ID   E6V2K2_VARPE            Unreviewed;       947 AA.
AC   E6V2K2;
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=Varpa_1512 {ECO:0000313|EMBL:ADU35723.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU35723.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Ovchinnikova G., Orwin P., Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU35723.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU35723.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium Variovorax
RT   paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-e00813(2013).
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; CP002417; ADU35723.1; -; Genomic_DNA.
DR   RefSeq; WP_013539966.1; NC_014931.1.
DR   AlphaFoldDB; E6V2K2; -.
DR   STRING; 595537.Varpa_1512; -.
DR   KEGG; vpe:Varpa_1512; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000008917; 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:ADU35723.1}.
FT   ACT_SITE        154
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        599
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   947 AA;  104659 MW;  75A6A0E59497708E CRC64;
     MKASKTPALP KRRQAEDQPL IDDIRLLGRI LGDVIREQEG DETYALVEKI RTLSVAFRRD
     ADQAADRALK NLLKGLSAAE TVRVIRAFTY FSHLANLAED RHQIRRRTEA DREGVLADGD
     LQTALARIRK AGVKPDEIVA SLAHSYVSPV LTAHPTEVQR KSILDAERAI ALLLTTRDEI
     KLRQSAYASG KDALSPIELA DNETQMRTRV TQIWQTRLLR FSKLTVADEI ENALSYYEAT
     FLREIPRVYA DLEKALTQGG HTPSVAPFLR MGQWIGGDRD GNPNVTAETL EYALGRQAEL
     ALRLYLTEVH YLGGELSLSA TLVDVSVEMQ ALAERSPDTS EHRKDEPYRR ALTGVYARLA
     ATLRELTGGE AARHAVAPQN PYAKAEEFLA DLRTVEESLG EKHGSVLAAP RLRPLIRAVE
     VFGFHLATVD LRQSSDKHEA VIAELLATAR IEPSYASLAE EAKQTLLLKL LDDARPLRVP
     DADYSPLAKS ELAIFAAART ARARYGAAAI RHYIISHTET VSDLLEALLL QKEVGLLRGA
     MATNAVCDLI VVPLFETIED LRNAAPIVRA FYALPNIQAL IERSGGEQDV MLGYSDSNKD
     GGIFTSNWEL YRAGIALVSL FDELNKKKAN PIRLRMFHGR GGTVGRGGGP SYQAILAQPP
     GTVRGQIRLT EQGEVIGSKY ANREIGRRNL ETLVAATLEA TLLPQGKSAP ATFLSAASEL
     SAASMAAYRK LVYETPGFGD YFFGSTPIRE IAELNIGSRP ASRNPSHKID DLRAVPWSFS
     WGQCRLTIPG WFGFGAGVEQ FLASAGNAAG KKERVALLQR MYAQWPFFRT LLSNMDMVLA
     KSDLALASRY AELVTDRKLR QKVFSMIDAE WHRTSDALTL ITGAKQRLEG NAEMQRSVRH
     RFPYIDPLHH LQVELMRRYR AGDGGERLQR GIHISINGVA AGLRNTG
//