ID E8U9H7_DEIML Unreviewed; 826 AA. AC E8U9H7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 64. 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 OrderedLocusNames=Deima_2073 {ECO:0000313|EMBL:ADV67716.1}; OS Deinococcus maricopensis (strain DSM 21211 / LMG 22137 / NRRL B-23946 / OS LB-34). OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae; OC Deinococcus. OX NCBI_TaxID=709986 {ECO:0000313|EMBL:ADV67716.1, ECO:0000313|Proteomes:UP000008635}; RN [1] {ECO:0000313|EMBL:ADV67716.1, ECO:0000313|Proteomes:UP000008635} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34 RC {ECO:0000313|Proteomes:UP000008635}; RX PubMed=21677853; DOI=10.4056/sigs.1633949; RA Pukall R., Zeytun A., Lucas S., Lapidus A., Hammon N., Deshpande S., RA Nolan M., Cheng J.F., Pitluck S., Liolios K., Pagani I., Mikhailova N., RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Brambilla E.M., Rohde M., Goker M., Detter J.C., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Deinococcus maricopensis type strain (LB- RT 34)."; RL Stand. Genomic Sci. 4:163-172(2011). RN [2] {ECO:0000313|Proteomes:UP000008635} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34 RC {ECO:0000313|Proteomes:UP000008635}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Kyrpides N., RA Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Zeytun A., RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Pukall R., Gehrich-Schroeter G., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Deinococcus maricopensis DSM 21211."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. 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; CP002454; ADV67716.1; -; Genomic_DNA. DR RefSeq; WP_013557221.1; NC_014958.1. DR AlphaFoldDB; E8U9H7; -. DR STRING; 709986.Deima_2073; -. DR KEGG; dmr:Deima_2073; -. DR eggNOG; COG2352; Bacteria. DR HOGENOM; CLU_006557_2_0_0; -. DR OrthoDB; 9768133at2; -. DR Proteomes; UP000008635; 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 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 Pyruvate {ECO:0000313|EMBL:ADV67716.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008635}. FT ACT_SITE 131 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10111" FT ACT_SITE 503 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10112" SQ SEQUENCE 826 AA; 91101 MW; 429DB5B7E2F1AC22 CRC64; MGIREDVNTL GRALGQVLKE QEGEAFFDTV ERVRALVRQA RAGDGDAPLR ELLEGATPED AENLVRAFSL YFQLVNLAEE YERVRTLAGR EGVRPQSLEA ALTELHASGL SADDAEALIQ RVNLGLTFTA HPTEMRRRTV RAHLVQVARD IPDLSDPTTY DAAVERITAH VEALWNTPEL RRLKPTVLDE VKGGLSYVPS IAQAVTRLQR DLQRAFERVY GRPTSARVPL SLHSWMGGDR DGNPFVTPDA TRDTLTLHRD RARDLLLNAI RQTYADLSQD ERGEETYRAE LQALHDAVQA GQHVDLTAQL DALDARLREH GQARSADVLL APLRTHARTF GQHLVSLDIR EHSALTGAAA AALLDAAGMP GYADLPEHAK TELLTRELRS RRPLWPAGEA LPEELERAVG PIREVARAVR KVGPRAFGRY IISMSESVSD VLEPLLLARE VGFRVLPVPL FETLDDLERA PSVVWELLSL PEYRAVLGSD VQEIMLGYSD SNKDAGFLAA NWALHEAQRR LADVCRRAGV PWRFFHGRGT SIGRGGGPAS RAILGQPAGT IGSGLRITEQ GEALADKYSH PVLAHRNLEQ ALSGLLLAAA RPAADLPAAW TEALDRAARA SAGAYRALVT TPEFLPFFEA ATPIHEISRL NIASRPVRRP GAPTLQNLRA IPWVMSWTQN RANLPGWYGL REGLREIGVP LARELYAQWP FFRSMLDNAQ MSLAKSDLLI FDEYLTLGGP ALGPDLKAAY ADTVALVQDI VGADLLRNEP RLHESIGLRN PYIDPIHRLQ VELLRRARRE DGGLDRYERP LLLSVQGIAA GVRNTG //