ID   F8FZW6_PSEP6            Unreviewed;       875 AA.
AC   F8FZW6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 59.
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=PPS_1156 {ECO:0000313|EMBL:AEJ11731.1};
OS   Pseudomonas putida (strain DSM 28022 / S16).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1042876 {ECO:0000313|EMBL:AEJ11731.1, ECO:0000313|Proteomes:UP000000502};
RN   [1] {ECO:0000313|EMBL:AEJ11731.1, ECO:0000313|Proteomes:UP000000502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S16 {ECO:0000313|EMBL:AEJ11731.1,
RC   ECO:0000313|Proteomes:UP000000502};
RX   PubMed=21914868; DOI=10.1128/JB.05663-11;
RA   Yu H., Tang H., Wang L., Yao Y., Wu G., Xu P.;
RT   "Complete genome sequence of the nicotine-degrading Pseudomonas putida
RT   strain S16.";
RL   J. Bacteriol. 193:5541-5542(2011).
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; CP002870; AEJ11731.1; -; Genomic_DNA.
DR   RefSeq; WP_013971224.1; NC_015733.1.
DR   AlphaFoldDB; F8FZW6; -.
DR   KEGG; ppt:PPS_1156; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000000502; 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:AEJ11731.1}.
FT   ACT_SITE        137
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        542
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   875 AA;  96978 MW;  C72BD41F0194BFA3 CRC64;
     MTDIDVRLRE DVHVLGELLG DTIRLQHGEA FLQKIEDIRH SAKADRRSAG EQLSSTLADL
     ADEDLLPVAR AFNQFLNLAN MAEQYQLIRR RDADHPEPFE ARVLPELLAR LKQAGHSNDA
     LARQLAKLDI QLVLTAHPTE VARRTLIQKY DAIAGQLAAQ DHRDLTPGER QQVRERLRRL
     IAEAWHTEEI RRTRPTPVDE AKWGFAVIEH SLWHAIPSHL RKVDKALLEA TGLRLPLEAA
     PIRFASWMGG DRDGNPNVTA AVTREVLLLA RWMAADLFLR DIDALASELS MQQADDALRE
     QVGDSAEPYR SLLKQLRDRL RATRAWAHSA LTSSQPASAE VLVDNRDLIA PLELCYQSLH
     ACGMGVIAEG PLLDCLRRAV TFGLFLGRLD VRQDAARHRD ALSEITDYLG LGRYADWDEE
     QRIEFLQAEL KNRRPLLPAH FKPQADTAEV LATCREIAAA PAASLGSYVI SMAGAASDVL
     AVQLLLKEAG LTRPMRVVPL FETLADLDNA GPVMQRLLGL PGYRANLRGP QEVMIGYSDS
     AKDAGTTAAA WAQYRAQENL VRICAEHQVE LLLFHGRGGT VGRGGGPAHA AILSQPPGSV
     AGRFRTTEQG EMIRFKFGLP GIAEQNLNLY LAAVLEATLL PPPPPQPAWR EVMVQLAADG
     VKAYRGVVRE NPDFVEYFRQ STPEQELGRL PLGSRPAKRR AGGIESLRAI PWIFGWTQTR
     LMLPAWLGWE TALNNALARG QGELLAQMRE QWPFFRTRID MLEMVLAKAD AQIAEAYDER
     LVQPHLLPLG AHLRDLLSQS CQVVLGLTGQ PVLLAHSPET LEFISLRNTY LDPLHRLQAE
     LLARSRSREA ALDSPLEQAL LVTVAGIAAG LRNTG
//