ID A0A133UNP1_9EURY Unreviewed; 632 AA.
AC A0A133UNP1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Phosphoenolpyruvate carboxykinase [GTP] {ECO:0000256|HAMAP-Rule:MF_00452};
DE Short=PEP carboxykinase {ECO:0000256|HAMAP-Rule:MF_00452};
DE Short=PEPCK {ECO:0000256|HAMAP-Rule:MF_00452};
DE EC=4.1.1.32 {ECO:0000256|HAMAP-Rule:MF_00452};
DE AltName: Full=GTP-dependent phosphoenolpyruvate carboxykinase {ECO:0000256|HAMAP-Rule:MF_00452};
DE Short=GTP-PEPCK {ECO:0000256|HAMAP-Rule:MF_00452};
GN Name=pckG {ECO:0000256|HAMAP-Rule:MF_00452};
GN ORFNames=AKJ65_00435 {ECO:0000313|EMBL:KXA95832.1};
OS candidate division MSBL1 archaeon SCGC-AAA259E19.
OC Archaea; Euryarchaeota; candidate division MSBL1.
OX NCBI_TaxID=1698264 {ECO:0000313|EMBL:KXA95832.1, ECO:0000313|Proteomes:UP000070284};
RN [1] {ECO:0000313|EMBL:KXA95832.1, ECO:0000313|Proteomes:UP000070284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC-AAA259E19 {ECO:0000313|EMBL:KXA95832.1};
RX PubMed=26758088; DOI=10.1038/srep19181;
RA Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT pools of the Red Sea.";
RL Sci. Rep. 6:19181-19181(2016).
CC -!- FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to
CC phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic
CC pathway that produces glucose from lactate and other precursors derived
CC from the citric acid cycle. {ECO:0000256|HAMAP-Rule:MF_00452}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00452};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00452};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00452};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|HAMAP-Rule:MF_00452}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00452}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC family. {ECO:0000256|ARBA:ARBA00005796, ECO:0000256|HAMAP-
CC Rule:MF_00452}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00452}.
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:KXA95832.1}.
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DR EMBL; LHXO01000003; KXA95832.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133UNP1; -.
DR PATRIC; fig|1698264.3.peg.864; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000070284; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
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 Gene3D; 2.170.8.10; Phosphoenolpyruvate Carboxykinase, domain 2; 1.
DR HAMAP; MF_00452; PEPCK_GTP; 1.
DR InterPro; IPR018091; PEP_carboxykin_GTP_CS.
DR InterPro; IPR013035; PEP_carboxykinase_C.
DR InterPro; IPR008209; PEP_carboxykinase_GTP.
DR InterPro; IPR035077; PEP_carboxykinase_GTP_C.
DR InterPro; IPR035078; PEP_carboxykinase_GTP_N.
DR InterPro; IPR008210; PEP_carboxykinase_N.
DR PANTHER; PTHR11561; PHOSPHOENOLPYRUVATE CARBOXYKINASE; 1.
DR PANTHER; PTHR11561:SF0; PHOSPHOENOLPYRUVATE CARBOXYKINASE (GTP)-RELATED; 1.
DR Pfam; PF00821; PEPCK_GTP; 1.
DR Pfam; PF17297; PEPCK_N; 1.
DR PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR SUPFAM; SSF68923; PEP carboxykinase N-terminal domain; 1.
DR SUPFAM; SSF53795; PEP carboxykinase-like; 1.
DR PROSITE; PS00505; PEPCK_GTP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00452};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_00452}; Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00452};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00452}; Kinase {ECO:0000313|EMBL:KXA95832.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00452};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00452};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00452};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00452}; Pyruvate {ECO:0000313|EMBL:KXA95832.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070284};
KW Transferase {ECO:0000313|EMBL:KXA95832.1}.
FT DOMAIN 37..249
FT /note="Phosphoenolpyruvate carboxykinase GTP-utilising N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF17297"
FT DOMAIN 254..614
FT /note="Phosphoenolpyruvate carboxykinase C-terminal P-loop"
FT /evidence="ECO:0000259|Pfam:PF00821"
FT ACT_SITE 282
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 230..232
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 239
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 258
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 281..286
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 299
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 394..396
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 396
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 427
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
SQ SEQUENCE 632 AA; 72997 MW; BE2E08A9D0BE03C8 CRC64;
MRDLLPRTKN KEKLLKDKCK QDGFCKLENL NNPKVTDFIA RYLEHCNPDS AFVRTDSQKD
VEYIRKRSIE KGEERQLEMD GHTVHFDGYN DQARDKENTK FLLPPDKEIG RQFNSINKEK
GLKEIRKYLE NIMKGKEAYI CFFCLGPKNS KFSIPALQIT DSTYVAHSED ILYRDGYDLF
KNRKFENEVE FFKFVHSAGP LEGGVSKKIH KRRIYTDLEA NTVFSTHTQY GGNTIGAKKL
AMRLAIKKAS EEGWLTEHMF IMGVHGDEDR TTYFTGAYPS ACGKTSTSMI ESEKLVGDDI
AYLREINGEL RAANPERGIF GIIRDVSPDD DPLIWKTITT PGEVIFSNVL IKDGKPYWMG
MGKELPEKGI NHSGKWWKGK KDESGKPIDP SHRNARYTVR ISDLENKDPN LENPDGVKIK
GIIYGGRDSD TWVPVSESFN WKHGILTKGS ALESETTSAT LGKSGTRRFN PMSNLDFLSI
KIRKYIKNQI RFGERLNNPP SIFSVNYFLK DENDEYLNGI HDKKVWLKWM ELRTHKEVAA
VKTPTGYIPK YDDLEGLFEN VLGKNYSRKD YTKQFSTRIP EHLAKIERIK TIYKERVKRA
PEILFEELEK QKKRLEKAKE KYGNYVDPEN FC
//
