ID   E6VGS8_RHOPX            Unreviewed;       936 AA.
AC   E6VGS8;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
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=Rpdx1_3760 {ECO:0000313|EMBL:ADU45325.1};
OS   Rhodopseudomonas palustris (strain DX-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=652103 {ECO:0000313|EMBL:ADU45325.1, ECO:0000313|Proteomes:UP000001402};
RN   [1] {ECO:0000313|Proteomes:UP000001402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DX-1 {ECO:0000313|Proteomes:UP000001402};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Misra M., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Logan B., Oda Y., Harwood C.,
RA   Woyke T.;
RT   "Complete sequence of Rhodopseudomonas palustris DX-1.";
RL   Submitted (DEC-2010) 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}.
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DR   EMBL; CP002418; ADU45325.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6VGS8; -.
DR   STRING; 652103.Rpdx1_3760; -.
DR   KEGG; rpx:Rpdx1_3760; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   OrthoDB; 9768133at2; -.
DR   BioCyc; RPAL652103:RPDX1_RS18545-MONOMER; -.
DR   Proteomes; UP000001402; 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:ADU45325.1}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        598
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   936 AA;  104089 MW;  F0D9A15A3D2F8EE8 CRC64;
     MSSLNLSAGA EPVSERPDDA AAIEAETRLR NDIRLLGRIL GDTVREQEGQ SVFDLVENIR
     QTSIRFHRDD DKTARAELAA ILDGMSIPDT MRIVRAFSYF SHLANIAEDQ NNIRQMRAGS
     TAGSAPRAGL LAKTLAHARQ EGISAAELRK FFATALVSPV LTAHPTEVRR KSTMDREMQI
     ASLLDQRDRV QLTADEWADN EERLRRAVET LWKTNLLRRT KLTVLDEVTN GLSFYDYTFL
     REVPRLHSAL EDRLADAAKA EGVNSEGELA SFLRMGSWIG GDRDGNPFVT AEVLHGTLKL
     QSTRVLRYYL EELHELGSEL SLASHLAGIT DTVKALAEIS PDTSPHRKYE PYRLAVSGIY
     ARLAATALAL EVENLRAPVG EAAPYASAQD FKADLDAIHL SLTQHNSGVI ARGRLRQLRR
     AIDCFGFHLA CLDMRQNSAV HERTVGELMD AARPGTSYAV LDEEARIALL IAELRSTRPL
     TSMFVKYSDE TVGELSVFRE AAKAHATYGA AAIPQCIISM TKGVSDLLEV AVLLKEVGLI
     DPSGRSAINV VPLFETIEDL QACAKIMDRL LAIPEYRRLV DSRGSVQEVM LGYSDSNKDG
     GFVTSGWELY KAEIGLIEIF EHHGVRLRLF HGRGGSVGRG GGPSYDAIVA QPGGAVNGQI
     RITEQGEIIT SKYSNVEVGR NNLEILAAAT LEASLLQPKR VAPHRDYLEA MEQLSALAFK
     AYRGLVYETD GFVDYFWAST VINEISTLNI GSRPASRKKT RAIEDLRAIP WVFSWAQCRL
     MLPGWYGFGS AVSAWVTAHP DKGIAFLQKM YQEWPFFRTL LSNMDMVLSK SSIGIASRYA
     ELVEDVDVRE RIFGRIRAEW HSSIEYLFAI MQQDRLLQSN PLLERSIRHR FPYLDPLNHV
     QVQLLREHRT HDPDEQVLRG VQLTINGISA GLRNSG
//