ID CAPP_AMAHP Reviewed; 964 AA. AC Q43299; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 16-JUN-2009, entry version 50. DE RecName: Full=Phosphoenolpyruvate carboxylase; DE Short=PEPCase; DE Short=PEPC; DE EC=4.1.1.31; OS Amaranthus hypochondriacus (Prince-of-Wales feather). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC Caryophyllales; Amaranthaceae; Amaranthus. OX NCBI_TaxID=28502; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Leaf; RA Rydzik E., Berry J.; RT "The C4 phosphoenolpyruvate carboxylase (PEPCase) from grain RT Amaranth."; RL (er) Plant Gene Register PGR95-135. CC -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) CC it forms oxaloacetate, a four-carbon dicarboxylic acid source for CC the tricarboxylic acid cycle. CC -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O + CC phosphoenolpyruvate + CO(2). CC -!- ENZYME REGULATION: By light-reversible phosphorylation (By CC similarity). CC -!- PATHWAY: Photosynthesis; C4 acid pathway. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the PEPCase type 1 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; Z68125; CAA92209.1; -; mRNA. DR EMBL; L49175; AAB18633.1; -; mRNA. DR HSSP; P04711; 1JQO. DR SMR; Q43299; 31-964. DR BRENDA; 4.1.1.31; 2722. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:EC. DR GO; GO:0015977; P:carbon utilization by fixation of carbon di...; IEA:UniProtKB-KW. DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR InterPro; IPR001449; PEP_COase. DR InterPro; IPR018129; PEP_COase_AS. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase_cat. DR Gene3D; G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1. DR Pfam; PF00311; PEPcase; 1. DR PRINTS; PR00150; PEPCARBXLASE. DR PROSITE; PS00781; PEPCASE_1; 1. DR PROSITE; PS00393; PEPCASE_2; 1. PE 2: Evidence at transcript level; KW Allosteric enzyme; Carbon dioxide fixation; Cytoplasm; Lyase; KW Phosphoprotein; Photosynthesis; Tricarboxylic acid cycle. FT CHAIN 1 964 Phosphoenolpyruvate carboxylase. FT /FTId=PRO_0000166656. FT ACT_SITE 172 172 By similarity. FT ACT_SITE 600 600 By similarity. FT MOD_RES 11 11 Phosphoserine (By similarity). SQ SEQUENCE 964 AA; 109480 MW; 3D49C2DE8BDE11B3 CRC64; MASGKVEKMA SIDAQLRLLA PKKVSEDDKL VEYDALLLDR FLDILESLHG SGIRETVQEL YEHAAEYERT HDTKKLEELG NLITSLDAGD SIVIAKSFSQ MLNLANLAEE VQLAYRRRIK KTKKGDFADE SSAITESDFE ETLRRLVDLK KSPEEIFATL KNQTVDLVLT AHPTQSVRRS LLQKHGRIRD CLSQLYAKDI SPDDKQELDE ALQRAIQAAF RTDEIRRVQP TPQDEMRMGM SYFHETIWKG VPKFLRRVDT ALKNIGINER VPYNVPLIQF SSWMGGDRDG NPRVTPEVTR DVVLLARMMA ANMYFTQITD LMFELSMWRC NDEVRARAQE LHSQSKSDAK HYIEFWKQIP LSEPYRVILG DVRDKLYNTR EHAHKLLANG SSDVPEESTF THIDQFLEPL ELCYKSLCAS GDQPIADGSL LDFMRQVSTF GLSLVKLDIR QESDRHTEVM DAITTHLGIG SYRSWSEEKR QEWLLSELRG KRPLFGSDLP MSYEVADAIG TFRVLAELPN DSFGAYIISM ATAPSDVLAV ELLQRECGIK KPLRVVPLFE KLADLQSAAA SMTRLFSIDW YKNRINGTQE VMIGYSDSGK DAGRLSAAWQ LYKVQEQLIQ VAKEYGVKLT MFHGRGGTVG RGGGPTHLAL LSQPPDTIHG SLRVTIQGEV IEQSFGEEHL CFRTLERYTA ATLEHGIDPP TSPKPEWRAL MDEMAVITTK EYRSVVLQEP RFVEYFRSAT PELEYGRMNI GSRPAKRKPG GGIETLRAIP WIFSWTQTRF HLPVWLGCGA AFKHVIEKDI KNLAMLKDMY NQWSFFRVTI DLLEMVFAKG DPGIAALYDK LLVKDELKPF GENLRKSYLE AQKFLLEIAG HKDPLDADPY LKQILRLRDP YTTTLNVFQV YTLKRIRDPS FHVTVRPHLS KEMDANSLAA DLVKLNPTSE YPPGLEDTLI LTMKGIAAGM QNTG //