ID PCKG_ASCSU Reviewed; 643 AA. AC Q05893; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 16-JUN-2009, entry version 50. DE RecName: Full=Phosphoenolpyruvate carboxykinase [GTP]; DE Short=PEPCK; DE EC=4.1.1.32; DE AltName: Full=Phosphoenolpyruvate carboxylase; GN Name=PEPCK; OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides). OC Eukaryota; Metazoa; Nematoda; Chromadorea; Ascaridida; Ascaridoidea; OC Ascarididae; Ascaris. OX NCBI_TaxID=6253; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Nerve cord, and Pharynx; RX MEDLINE=93387435; PubMed=8375484; DOI=10.1006/expr.1993.1072; RA Geary T.G., Winterrowd C.A., Alexander-Bowman S.J., Favreau M.A., RA Nulf S.C., Klein R.D.; RT "Ascaris suum: cloning of a cDNA encoding phosphoenolpyruvate RT carboxykinase."; RL Exp. Parasitol. 77:155-161(1993). CC -!- FUNCTION: In parasitic nematodes PEPCK carboxylates CC phosphoenolpyruvate to oxaloacetate thus introducing the products CC of glycolysis to mitochondrial metabolism. 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 CC derived from the citric acid cycle (By similarity). CC -!- CATALYTIC ACTIVITY: GTP + oxaloacetate = GDP + phosphoenolpyruvate CC + CO(2). CC -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity). CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP] CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L01787; AAA29378.1; -; mRNA. DR HSSP; P35558; 1KHB. DR BRENDA; 4.1.1.32; 649. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) act...; IEA:EC. DR GO; GO:0006094; P:gluconeogenesis; IEA:InterPro. DR InterPro; IPR018091; PEP_carboxykin_GTP_CS. DR InterPro; IPR013035; PEP_carboxykinase_C. DR InterPro; IPR008209; PEP_carboxykinase_GTP. DR InterPro; IPR008210; PEP_carboxykinase_N. DR Gene3D; G3DSA:3.90.228.20; PEP_carboxykinase_C; 1. DR Gene3D; G3DSA:3.40.449.10; PEP_carboxykinase_N; 1. DR PANTHER; PTHR11561; PEP_carboxykin; 1. DR Pfam; PF00821; PEPCK; 1. DR PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1. DR ProDom; PD004738; PEPCK_N; 1. DR PROSITE; PS00505; PEPCK_GTP; 1. PE 2: Evidence at transcript level; KW Decarboxylase; GTP-binding; Lyase; Manganese; Metal-binding; KW Nucleotide-binding. FT CHAIN 1 643 Phosphoenolpyruvate carboxykinase [GTP]. FT /FTId=PRO_0000103632. FT NP_BIND 305 310 GTP (By similarity). FT NP_BIND 548 551 GTP (By similarity). FT REGION 422 424 Substrate binding (By similarity). FT ACT_SITE 306 306 By similarity. FT METAL 262 262 Manganese (By similarity). FT METAL 282 282 Manganese (By similarity). FT METAL 329 329 Manganese (By similarity). FT BINDING 102 102 Substrate (By similarity). FT BINDING 255 255 Substrate; via amide nitrogen (By FT similarity). FT BINDING 262 262 Substrate (By similarity). FT BINDING 304 304 Substrate (By similarity). FT BINDING 424 424 GTP (By similarity). FT BINDING 455 455 GTP (By similarity). SQ SEQUENCE 643 AA; 72230 MW; A9C369959AA79E27 CRC64; MRCRSLSHFK DDDFAVVSEV VTHKQNHIPV IKGDFVSLPK HVQRFVAEKA ELMKPSAIFI CDGSQNEADE LIARCVERGV LVPLKAYKNN YLCRTDPRDV ARVESKTWMI TPEKYDSVCH TPEGVKPMMG QWMSPDEFGK ELDDRFPGCM AGRTMYVIPY SMGPVGGPLS KIGIELTDSD YVVLCMRIMT RMGEPVLKAL AKNNGEFVRC VHSVGQPKPV ATKVINHWPC NPEKTIIAHR PAEREIWSFG SGYGGNSLLG KKCFALRIAM NIGYDEGWMA EHMLIMGVTS PKGEERFVAA AFPSACGKTN LAMLEPTIPG WKVRVIGDDI AWMKFGADGR LYAINPEYGF FGVAPGTSHK TNPMAMASFQ ENTIFTNVAE TADGEYFWEG LEHEVKNPKV DMINWLGEPW HIGDESKAAH PNSRFTAPAG QCPIIHPDWE KPEGVPIDAI IFGGRRPEGV PLVFESRSWV HGIFVGACVK SEATAAAEHT GKQVMHDPMA MRPFMGYNFG RYMRHWMKLG QPPHKVPKIF HVNWFRQSAD HKFLWPGYGD NIRVIDWILR RCSGDATIAE ETPIGFIPKK GTINLEGLPN VNWDELMSIP KSYWLEDMVE TKTFFENQVG SDLPPEIAKE LEAQTERIKA LKE //