ID PCKA_NITSB Reviewed; 525 AA.
AC A6Q102;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
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=NIS_0043;
OS Nitratiruptor sp. (strain SB155-2).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Nautiliales;
OC Nitratiruptoraceae; Nitratiruptor.
OX NCBI_TaxID=387092;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB155-2;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00453};
CC Note=Binds 1 Mn(2+) ion per subunit. {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; AP009178; BAF69161.1; -; Genomic_DNA.
DR RefSeq; WP_011979587.1; NC_009662.1.
DR AlphaFoldDB; A6Q102; -.
DR SMR; A6Q102; -.
DR STRING; 387092.NIS_0043; -.
DR KEGG; nis:NIS_0043; -.
DR eggNOG; COG1866; Bacteria.
DR HOGENOM; CLU_018247_0_1_7; -.
DR InParanoid; A6Q102; -.
DR OrthoDB; 9806325at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001118; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
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; Cytoplasm; Decarboxylase; Gluconeogenesis; Lyase; Manganese;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..525
FT /note="Phosphoenolpyruvate carboxykinase (ATP)"
FT /id="PRO_1000026333"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 196
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 215
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 231..239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 252
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 441
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
SQ SEQUENCE 525 AA; 59153 MW; 6B802A6022DABDCA CRC64;
MEINDFDKLG IKDVKKVYYN PDYETLFQKE LEQQEGVETT LGAVAVDTGI FTGRSPKDKY
FVKQPPSEKY IAWGDINQPI SKEIFDELFE KTKEYLSGKE LYVMDAFAGA SDDSKKAIRV
VTEIAWQAHF VKNMFIRPTE EELQNFHPDF TLYVAANLKN DRYKEHGLNS DVFIIFNIEE
NIAIIGGTWY GGEIKKGIFS MMNYWLPLEG KLSMHCSANI GDKDDVALFF GLSGTGKTTL
SADPNRRLIG DDEHGWDDNG VFNFEGGCYA KVIGLDPEKE PDIYAAIKRD ALLENVVVKE
NGEVDFEDSS KTENTRVSYP IYHICKHKED LQGPHPKNII FLSADAFGVL PPVSKLTKEQ
AMYYFLSGYT AKVAGTERGI TEPVATFSAC FGEAFLPLHP TVYAKLLGEK IDKHGVNVYL
VNTGWTGGPY GIGQRMSLPA TRSCINAILN GSITQSEYEI LPIFNLEIPT YVEGVDPAIL
NPRNTWEDKE AYDRQLEHLA KLFIDNFKRY EGYGNFDYSK AGPQL
//
