ID PCKG_CHLFF Reviewed; 600 AA. AC Q256B8; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 16-JUN-2009, entry version 22. DE RecName: Full=Phosphoenolpyruvate carboxykinase [GTP]; DE Short=PEP carboxykinase; DE Short=PEPCK; DE EC=4.1.1.32; DE AltName: Full=Phosphoenolpyruvate carboxylase; GN Name=pckG; OrderedLocusNames=CF0098; OS Chlamydophila felis (strain Fe/C-56). OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydophila. OX NCBI_TaxID=264202; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16766509; DOI=10.1093/dnares/dsi027; RA Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H., RA Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., RA Fukushi H., Hattori M., Kuhara S., Shirai M.; RT "Genome sequence of the cat pathogen, Chlamydophila felis."; RL DNA Res. 13:15-23(2006). 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 -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). 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; AP006861; BAE80870.1; -; Genomic_DNA. DR RefSeq; YP_515015.1; -. DR GeneID; 3959148; -. DR GenomeReviews; AP006861_GR; CF0098. DR KEGG; cfe:CF0098; -. DR HOGENOM; Q256B8; -. DR OMA; Q256B8; SHPNARF. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) act...; IEA:HAMAP. DR GO; GO:0006094; P:gluconeogenesis; IEA:HAMAP. DR HAMAP; MF_00452; -; 1. 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; Decarboxylase; Gluconeogenesis; KW GTP-binding; Lyase; Manganese; Metal-binding; Nucleotide-binding. FT CHAIN 1 600 Phosphoenolpyruvate carboxykinase [GTP]. FT /FTId=PRO_1000080984. FT NP_BIND 268 273 GTP (By similarity). FT NP_BIND 508 511 GTP (By similarity). FT REGION 381 383 Substrate binding (By similarity). FT ACT_SITE 269 269 By similarity. FT METAL 225 225 Manganese (By similarity). FT METAL 245 245 Manganese (By similarity). FT METAL 292 292 Manganese (By similarity). FT BINDING 76 76 Substrate (By similarity). FT BINDING 218 218 Substrate; via amide nitrogen (By FT similarity). FT BINDING 225 225 Substrate (By similarity). FT BINDING 267 267 Substrate (By similarity). FT BINDING 383 383 GTP (By similarity). FT BINDING 414 414 GTP (By similarity). SQ SEQUENCE 600 AA; 66477 MW; 52F3231C978B8B74 CRC64; MTSAWSNEIQ HEGLKQWIQE VAELVTPEDI RVCNGSDSEY AEVYSIMQKS GVAIPLNSDL HPNCFLVRSS PEDVARVEKF TFICTAKKEE AGPTNNWRDP QEMRQELQGL FRGCMRGRTL YVVPFCMGPL NSPFSLIGVE LTDSPYVVCS MKIMTRMGAE VLKSLGTSGT FHKCLHSVGV PLSPGEKDVA WPCNPEHMRI VHFQDDSSVM SFGSGYGGNA LLGKKCVALR LASYIARSKN WLAEHMLIIG VTNPEGQKKY FAASFPSACG KTNLAMLKPK IPGWKIECIG DDIAWIRPGS DGRLYAVNPE YGFFGVAPGT SEKTNPNALA TCRSNSIFTN VALTPDGDVW WEGLTSQPPA GLIDWRGNPW QPGGTPAAHP NSRFTTPLQQ CPVLDSQWNS SEGVPLEAII FGGRRSDTIP LVYEALSWQH GVTIGASMSS ATTAAIVGEQ GKLRHDPFAM LPFCGYNMAL YFDHWLSFAS NASLKLPKIY GVNWFRKDKD GNFIWPGFSE NLRVLEWIFR RTNGEESIAK RTPIGYLPEE SSLNLEGLNL SSQALQDLLA VDVPGWLKEV ADVREYCKIF GSDLPQIISD ELFRIERELK //