ID   K0IDF0_9BURK            Unreviewed;       929 AA.
AC   K0IDF0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 60.
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   ORFNames=C380_18335 {ECO:0000313|EMBL:AFU47361.1};
OS   Acidovorax sp. KKS102.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU47361.1, ECO:0000313|Proteomes:UP000006306};
RN   [1] {ECO:0000313|EMBL:AFU47361.1, ECO:0000313|Proteomes:UP000006306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KKS102 {ECO:0000313|EMBL:AFU47361.1,
RC   ECO:0000313|Proteomes:UP000006306};
RX   PubMed=23209225; DOI=10.1128/JB.01848-12;
RA   Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT   "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT   Polychlorinated-Biphenyl Degrader.";
RL   J. Bacteriol. 194:6970-6971(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}.
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DR   EMBL; CP003872; AFU47361.1; -; Genomic_DNA.
DR   RefSeq; WP_015015327.1; NC_018708.1.
DR   AlphaFoldDB; K0IDF0; -.
DR   STRING; 358220.C380_18335; -.
DR   KEGG; ack:C380_18335; -.
DR   PATRIC; fig|358220.3.peg.3734; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000006306; 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:AFU47361.1}.
FT   ACT_SITE        144
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        585
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   929 AA;  103657 MW;  F8908C7E7086AAEE CRC64;
     MKRSDKDQPL IDDIRLLGRI LGDVIREQEG VEAYELVEQV RKLSVAFRRD ADQEADRALK
     KLLKSLSGDQ TVSVIRAFTY FSHLANLAED RHHIRRRAVH ERAGDTQEGS IEVALSRLRW
     AGIAPKTISQ TLAGSYVAPV LTAHPTEVQR KSILDAERDI AQLLATRDDI QVRAQLYNSA
     KDALTPRELA ANEALLRARV AQLWQTRLLR YSKLTVADEI ENALSYYEAT FLREIPKIYA
     DLENELGQYP VHSFLRMGQW IGGDRDGNPN VTAQTLQYAL SRQAEVALRH YLTEVHYLGG
     ELSLSARLVQ VSAEMEALAQ RSPDTNEHRV DEPYRRALTG IYARLAASLK DLTGGEAARH
     AVAPQNAYAS AEEFLADLRV IEASLKSHHG EALAAERLHP LIRAVQVFGF HLATVDLRQS
     SDKHEEVVAE LLAKARIEPN YASLQEAAKR ALLIKLLNDA RPLRVVGAEY SAHAQGELAI
     FETARVMRER FGHEAIRHYI ISHTETVSDL LEVLLLQKEV GLMSGTLDTE SKNHLIVVPL
     FETIEDLRNA APIMREFYAL PGVAALVQRS GGEQDIMLGY SDSNKDGGIF TSNWELYRAE
     IALVELFDEL ATSHGIQLRM FHGRGGTVGR GGGPSYQAIL AQPPGTVRGQ IRLTEQGEVI
     ASKYANPEIG RRNLETLVAA TLEATLLQPT KPATKAFLDA AAQLSLASMG SYRALVYETP
     GFTDYFFNST PIREIAELNI GSRPASRKAS QKIEDLRAIP WGFSWGQCRL TLPGWFGFGS
     AVEAFINTEG KDPKAQLALL QKMYRQWPFF RTLLSNMDMV LAKSDLALAS RYSELVTDAR
     LRKKVFTSIE AEWHRTADAL TRITGDKQRL THNTALARSI KHRFPYIDPL HHLQVELVRR
     WRAGQGDERV QTGIHISING IAAGLRNTG
//