ID A0A6J4K2D1_9BACT Unreviewed; 542 AA. AC A0A6J4K2D1; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 02-DEC-2020, entry version 2. DE RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00012363, ECO:0000256|HAMAP-Rule:MF_00453}; DE Short=PCK {ECO:0000256|HAMAP-Rule:MF_00453}; DE Short=PEP carboxykinase {ECO:0000256|HAMAP-Rule:MF_00453}; DE Short=PEPCK {ECO:0000256|HAMAP-Rule:MF_00453}; DE EC=4.1.1.49 {ECO:0000256|ARBA:ARBA00012363, ECO:0000256|HAMAP-Rule:MF_00453}; GN Name=pckA {ECO:0000256|HAMAP-Rule:MF_00453}; GN ORFNames=AVDCRST_MAG68-1670 {ECO:0000313|EMBL:CAA9293917.1}; OS uncultured Gemmatimonadetes bacterium. OC Bacteria; Gemmatimonadetes; environmental samples. OX NCBI_TaxID=203437 {ECO:0000313|EMBL:CAA9293917.1}; RN [1] {ECO:0000313|EMBL:CAA9293917.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AVDCRST_MAG68 {ECO:0000313|EMBL:CAA9293917.1}; RA Meier V. D.; RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes the conversion of CC oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct CC phosphoryl transfer between the nucleoside triphosphate and OAA. CC {ECO:0000256|HAMAP-Rule:MF_00453}. 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 ECO:0000256|HAMAP-Rule:MF_00453}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00453}; CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00453}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000256|ARBA:ARBA00004742, ECO:0000256|HAMAP-Rule:MF_00453}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00453}. CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP) CC family. {ECO:0000256|ARBA:ARBA00006052, ECO:0000256|HAMAP- CC Rule:MF_00453}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00453}. 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; CADCTW010000001; CAA9293917.1; -; Genomic_DNA. DR UniPathway; UPA00138; -. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IEA:UniProtKB-EC. DR CDD; cd00484; PEPCK_ATP; 1. DR Gene3D; 3.40.449.10; -; 1. DR Gene3D; 3.90.228.20; -; 1. DR HAMAP; MF_00453; PEPCK_ATP; 1. DR InterPro; IPR001272; PEP_carboxykinase_ATP. DR InterPro; IPR013035; PEP_carboxykinase_C. DR InterPro; IPR008210; PEP_carboxykinase_N. DR InterPro; IPR015994; PEPCK_ATP_CS. DR PANTHER; PTHR30031; PTHR30031; 1. DR Pfam; PF01293; PEPCK_ATP; 1. DR PIRSF; PIRSF006294; PEP_crbxkin; 1. DR SUPFAM; SSF68923; SSF68923; 1. DR TIGRFAMs; TIGR00224; pckA; 1. DR PROSITE; PS00532; PEPCK_ATP; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00453}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00453}; KW Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00453}; KW Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00453}; KW Kinase {ECO:0000313|EMBL:CAA9293917.1}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00453, KW ECO:0000313|EMBL:CAA9293917.1}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_00453}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00453}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00453}; Pyruvate {ECO:0000313|EMBL:CAA9293917.1}; KW Transferase {ECO:0000313|EMBL:CAA9293917.1}. FT NP_BIND 246..254 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT METAL 211 FT /note="Manganese" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453" FT METAL 230 FT /note="Manganese; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453" FT METAL 267 FT /note="Manganese" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453" FT BINDING 70 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453" FT BINDING 205 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453" FT BINDING 211 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453" FT BINDING 211 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453" FT BINDING 230 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453" FT BINDING 295 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453" FT BINDING 332 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453" FT BINDING 332 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453" FT BINDING 457 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453" SQ SEQUENCE 542 AA; 60089 MW; B3A25F8C40609F97 CRC64; MATTLNPSTD APAFGRESRH GLDNHGLRNP GTVFWNLTPA ELVEHAVQRR EGILVEGGPF NAVTRPHTGR SPNDKFVVRD ENTEADVWWG KVNQPISPEH YAALREDVLT HLEGQNLYVR DMWAGADPEY RLAVRVITPN AWHNLFANNM FRRPDDAELE AMVPGFTILH APEYEADPAR HGTRTSTFIL VNFTAKEIMI GGTRYAGELK KSIFSILNYL LPRQGVLAMH CSANIGPDGD TALFFGLSGT GKTTLSADPE RGLIGDDEHG WTDRGIFNFE GGCYAKAVKL SPEGEPEIYA TTRMFGTVLE NCIVDEKRRV DFDDISITEN TRISYPLHYI TNFVPDAQGG HPRNIVFLTA DAYGVLPPIS RLTPEQAMFY FLSGYTAKVA GTERGVKEPQ PTFSACFGQV FLPLHPGVYA DLLGQRIAEH GSRVWLVNTG WTGGPYGVGS RMKLSYTRAM VRAALAGELD DVETVESPFF RLHIPTSIPG VPSEVLVPRE TWADKDAFDK QARELADKFI QNFEQFADRV PEAVRTAGPR PA //