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Database: UniProt
Entry: L9Y681_9EURY
LinkDB: L9Y681_9EURY
Original site: L9Y681_9EURY 
ID   L9Y681_9EURY            Unreviewed;       503 AA.
AC   L9Y681;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00012363};
DE            EC=4.1.1.49 {ECO:0000256|ARBA:ARBA00012363};
GN   ORFNames=C489_04798 {ECO:0000313|EMBL:ELY69247.1};
OS   Natrinema versiforme JCM 10478.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=1227496 {ECO:0000313|EMBL:ELY69247.1, ECO:0000313|Proteomes:UP000011632};
RN   [1] {ECO:0000313|EMBL:ELY69247.1, ECO:0000313|Proteomes:UP000011632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10478 {ECO:0000313|EMBL:ELY69247.1,
RC   ECO:0000313|Proteomes:UP000011632};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:ELY69247.1}.
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DR   EMBL; AOID01000016; ELY69247.1; -; Genomic_DNA.
DR   RefSeq; WP_006430018.1; NZ_AOID01000016.1.
DR   AlphaFoldDB; L9Y681; -.
DR   STRING; 1227496.C489_04798; -.
DR   PATRIC; fig|1227496.3.peg.964; -.
DR   OrthoDB; 192074at2157; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000011632; 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   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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW   Kinase {ECO:0000313|EMBL:ELY69247.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ELY69247.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyruvate {ECO:0000313|EMBL:ELY69247.1};
KW   Transferase {ECO:0000313|EMBL:ELY69247.1}.
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          470..497
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   503 AA;  55681 MW;  6244E1BC1E24124E CRC64;
     MSESGTETRP LVRQLPDPTT ASNVRYNPSL EELRELAAPA ETTTEFGSAS YVSEARSRSA
     DLTKNAVDDD FTDRDHDLVD DAIDLVGDRE MLCVDRLMGR HSDATFCCRL FVPVEHARIA
     YAWASLFEPT DGRDPDLYTV HLPDYDETAI RVRPDTGVTT VLGTDYIGEA KKSFLRLYMY
     RIKQQGGLGL HAGSKRVRVR DADGELQTVG QVFMGLSATG KSTLTSHGCW LEEPEDAAML
     QDDVCGLLSD GSVAGSEGEG LFIKTIGLDE DEQPELYEAA TSESAILENV AVDDDGTVHF
     DEDRYTANSR AIIRRDELES AADEIDLDRM DQAFFITRNP LMPPVAKLDE EQAAVAFMLG
     ESIETSAGDP SRAGESIRVV GTNPFIIGPE GEEGNIFHEL IDILDVDCYV INTGYLGEQS
     KDIGVTESVT ILTETARGTI EWTHDERTGL TIPDSVPGLD IEDYYVPDHV DDYDDAVAEL
     RADRREYLEQ FDELREEIRD AVY
//
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