ID Q0ICY4_SYNS3 Unreviewed; 1001 AA. AC Q0ICY4; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 108. 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:ABI46533.1}; GN OrderedLocusNames=sync_0460 {ECO:0000313|EMBL:ABI46533.1}; OS Synechococcus sp. (strain CC9311). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=64471 {ECO:0000313|EMBL:ABI46533.1, ECO:0000313|Proteomes:UP000001961}; RN [1] {ECO:0000313|EMBL:ABI46533.1, ECO:0000313|Proteomes:UP000001961} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC9311 {ECO:0000313|EMBL:ABI46533.1, RC ECO:0000313|Proteomes:UP000001961}; RX PubMed=16938853; DOI=10.1073/pnas.0602963103; RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H., RA Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S., RA Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R., RA Paulsen I.T.; RT "Genome sequence of Synechococcus CC9311: insights into adaptation to a RT coastal environment."; RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006). 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; CP000435; ABI46533.1; -; Genomic_DNA. DR AlphaFoldDB; Q0ICY4; -. DR STRING; 64471.sync_0460; -. DR KEGG; syg:sync_0460; -. DR eggNOG; COG2352; Bacteria. DR HOGENOM; CLU_006557_2_0_3; -. DR Proteomes; UP000001961; 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 Pyruvate {ECO:0000313|EMBL:ABI46533.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001961}. FT REGION 1..32 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 958..977 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7..22 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 961..976 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 187 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10111" FT ACT_SITE 643 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10112" SQ SEQUENCE 1001 AA; 112840 MW; 34237888CB62A6B2 CRC64; MIPSDSGFPS MHSSSALIPE STQPRADGNE AGGGQLLQQR LALVEDLWRT VLRSECPPEQ AEQLLRMKQL SDPVLPGEHP AGTDALIDLI KGMDLAEAIA AARAFSLYFQ LVNILEQRIE EDTYLESINR SQDQAEQFDP FAPPLATQTE PATFRELFER LRRLNVPPAQ LEALLQELDI RLVFTAHPTE IVRHTVRHKQ RRVASLLQQL ETQPPTPSGA TDSVRLQLEE EIRLWWRTDE LHQFKPSVLD EVDYALHYFQ QVLFNAMPQL RRRIVASLAA SYPDVRVPSS SFCTFGSWVG SDRDGNPSVT TEITWRTACY QRQLMLDRYI SAVQHLRNQL SISMQWSQVS PPLLESLEMD RLRFPDVYEE RATRYRLEPY RLKLSFVLER LRLTQLRNQQ LADAGWRTPP EGLPSFTPGN APGDALHYGS IAEFRSELEL IRTSLVNTDL SCEPLDTLLT QVHIFGFSLA GLDIRQESTR HSDALDELSR YINPDRAYGA MDEAERVAWL MEELQTRRPL IPPAVSWSAA TAETVDVFRM LHRLQDEFGS RICGTYVISM SHSVSDLLEV LLLAKEAGLV DPSARHADLL VVPLFETVED LQRAPEVMEH LFQTPLYRDL LPKVGTQGLL LQELMLGYSD SNKDSGFLSS NWEIHQAQIA LQDLASRQGI ALRLFHGRGG SVGRGGGPAY QAILAQPSGT LQGRIKITEQ GEVLASKYSL PELALYNLET VTTAVIQNSL VTNQLDATPS WNKLMSRVAK SSRRNYRALV HDNPDLVAFF QQVTPIEEIS KLQISSRPAR RKTGTRDLSS LRAIPWVFGW TQSRFLLPSW FGVGSALSEE LEADPDQLTL LRTLHQRWPF FRMLISKVEM TLSKVDLDLA RHYVTSLGSA EHHEAFEKIY ATVAEEYART KELVLAITGQ ERLLDADPAL QLSVDLRNRT IVPLGFLQVA LLRRLRDQNR QPPMSESPSS DGDGRTYSRS ELLRGALLTI NGIAAGMRNT G //