ID   PCKA_AERPE              Reviewed;         489 AA.
AC   Q9YG68;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000255|HAMAP-Rule:MF_00453};
DE            Short=PCK {ECO:0000255|HAMAP-Rule:MF_00453};
DE            Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00453};
DE            Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00453};
DE            EC=4.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00453};
GN   Name=pckA {ECO:0000255|HAMAP-Rule:MF_00453}; OrderedLocusNames=APE_0033.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes the conversion of
CC       oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct
CC       phosphoryl transfer between the nucleoside triphosphate and OAA.
CC       {ECO:0000255|HAMAP-Rule:MF_00453}.
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:0000255|HAMAP-Rule:MF_00453};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC       family. {ECO:0000255|HAMAP-Rule:MF_00453}.
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DR   EMBL; BA000002; BAA78942.2; -; Genomic_DNA.
DR   PIR; D72755; D72755.
DR   AlphaFoldDB; Q9YG68; -.
DR   SMR; Q9YG68; -.
DR   STRING; 272557.APE_0033.1; -.
DR   EnsemblBacteria; BAA78942; BAA78942; APE_0033.1.
DR   KEGG; ape:APE_0033.1; -.
DR   eggNOG; arCOG06073; Archaea.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000002518; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.228.20; -; 2.
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   Pfam; PF01293; PEPCK_ATP; 1.
DR   PIRSF; PIRSF006294; PEP_crbxkin; 1.
DR   SUPFAM; SSF68923; SSF68923; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Decarboxylase; Gluconeogenesis; Lyase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..489
FT                   /note="Phosphoenolpyruvate carboxykinase (ATP)"
FT                   /id="PRO_0000203861"
FT   BINDING         53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         208..216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         258
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         300
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         300
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         409..410
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         415
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
SQ   SEQUENCE   489 AA;  54971 MW;  7591B394F7875811 CRC64;
     MEDVVKALAK EVLSSADIEW NPPPGLLRRE SSRYAGFTKT GSLAVVSSKA RARRPDRTRV
     KYLRDEGFDR LVVDAWDYVV KASFYAVERC VGSGDRRFRI LALVEKSYPH LALMSHLNFF
     PCGSTGSYDM VTIDVPSYSD VWMLVERRSN STLVLGSDYY GELKMSFLRL AMNEARDRHL
     GVGLHAASKL YRVRVEGSMR EVGVLVFGLS GTGKTTLTVE DHGLREPEYV RVMQDDIVIL
     DWRGVAHGTE MNLYPKTDSV PELKKLEPAV LHPDAVLENV VVKSDGTPDF TDLSLTRNAR
     ALAIREAIPI ASGSVDLMGT NVLVFLTRRP EMPPLARLTS PYQAVAYFML GESFRTSAEA
     GKPEPVRVPG FDPFMLEPKW RSAYSLLDLI KSLNMNVYVM NTGHAKDRKI PPELSKHLLL
     SLVKENVDWK LDKHMGFEIA VRAGGVNLDG YNPEELYGES YVRVVDLLRR DRQEFLRSIP
     SVSFLADYV