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Database: UniProt
Entry: A0A2G9P496_9ARCH
LinkDB: A0A2G9P496_9ARCH
Original site: A0A2G9P496_9ARCH 
ID   A0A2G9P496_9ARCH        Unreviewed;       511 AA.
AC   A0A2G9P496;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00012363};
DE            EC=4.1.1.49 {ECO:0000256|ARBA:ARBA00012363};
GN   ORFNames=COT90_05550 {ECO:0000313|EMBL:PIN98163.1};
OS   Candidatus Diapherotrites archaeon CG10_big_fil_rev_8_21_14_0_10_31_34.
OC   Archaea; Candidatus Diapherotrites.
OX   NCBI_TaxID=1974406 {ECO:0000313|EMBL:PIN98163.1, ECO:0000313|Proteomes:UP000230773};
RN   [1] {ECO:0000313|EMBL:PIN98163.1, ECO:0000313|Proteomes:UP000230773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG10_big_fil_rev_8_21_14_0_10_31_34
RC   {ECO:0000313|EMBL:PIN98163.1};
RA   Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.,
RA   Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M.,
RA   Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT   "Depth-based differentiation of microbial function through sediment-hosted
RT   aquifers and enrichment of novel symbionts in the deep terrestrial
RT   subsurface.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001389};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC       family. {ECO:0000256|ARBA:ARBA00006052}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIN98163.1}.
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DR   EMBL; PFAI01000059; PIN98163.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G9P496; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000230773; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; 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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   InterPro; IPR001272; PEP_carboxykinase_ATP.
DR   InterPro; IPR013035; PEP_carboxykinase_C.
DR   InterPro; IPR008210; PEP_carboxykinase_N.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW   Kinase {ECO:0000313|EMBL:PIN98163.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyruvate {ECO:0000313|EMBL:PIN98163.1};
KW   Transferase {ECO:0000313|EMBL:PIN98163.1}.
FT   REGION          367..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   511 AA;  58307 MW;  2D92E905D315DB99 CRC64;
     MDKKTVIKKL EENCKIIKNI SPEELREIAK PMETTTEFGS ASYVTKIRNR SAKKTFIVPE
     IKLGIKQTPI KEKEAEELAE KVFEYLNDKE LIQINKTMCL NPKNEIECRL YVSKEQAKLA
     FMWNYMLYPS KEKEPEMISI HVPEWPETKI FCYPKQKITF CLGSDYFGEV KKSFLRMGML
     FHKEKTKGLG LHAGSKLLKV KNKNNELQEV GFIMFGLSGT GKTTLTIHNH ELTGEEGVSI
     RQDDVVFMDE KGFCAGTEFG FFIKTEGLDE SQKVLYEASV KPTAIFENVK VSENGKVDFK
     NLELTANGRG VLPRDSVEGA EKEIDLEKAH KIIFITRRED IVPVIAKLTP EQAAAYFMLG
     ESIETSAGDP TKAGQSKREV GTNPFITGKE EDEGNRLYEI LKNNKDIECF VMNTGGIGRT
     GFEKGKNISI KLSTDIMKFI AQGKIEWKKD SNWNYLVPKG IEGIDFSEFD PANYYSKEEF
     EEKVNKLLEE RKQWLAQFPG LKKEIVESIY K
//
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