ID D6ZX83_BIFLJ Unreviewed; 917 AA. AC D6ZX83; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAR-2024, entry version 68. DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419}; GN OrderedLocusNames=BLJ_0033 {ECO:0000313|EMBL:ADG99529.1}; OS Bifidobacterium longum subsp. longum (strain JDM301). OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=759350 {ECO:0000313|EMBL:ADG99529.1, ECO:0000313|Proteomes:UP000006740}; RN [1] {ECO:0000313|EMBL:ADG99529.1, ECO:0000313|Proteomes:UP000006740} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JDM301 {ECO:0000313|EMBL:ADG99529.1, RC ECO:0000313|Proteomes:UP000006740}; RX PubMed=20525832; DOI=10.1128/JB.00538-10; RA Wei Y.X., Zhang Z.Y., Liu C., Zhu Y.Z., Zhu Y.Q., Zheng H., Zhao G.P., RA Wang S., Guo X.K.; RT "Complete genome sequence of Bifidobacterium longum JDM301."; RL J. Bacteriol. 192:4076-4077(2010). CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source CC for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670}. CC -!- CATALYTIC ACTIVITY: CC Reaction=oxaloacetate + phosphate = hydrogencarbonate + CC phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452, CC ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31; CC Evidence={ECO:0000256|ARBA:ARBA00001071}; 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; CP002010; ADG99529.1; -; Genomic_DNA. DR RefSeq; WP_013139971.1; NC_014169.1. DR AlphaFoldDB; D6ZX83; -. DR KEGG; bll:BLJ_0033; -. DR HOGENOM; CLU_006557_2_0_11; -. DR Proteomes; UP000006740; Chromosome. DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:InterPro. DR GO; GO:0015977; P:carbon fixation; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1. DR InterPro; IPR021135; PEP_COase. DR InterPro; IPR018129; PEP_COase_Lys_AS. DR InterPro; IPR033129; PEPCASE_His_AS. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1. DR PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1. DR Pfam; PF00311; PEPcase; 2. DR PRINTS; PR00150; PEPCARBXLASE. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. DR PROSITE; PS00781; PEPCASE_1; 1. DR PROSITE; PS00393; PEPCASE_2; 1. PE 4: Predicted; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Pyruvate {ECO:0000313|EMBL:ADG99529.1}. FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 180 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10111" FT ACT_SITE 579 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10112" SQ SEQUENCE 917 AA; 102621 MW; 9CA5100286F48434 CRC64; MATPEEQITP ADAAIVTTGT GRKGPEEHDL PESLKYDMDL CLEILRNVLG EYNPELLSTF DTVRHYAVEA SAEHFAELKD PNPDQDGLKE AVNVIDNMTL HDAQLLARAF ATYFHLANLS EENYRVSVLH ERENNVSVDQ AVDPINELTV AYHQLINETG PAKAKELLNQ LEFHPVFTAH PTEARRKAVE GKIRRVSELL EEYKRLGGSD KKECLRRLYN EIDALFRTSP IALKKPTPVE EADTILDIFD NTLFNTIPKV YRRFDDWVLG DKAGLVEPAC PAFFHPGSWI GSDRDGNPNV TAKVSRAVAR KFSDHVIAAL EQATRTVGRN LTMEAETTPP SAELKSLWSH QKEMSERLTD KAALISTKEM HRAVMLVMAD RLHYTIERDA DLMYHSCDDF LADLKVVQRS LAAAGAKRSA YGPLQDLIWQ TETFGFHMVE MEFRQHSVVH ARALADIREH GLHGERGELQ PMTHEVLDTF RALGAIQKRN GLKAARRYII SFTKSAQNIK DVYELNRLAF SHPEDVPTID VIPLFEQLED LQNSVDVLEE MIKIPEVQAR LKATGNKLEV MLGYSDSSKD AGPTSATLAL HSAQERIAKW AESHDIDLTL FHGRGGAVGR GGGPANRAVL AQPVGSVKCR FKLTEQGEVI FARYGNPVLA IRHVESVAAA TLLQSAPSVE KRNTEMTERY ADMAAQLDEA AHNRFLDLLN TDGFAPWFSI VTPLTEIGLL PIGSRPAKRG LGAKSLDDLR TIPWIFSWAQ ARINLAAWYG LGTACEKFGD LETMRQAYEE WPLFSTFIDN IEMSIAKTDE RIARMYLALG DREDLNEKVL NEMELTRKWV LAIVGDKWPL QHRHVLGQAI RIRSPYVDAL SVTQVLALKS LRKKVDKEEL SQSQQAGFIY LILCTVSGVA AGLQNTG //