FNLNVPTSCP GVPSEILNPT KAWTQGTDSF NKEIKSLATK FAENFKTYAD
     QATAEVKAAG PEA