ID D5TZI6_THEAM Unreviewed; 630 AA. AC D5TZI6; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAR-2024, entry version 69. 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 OrderedLocusNames=Tagg_0003 {ECO:0000313|EMBL:ADG90286.1}; OS Thermosphaera aggregans (strain DSM 11486 / M11TL). OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Thermosphaera. OX NCBI_TaxID=633148 {ECO:0000313|EMBL:ADG90286.1, ECO:0000313|Proteomes:UP000002376}; RN [1] {ECO:0000313|EMBL:ADG90286.1, ECO:0000313|Proteomes:UP000002376} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376}; RX PubMed=21304709; RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A., RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Brettin T., RA Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E., RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Thermosphaera aggregans type strain (M11TL)."; RL Stand. Genomic Sci. 2:245-259(2010). RN [2] {ECO:0000313|Proteomes:UP000002376} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376}; RX DOI=10.4056/sigs.821804; RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A., RA Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.C., Brettin T., RA Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E., RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.-P.; RT "Complete genome sequence of Thermosphaera aggregans type strain RT (M11TLT)."; RL Stand. Genomic Sci. 2:245-259(2010). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 11486; RG US DOE Joint Genome Institute (JGI-PGF); RA Spring S., Lapidus A., Munk C., Schroeder M., Glavina Del Rio T., Tice H., RA Copeland A., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J., RA Jeffries C.C., Brettin T., Detter J.C., Tapia R., Han C., Chain P., RA Heimerl T., Weik F., Goker M., Rachel R., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.; RT "Complete genome sequence of Thermosphaera aggregans type strain (M11TL)."; RL Submitted (FEB-2010) 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; Evidence={ECO:0000256|HAMAP- CC 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 --------------------------------------------------------------------------- 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; CP001939; ADG90286.1; -; Genomic_DNA. DR RefSeq; WP_013128879.1; NC_014160.1. DR AlphaFoldDB; D5TZI6; -. DR STRING; 633148.Tagg_0003; -. DR GeneID; 9165007; -. DR KEGG; tag:Tagg_0003; -. DR eggNOG; arCOG05865; Archaea. DR HOGENOM; CLU_028872_1_1_2; -. DR OrthoDB; 55875at2157; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000002376; Chromosome. 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:ADG90286.1}; 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:ADG90286.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002376}; KW Transferase {ECO:0000313|EMBL:ADG90286.1}. FT DOMAIN 36..246 FT /note="Phosphoenolpyruvate carboxykinase GTP-utilising N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF17297" FT DOMAIN 251..610 FT /note="Phosphoenolpyruvate carboxykinase C-terminal P-loop" FT /evidence="ECO:0000259|Pfam:PF00821" FT ACT_SITE 279 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452" FT BINDING 94 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452" FT BINDING 227..229 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452" FT BINDING 236 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452" FT BINDING 255 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452" FT BINDING 278..283 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452" FT BINDING 295 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452" FT BINDING 391..393 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452" FT BINDING 393 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452" FT BINDING 424 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452" SQ SEQUENCE 630 AA; 72093 MW; 04EF80C467CDB31E CRC64; METQGFCTES LNALKPYMSS RELGKLARIR DCSLVEWIRQ VVEHLKPSSI FINTGSEEDL DYIRRRAVEN KEEYVSSYNQ LHTVHFDGVR DLARDRGNTK IMTGKGVKIP LVNSGEREEL KKEVWEIYRD IMRGKEMFIG FYCFGPRGSP FTLYGVQVTD SAYVVHSENI LYRVCYDEFT RNDRIEYMRF LHSSGERDEN GWSKNISKRR IYIDPEEMIT YSVNTQYAGN TVGLKKLSLR LCVYKGFREG WLCEHMFIIG MKGSGDRVAY FTGAFPAGCG KTSTALIADL VVGDDLAIIR NVDGVARAVN PEVGMFGIID GVNPVDDAEI YKILTSRTSE VIFANVLYTE DGDVWWNGKE GAPKPGVNYA GEWWPGKRDE NGNPIPPSHP NARFTTSIFY LSRVDPRIND PMGVPVSGMI FGGRDSDTWV PVEEAFDWFH GIVTKGASLE SERTTAVLGQ AGVREFNPFA ILDFLSISPG AFIDLHFRFA RELSQSPKVY GVNYFLRGED GRFLTEKVDK RVWLRWMEKR VHGELDAVET PTGYIPIYSD LVDLFNKELG KEFPESLYEK LFTVRVKQHL DKIERIWRIY AEIPDTPALF FSILKEEKQR LVNARNRFGD FISPFRLDRA //