ID E2JE39_AMAHP Unreviewed; 964 AA. AC E2JE39; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 25-MAY-2022, entry version 31. DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305}; DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305}; GN Name=pepc {ECO:0000313|EMBL:ADO15315.1}; OS Amaranthus hypochondriacus (Prince-of-Wales feather) (Amaranthus hybridus OS var. hypochondriacus). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC Caryophyllales; Amaranthaceae; Amaranthus. OX NCBI_TaxID=28502 {ECO:0000313|EMBL:ADO15315.1}; RN [1] {ECO:0000313|EMBL:ADO15315.1} RP NUCLEOTIDE SEQUENCE. RA Bai Y., Zhang W., Li P.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}. CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. CC {ECO:0000256|ARBA:ARBA00008346}. 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; HQ186302; ADO15315.1; -; mRNA. DR SMR; E2JE39; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR HAMAP; MF_00595; PEPcase_type1; 1. DR InterPro; IPR021135; PEP_COase. DR InterPro; IPR022805; PEP_COase_bac/pln-type. DR InterPro; IPR018129; PEP_COase_Lys_AS. DR InterPro; IPR033129; PEPCASE_His_AS. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR PANTHER; PTHR30523; PTHR30523; 1. DR Pfam; PF00311; PEPcase; 1. DR PRINTS; PR00150; PEPCARBXLASE. DR SUPFAM; SSF51621; SSF51621; 1. DR PROSITE; PS00781; PEPCASE_1; 1. DR PROSITE; PS00393; PEPCASE_2; 1. PE 2: Evidence at transcript level; KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300}; KW Lyase {ECO:0000256|ARBA:ARBA00023239}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Pyruvate {ECO:0000313|EMBL:ADO15315.1}. FT ACT_SITE 172 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10111" FT ACT_SITE 600 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10112" SQ SEQUENCE 964 AA; 109653 MW; 5F980B49CB173EE1 CRC64; MASGKLEKMA SIDAQLRLLA PKKVSEDDKL VEYDALLLDR FLDILESLHG SGIRETVQEL YEHAAEYERT HDTKKLEELG NLITSLDAGD SIVIAKSFSQ MLNLANLAEE VQLAYRRRIK KTKKGDFADE SSAITESDFE ETLRRLVDLK ESPEEIFATL KNQTVDLVLT AHPTQSVRRS LLQKHGRIRD CLSQLYAKDI TPDDKQELDE ALQREIQAAF RTDEIRRVQP TPQDEMRMGM SYFHETIWKG VPKFLRRVDT ALKNIGINER VPYNVPLIQF SSWMGGDRDG NPRVTPEVTR DVVLLARMMA ANMYFTQITD LMFELSMWRC NDEVRARAQE LRSQSKSDAK HYIEFWKQIP LSEPYRVILG DVRDKLYNTR EHAHQLLANG ASDVPEESTF THIDQFLEPL ELCYKSLCAS GDRPIADGSL 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 ATLEHGMHPP TSPKPEWRAL MDEMAVITTK EYRSVVLQEP RFVEYFRSAT PELEYGRMNI GSRPAKRKPG GGIETLRAIP WIFSWTQTRF HLPVWLGCGA AFKHVIEKDI KNLAMLKDMY NQWSFFRVTI DLLEMVFAKG DPGIAALYDK LLVKDELKPF GENLRKSYLE AQKFLLEIAG HKDPLDADPY LKQILRLRDP YTTTLNVFQV YTLKRIRDPS FHVTVRPHLS KEMDANSLAA ELVKLNPTSE YPPGLEDTLI LTMKGIAAGM QNTG //