ID   CAPP_THET2              Reviewed;         858 AA.
AC   Q72L05;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=TT_C0260;
OS   Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA   Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA   Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA   Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
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DR   EMBL; AE017221; AAS80608.1; -; Genomic_DNA.
DR   RefSeq; WP_011172711.1; NZ_CP133179.1.
DR   AlphaFoldDB; Q72L05; -.
DR   SMR; Q72L05; -.
DR   GeneID; 3169755; -.
DR   KEGG; tth:TT_C0260; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_0; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000000592; 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   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; Lyase; Magnesium.
FT   CHAIN           1..858
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166644"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        531
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   858 AA;  96534 MW;  D93E356DE0BB036F CRC64;
     MSQDPFALLK AEVDLLGRLL GEAIRTLSGE RFFALVEEVR ALAKARRQGD EAAGEALLAR
     VEGLSTEEAE ALVRAFTHYF HLVNLAEERH RVRVNRLRAQ AETLESPRPE GFLALAKALK
     ERGLSLEEAE AHLNRLELLL TFTAHPTETR RRTLRHHLEA LQRELEAGDR ERLAARVALL
     YGTEEVRKAR PTVEDEIKGG LYYLPTTLWE AVPRVVAGLE AALERVYGRR PRLKSPVRFR
     SWIGGDRDGN PFVTPEVTAF AGRYAREVAR RRFLEALEDL VRDLSLAEAR VPVPREVRER
     GEGVERFMGE PYRRYFAALY RALEREEATT EGLLAALKAA ERGLREVGLG RVAEAFLDPL
     EARLSAFGLE LAPLDLREES GRLLEAAAEL LRVGGVHPDF LALPQEERER LLTEELKTAR
     PLLPVGEAPE GEALRVALGA LKAWRDKGAH VVSMTHHPED LLAVFLLARE VGLYRPGRPL
     PFDVVPLFET LEDLRRAPGV LRRLLENPVF LAHARGRGGV EVMIGYSDSN KDAGFLMANL
     ALYEAQEALS RVGEEVGLPV YFFHGRGTST ARGGGPAGRA IASLPPRSVG RRIRLTEQGE
     ALADRYSHPD LAVRHLEQML YHFALAALGP GQEPEARWRE ALAQAAEEST RRYRALLQEE
     GFFDFFEAFT PIREIGELPI ASRPVYRRGR VRDIRDLRAI PWVMAWTQVR VLLPGWYGLS
     ALEELPLDLL REMYRGWPFF ASTLEAAAMA LAKADMGVAR LYLRLVPEPL RFFYRRLAEE
     HARTVALLEA VFQAPLLHNQ RTLERQIRLR NPYVDPINIV QVELLRRYRA PGGKEDEALR
     RALLLSILGV AAGLRNAG
//