ID PCKG_SALTO Reviewed; 612 AA. AC A4X388; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 96. DE RecName: Full=Phosphoenolpyruvate carboxykinase [GTP] {ECO:0000255|HAMAP-Rule:MF_00452}; DE Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00452}; DE Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00452}; DE EC=4.1.1.32 {ECO:0000255|HAMAP-Rule:MF_00452}; GN Name=pckG {ECO:0000255|HAMAP-Rule:MF_00452}; GN OrderedLocusNames=Strop_0861; OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC OS 105044 / CNB-440). OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales; OC Micromonosporaceae; Salinispora. OX NCBI_TaxID=369723; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC 105044 / CNB-440; RX PubMed=17563368; DOI=10.1073/pnas.0700962104; RA Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W., RA Jensen P.R., Moore B.S.; RT "Genome sequencing reveals complex secondary metabolome in the marine RT actinomycete Salinispora tropica."; RL Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007). 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:0000255|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:0000255|HAMAP-Rule:MF_00452}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00452}; CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00452}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000255|HAMAP-Rule:MF_00452}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00452}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00452}. CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP] CC family. {ECO:0000255|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; CP000667; ABP53338.1; -; Genomic_DNA. DR RefSeq; WP_011904772.1; NC_009380.1. DR AlphaFoldDB; A4X388; -. DR SMR; A4X388; -. DR STRING; 369723.Strop_0861; -. DR KEGG; stp:Strop_0861; -. DR PATRIC; fig|369723.5.peg.879; -. DR eggNOG; COG1274; Bacteria. DR HOGENOM; CLU_028872_1_1_11; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000000235; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. 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 CDD; cd00819; PEPCK_GTP; 1. 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; 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; Decarboxylase; Gluconeogenesis; GTP-binding; Lyase; Manganese; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1..612 FT /note="Phosphoenolpyruvate carboxykinase [GTP]" FT /id="PRO_1000080989" FT ACT_SITE 274 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 82 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 221..223 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 230 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 250 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 272 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 273..278 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 297 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 387..389 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 389 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 420 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 517..520 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" SQ SEQUENCE 612 AA; 68188 MW; 6E8EF4A30279CA17 CRC64; MVAPATVRGI DQAPTSHPKL LAWVREIAEL TTPDRVVWAD GSEEEWRRIT DELVEAGTLV RLNPEKKRNS FYARTDPTDV ARVEERTFIC SVDEADAGPT NNWMAPAEMK RTMTELYRGC MRGRTMYVIP FCMGPVEAKN PMFGIEITDS PYVVASMRIM TRMGTKILEA MGDDADFVHA LHSIGAPLAP GQQDVSWPCN ETKYISHFPE TREIWSYGSG YGGNSLLGKK CYSLRIASVM GRDEGWLAEH MLILKITSPE GRAYHIAGAF PSACGKTNLA MLEPTIPGWK VETVGDDIAW MRFGPDGRLY AVNPEYGLFG VAPGTDWKTN ANAMRTLDRG NSIFTNVALT DDGDIWWEGM GEPPTHLIDW KGNDWTPQSE HLSSHANSRF CTPITQCPIL AEDYYDPNGV PIDAILFGGR RRDTVPLVTE ARDWVHGVYL GATLSSETTA AASGAVGVVR RDPMAMLPFI GYNAGDYFRH WIEMGKGTDG DESKLPSVYY VNWFRKDAEG SFLWPGFGEN SRVLKWIVER LEGRAEAVET PIGMVPAEDA LDVEGLDMTS EDIRIALKVD VNEWQAELPL VTEWFEKFGD KLPGVLWAEL DALRARLDAE PQ //