ID   Q126H5_POLSJ            Unreviewed;       970 AA.
AC   Q126H5;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 105.
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=Bpro_3665 {ECO:0000313|EMBL:ABE45567.1};
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE45567.1, ECO:0000313|Proteomes:UP000001983};
RN   [1] {ECO:0000313|Proteomes:UP000001983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX   PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE45567.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q126H5; -.
DR   STRING; 296591.Bpro_3665; -.
DR   KEGG; pol:Bpro_3665; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   Proteomes; UP000001983; 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   Reference proteome {ECO:0000313|Proteomes:UP000001983}.
FT   REGION          26..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        183
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        624
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   970 AA;  107864 MW;  7D128990C08C3D82 CRC64;
     MLACEVQEQV QNQRVEMVIS ARARKVSENA KDGTPGKTGT RARDNERPLV EDIRLLGRIL
     GDVIREQEGV TAYELIEQVR KLSVAFRRDA DQEADKALKK LLKGLSGEQT VSVIRAFTYF
     SHLANLAEDR HHIRRRAVHE RAGDTQEGSI EVALARLRWA GISPKTIATT LAHSFVSPVL
     TAHPTEVQRK SILDAERDIA QLLTARDDIK ALALATNAAK DALTPRELAA NEAQLRARVM
     QLWQTRLLRF SKLTVADEIE NALSYYEATF LREIPKLYAN LERELGNQPV HSFLRMGQWI
     GGDRDGNPNV SADTLNYALA RQAEVALRHY LTEVHYLGGE LSLSAMLVAV SPGMQALAES
     SPDTNEHRKD EPYRRALTGV YARLAATLKE LTGGEAARHA VAPQNAYARA EDFLADLRTI
     ETSLRSNHGE ALIAQRLHPL IRAVEVFGFH LATVDLRQSS DKHEEVVAEL LAVARIEPRY
     PSLDEAAKRA LLIRLLNDAR PLRVISTIYS AHAQSELAIF EAARTARARF GKEAIRHYII
     SHTETVSDLL EVLLLQKEVG LMHRTLDDKA TNDLIVVPLF ETIEDLRNAA PIMREYYALP
     GIAQLVQRSG AEQDIMLGYS DSNKDGGIFT SNWELYRAEI ALVELFDQLA NSHNIQLRMF
     HGRGGTVGRG GGPSYQAILA QPPGTVRGQI RLTEQGEVIG SKYANPEIGR RNLETLVAAT
     LEATLLQPTK PATKAFLQAA AELSQASMAA YRALVYDTPG FNEYFFGATP IREIAELNIG
     SRPASRKASQ KIEDLRAIPW GFSWGQCRLT LPGWYGFGAA IEKMLDAGGT PATRKEALAL
     LQKMYKQWPF FRTLLSNMDM VLAKSDLALA SRYAELVADA RLRKKVFTAI EAEWHRTAEA
     LTLITGEKQR LAGNAALQRS IRHRFPYIDP LHHLQVELVR RYREGKADQK VQTGIHISIN
     GIAAGLRNTG
//