ID D3VH32_XENNA Unreviewed; 879 AA. AC D3VH32; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 27-MAR-2024, entry version 75. DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595}; DE Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595}; DE Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595}; DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595}; GN Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595, GN ECO:0000313|EMBL:CBJ88317.1}; GN OrderedLocusNames=XNC1_0229 {ECO:0000313|EMBL:CBJ88317.1}; OS Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / CCUG 14189 / LMG OS 1036 / NCIMB 9965 / AN6). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Xenorhabdus. OX NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88317.1, ECO:0000313|Proteomes:UP000008075}; RN [1] {ECO:0000313|EMBL:CBJ88317.1, ECO:0000313|Proteomes:UP000008075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19061 / DSM 3370 / CCUG 14189 / LMG 1036 / NCIMB 9965 / RC AN6 {ECO:0000313|Proteomes:UP000008075}; RX PubMed=22125637; DOI=10.1371/journal.pone.0027909; RA Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E., RA Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L., RA Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J., RA Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P., RA Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R., RA Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S., RA Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R., RA Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C., RA van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B., RA Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S., RA Goodrich-Blair H.; RT "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus: RT convergent lifestyles from divergent genomes."; RL PLoS ONE 6:E27909-E27909(2011). CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source CC for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670, CC ECO:0000256|HAMAP-Rule:MF_00595}. 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, ECO:0000256|HAMAP- CC Rule:MF_00595}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP- CC Rule:MF_00595}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}. CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. CC {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}. 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; FN667742; CBJ88317.1; -; Genomic_DNA. DR AlphaFoldDB; D3VH32; -. DR STRING; 406817.XNC1_0229; -. DR KEGG; xne:XNC1_0229; -. DR eggNOG; COG2352; Bacteria. DR HOGENOM; CLU_006557_2_0_6; -. DR Proteomes; UP000008075; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule. DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1. 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; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1. DR PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1. DR Pfam; PF00311; PEPcase; 1. DR PRINTS; PR00150; PEPCARBXLASE. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. DR PROSITE; PS00781; PEPCASE_1; 1. DR PROSITE; PS00393; PEPCASE_2; 1. PE 3: Inferred from homology; KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP- KW Rule:MF_00595}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595}; KW Reference proteome {ECO:0000313|Proteomes:UP000008075}. FT ACT_SITE 137 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10111" FT ACT_SITE 545 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10112" SQ SEQUENCE 879 AA; 98605 MW; 81E50940A6F8C677 CRC64; MNQQYSAMRS NVSMLGKLLG DTIKEALGED ILDKVETIRK LSKSSRAGNE VHRQQLLSTL ENLSNDELLP VARAFNQFLN LANAAEQYHS ISPHGEAASN PVALAALFNR LKDKQFSNDD LVKAIDELAI ELVLTAHPTE IARRTLIHKL VEVNGCLAQL DHDDLADYER NNIMRRLRQL IAQSWHTDEI RKIRPTPIDE AKWGFAVVEN SLWEGVPAFL REFNEQLEES IGYSLPVEAV PVRFTSWMGG DRDGNPNVTA DITRHVLLLS RWKAADLFLK DIQILVSELS MSECTPEVRQ MAGGDHVLEP YREIAKQLRT QLSHTLAYLE KCLKGEQVLP PSDLLLHNEQ LWQPLYACYQ SLKACGMEII ANGQLLDTLR RIRCFGLCLV RIDIRQESTR HTDAIAELTQ YLEMGDYASW PEAEKQAFLL HELNSKRPLT PRDWQPSAET QEVFETCKVI AETPQDAIAA YVISMAKVPS DVLAVKLLLK EAGCSLSLPV APLFETLDDL NNAESVIRKL LGITWYRELI QDKQMVMIGY SDSAKDAGVM AASWAQYQAQ DALIKVCEQE GVTLTLFHGR GGTIGRGGAP AHSALLSQPP GSLKGGLRVT EQGEMIRFKF GLPQVAISSL ALYASAILEA NLLPPPEPKP EWRQIMGILS DVSCNMYRDY VREQPEFVPY FRAATPEQEL AKLPLGSRPA KRRPTGGVES LRAIPWIFAW TQNRLMLPTW LGAGAALQQV IDAGKLSVLT DMSRDWPFFN TRIAMLEMVF AKADLWLAEY YDQRLVDPKL WPLGLKLRNQ LAEDIKTVLT ISQDEQLMAD LPWIAESIAL RNVYTDPLNV LQVELLQRSR QQEEALDPHL EQALMVTIAG VAAGMRNTG //