ID A0A031LR41_9CREN Unreviewed; 604 AA.
AC A0A031LR41;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=CM19_04795 {ECO:0000313|EMBL:EZQ09964.1};
OS Candidatus Acidianus copahuensis.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=1160895 {ECO:0000313|EMBL:EZQ09964.1, ECO:0000313|Proteomes:UP000024332};
RN [1] {ECO:0000313|EMBL:EZQ09964.1, ECO:0000313|Proteomes:UP000024332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALE1 {ECO:0000313|EMBL:EZQ09964.1,
RC ECO:0000313|Proteomes:UP000024332};
RA Urbieta M.S., Rascovan N., Castro C., Revale S., Giaveno M.A.,
RA Vazquez M.P., Donati E.R.;
RT "Draft genome sequence of the novel thermoacidophilic archaea Acidianus
RT copahuensis ALE1 strain, isolated from Copahue volcanic area in Neuquen
RT Argentina.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:EZQ09964.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JFZT01000036; EZQ09964.1; -; Genomic_DNA.
DR RefSeq; WP_048099254.1; NZ_JFZT01000036.1.
DR AlphaFoldDB; A0A031LR41; -.
DR STRING; 1160895.CM19_04795; -.
DR OrthoDB; 55875at2157; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000024332; 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; -; 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_00452; PEPCK_GTP; 1.
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.
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:EZQ09964.1};
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:EZQ09964.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000024332};
KW Transferase {ECO:0000313|EMBL:EZQ09964.1}.
FT DOMAIN 30..225
FT /note="Phosphoenolpyruvate carboxykinase GTP-utilising N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF17297"
FT DOMAIN 230..586
FT /note="Phosphoenolpyruvate carboxykinase C-terminal P-loop"
FT /evidence="ECO:0000259|Pfam:PF00821"
FT ACT_SITE 257
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 206..208
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 215
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 234
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 256..261
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 272
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 368..370
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 370
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
SQ SEQUENCE 604 AA; 68197 MW; 9B751A0EDDDA2FC2 CRC64;
MKFSSAIYKK ISSAKLDSLL RLNNDSLLSF LDEMVSICEP ETVYIVENKD DAEYVKRKAI
DTGEEIPLKV EGHTIHFDPP QDQARARDDT FILGEKIPFV NTKPKEEGLE EVLSLLRGSM
NGREMFVGFY SLGPSGSPRR FLAVQISDSP YVIHSENILY RMSFSDFKGN IPFFKFVHSK
GELDIKKRRI VVDIENEIVY SVNTTYAGNS IGLKKLALRL TLNRAIKEGW LSEHMAIIGL
SGKDRDHYIT ASFPSGSGKT STSMIGKLIS DDLAIILNIN GEMRSWNPEI GVFGIIHGVN
QTDDPIIWDV LNSPGEVIFS NVLMKDDGTV YWQGNGEKEP DKGINFAGNW WKGKTDKNGN
IIPPSHPNAR FTAPITSFKN VDLNYDNPKG VVVEGIIFGV KDFTTLVPIA EAFNWEHGVI
TMGASMESAR TSAVVGKTDE MEFNPMAIID FMSIHIGKYL ENYLAFGKSL KNPPKIFGAN
YFLKNEKGVF LNSKDDKKVW LSWITKRIEE KSDAIETPVG LIPVYSDLRE IFVEVLGKEY
TKKDYETQFS IRLTKYKEKF ERIRGIYSKV DGMPDEVNKA LDEQIERINK YIKKYGDVVS
PFNL
//
