ID F8H5J5_STUS2 Unreviewed; 879 AA. AC F8H5J5; A0A137XUR1; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAR-2024, entry version 73. 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=PSTAB_2731 {ECO:0000313|EMBL:AEJ06012.1}; OS Stutzerimonas stutzeri (strain ATCC 17588 / DSM 5190 / CCUG 11256 / JCM OS 5965 / LMG 11199 / NBRC 14165 / NCIMB 11358 / Stanier 221) (Pseudomonas OS stutzeri). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Stutzerimonas. OX NCBI_TaxID=96563 {ECO:0000313|EMBL:AEJ06012.1, ECO:0000313|Proteomes:UP000008932}; RN [1] {ECO:0000313|EMBL:AEJ06012.1, ECO:0000313|Proteomes:UP000008932} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17588 / DSM 5190 / CCUG 11256 / JCM 5965 / LMG 11199 / RC NCIMB 11358 / Stanier 221 {ECO:0000313|Proteomes:UP000008932}; RX PubMed=21994926; DOI=10.1128/JB.06061-11; RA Chen M., Yan Y., Zhang W., Lu W., Wang J., Ping S., Lin M.; RT "Complete Genome Sequence of the Type Strain Pseudomonas stutzeri CGMCC RT 1.1803."; RL J. Bacteriol. 193:6095-6095(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17588; RA Yan Y., Chen M., Lu W., Zhang W., Ping S., Lin M.; RT "Complete Genome Sequence of Pseudomonas stutzeri Strain CGMCC 1.1803."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Proteomes:UP000008932} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17588 / DSM 5190 / CCUG 11256 / JCM 5965 / LMG 11199 / RC NCIMB 11358 / Stanier 221 {ECO:0000313|Proteomes:UP000008932}; RA Yan Y., Chen M., Lu W., Zhang W., Ping S., Lin M.; RT "Complete genome sequence of Pseudomonas stutzeri strain CGMCC 1.1803."; RL Submitted (JUN-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; CP002881; AEJ06012.1; -; Genomic_DNA. DR AlphaFoldDB; F8H5J5; -. DR SMR; F8H5J5; -. DR KEGG; psz:PSTAB_2731; -. DR HOGENOM; CLU_006557_2_0_6; -. DR Proteomes; UP000008932; 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:AEJ06012.1}. FT ACT_SITE 141 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10111" FT ACT_SITE 546 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10112" SQ SEQUENCE 879 AA; 97821 MW; 06C443CBFB4FFB90 CRC64; MAKIIDARLR DNVHLLGELL GNTIRAQHGD QFFDKIERIR KGAKAARKGS AEGAQLLAET LDSLDESELL PMTRAFNQFL NLANIAEQYH QVRRRAAGEP APFEIGVFAD LIERLKAAGH DNEFIARQVS RLEIELVLTA HPTEVSRRTL IQKYDAIAQQ LAARDHTDLS DAERASIELS LQRLIAEVWH TEEIRRNRPT PVEEAKWGFA AIENSLWKAV PNVLRQTDAT LHRLTGLHLP LEAAPIRFAS WMGGDRDGNP NVTAMVSREV LLTARWVAAD LYLREIEGLI TALSMREASD ELLRQSGDSA EPYRVLLKPL RQRLRATREW ARAAIEHGQP APAEVLQDCA ELRRPLELCY RSLHACGMGV IADGALLDCL RRLAVFGLFL VRLDIRQDAA RHAAALAEIT DYLGLGDYQQ WDEQKRLDWL QHELANRRPL LPAHYHPSAD TAEVLATCAV IAEAPAASLG SYVISMAHAA SDVLAVQLLL KEAGLQRPMR VVPLFETLDD LNNAAPTIDR LLSLPGYRQR LHGPQEVMIG YSDSAKDAGT TAAAWAQYRA QEQLVEVCRE HGVELLLFHG RGGTVGRGGG PAHAAILSQP PGSVAGRFRT TEQGEMIRFK FGLPDIAEQN LNLYLAAVLE ATLLPPPPPE PGWRETMDRL AAEGVAAYRG VVREHPLFVD YFRQATPELE LGRLPLGSRP AKRREGGVES LRAIPWIFAW TQTRLMLPAW LGWEQALHGA LQRGEGERLA EMRARWPFFS TRIDMLEMVL AKADADIARR YDERLVQPEL LSLGSDLRDR LSQVIEAVLS LTGQSDLLDH SPKTQEAFSL RNTYLDPLHL MQIELLARSR QRQGPAESPL EQALLVSVAG IAAGLRNTG //