ID L0IDG6_HALRX Unreviewed; 503 AA.
AC L0IDG6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00012363};
DE EC=4.1.1.49 {ECO:0000256|ARBA:ARBA00012363};
GN OrderedLocusNames=Halru_1399 {ECO:0000313|EMBL:AGB16012.1};
OS Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halovivax.
OX NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB16012.1, ECO:0000313|Proteomes:UP000010846};
RN [1] {ECO:0000313|Proteomes:UP000010846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18193 / JCM 13892 / XH-70
RC {ECO:0000313|Proteomes:UP000010846};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Halovivax ruber XH-70.";
RL Submitted (SEP-2011) 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}.
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DR EMBL; CP003050; AGB16012.1; -; Genomic_DNA.
DR AlphaFoldDB; L0IDG6; -.
DR STRING; 797302.Halru_1399; -.
DR KEGG; hru:Halru_1399; -.
DR eggNOG; arCOG06073; Archaea.
DR HOGENOM; CLU_536211_0_0_2; -.
DR OrthoDB; 192074at2157; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000010846; Chromosome.
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; -; 2.
DR Gene3D; 3.40.449.10; Phosphoenolpyruvate Carboxykinase, domain 1; 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 Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW Kinase {ECO:0000313|EMBL:AGB16012.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:AGB16012.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010846};
KW Transferase {ECO:0000313|EMBL:AGB16012.1}.
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 55280 MW; BB31B93FBBB1A690 CRC64;
MSETGTEPPT YATRLPDPER ASNIRYNPTL TELRSLARDD ERTTEYGSPA YVSKYRSRSA
DRTKNAIDDE LTEADHSLVL DAVTSLSDRD LLCVDRLVGR HPDATYCCRL FVPTAYARIA
LTWAKLFEPT DGREPDFQTV QLPDAEETAI RIFPDEGTTA VLGSDYTGEA KKSFLRLFMY
RAKENGGLGL HAGSKRVTVT DDESTERTVG QLFLGLSATG KSTLTSHGCW LDEPEHAAML
QDDVCALLPD GSVAGSEGQG LYIKTHGLTQ SEQPALYDAA TAESAVFENV AVDEDGAVDF
EDDQYTANGR AVVQREELES AAEEIDLDGV DQIFFITRNP LMPPVTRLDD QQAAVAFMLG
ESIETSAGDP SRAGESIRVV GTNPFIIGPE GTEGNIFREL VRSLDVDCYV MNTGYIGQQT
VDIGVTESVT LLTEIARGTV EWRTDDRMGL TIPESVPGLD IEQFYVPDHV EDYDDARTAL
REERAAYLDS FPQLDDEIAD AVY
//
