ID   D5W4Q5_PARAM            Unreviewed;      1072 AA.
AC   D5W4Q5;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 72.
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=BC1002_0773 {ECO:0000313|EMBL:ADG14870.1};
OS   Paraburkholderia atlantica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=2654982 {ECO:0000313|EMBL:ADG14870.1, ECO:0000313|Proteomes:UP000002190};
RN   [1] {ECO:0000313|EMBL:ADG14870.1, ECO:0000313|Proteomes:UP000002190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCGE1002 {ECO:0000313|EMBL:ADG14870.1,
RC   ECO:0000313|Proteomes:UP000002190};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ovchinnikova G., Martinez-Romero E., Hernandez M.A.R.,
RA   Tiedje J.M., Woyke T.;
RT   "Complete sequence of chromosome 1 of Burkholderia sp. CCGE1002.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG14870.1, ECO:0000313|Proteomes:UP000002190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCGE1002 {ECO:0000313|EMBL:ADG14870.1,
RC   ECO:0000313|Proteomes:UP000002190};
RX   PubMed=23209196; DOI=10.1128/JB.01756-12;
RA   Ormeno-Orrillo E., Rogel M.A., Chueire L.M., Tiedje J.M.,
RA   Martinez-Romero E., Hungria M.;
RT   "Genome Sequences of Burkholderia sp. Strains CCGE1002 and H160, Isolated
RT   from Legume Nodules in Mexico and Brazil.";
RL   J. Bacteriol. 194:6927-6927(2012).
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; CP002013; ADG14870.1; -; Genomic_DNA.
DR   RefSeq; WP_013088759.1; NC_014117.1.
DR   AlphaFoldDB; D5W4Q5; -.
DR   STRING; 640511.BC1002_0773; -.
DR   KEGG; bge:BC1002_0773; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   Proteomes; UP000002190; Chromosome 1.
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}.
FT   REGION          1..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        282
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        724
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1072 AA;  117851 MW;  A976EF9514FAC546 CRC64;
     MTSSGSARPA RRNTASPTAR PADAAAPDVL SDAAAHGRSS SVADQRAKRR AIAAQAAKAS
     KASQTTVPVK QDKAQKAPKA GKAEKAATSA TASKPAKVKI KVDGDATPPR AAKAERLEAM
     PQAESAAAPT VKNGGGRTRE DKDHPLFQDI RYLGRLLGDV LREQEGDAVF DVVETIRQNA
     VRFRREDDSA AAQTLDKKLR SLTPEQTVSV VRAFSYFSHL ANIAEDRHRN RRHRIHALAG
     SASQPGTIAH ALERLVAAGA AATPVLQRFF DDALIMPVLT AHPTEVQRKS ILDAQHDIAR
     LLAERDQPLT NRERAHNEAM LRARVTSLWQ TRMLRDARLT VADEIENALS YYRSTFLEEL
     PALYADIEEA LKEHGLEARL PPFFQMGSWI GGDRDGNPNV TAETLENAIT RQAAVIFEHY
     LVQVHKLGEE LSMSNVLVGV SDALNELADI SPDHSPHRTD EPYRRALIGI YTRLAASARV
     RLGEGSVPLR SAGRGVAPIR ATPYDDAADF VRDLHVLIDS LAEHHGAPLA APRLAPLARA
     AEVFGFHLAS IDLRQSSDIH EAVIAELLKR AGVEDDYAGL SEANKLKVLL AELAQPRALR
     VPYAEYSDLV KSELAVLEEA RITREKFGAR AVRNYIISHT ETVSDLVEVM LLQKETGLLL
     GHLGDEHDPA RASLMVIPLF ETIPDLRNAP HIMRDLIALP GIGALIEHQG NEQEVMLGYS
     DSNKDGGFLT SNWELYRAEL ALVSLFNERG VTLRLFHGRG GTVGRGGGPT YQAILSQPPG
     TVAGQIRLTE QGEVIASKFA NPEIGRRNLE TVVAATLEAS LLPHDHTLAE LPVYEETMQQ
     LSDTAMAAYR ALVYETPGFK EYFFESTPIA EIAELNIGSR PASRKLQDPK QRKIEDLRAI
     PWGFSWGQCR LLLTGWYGFG SAVTEHLDSA PSDAERARRL ALLKKMHKSW PFFANLMSNM
     DMVIAKTDLA VASRYAALVT DKKLRKHVFE RIVAEWERTS KVLSEITGKS ERLAENPLLA
     RSIKNRFPYL DPLNHLQVEL LKRYRAGDTN ARVRRGIHLC INGIAAGLRN TG
//