CAPP_THES7
ID CAPP_THES7 Reviewed; 857 AA.
AC P51060;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Phosphoenolpyruvate carboxylase;
DE Short=PEPC;
DE Short=PEPCase;
DE EC=4.1.1.31;
GN Name=ppc;
OS Thermus sp. (strain 71).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus;
OC unclassified Thermus.
OX NCBI_TaxID=72595;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8543565; DOI=10.1093/oxfordjournals.jbchem.a124909;
RA Nakamura T., Yoshioka I., Takahashi M., Izui K.;
RT "Cloning and sequence analysis of the gene for phosphoenolpyruvate
RT carboxylase from an extreme thermophile, Thermus sp.";
RL J. Biochem. 118:319-324(1995).
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable. Retains almost full activity after 10 min at 65 degrees
CC Celsius.;
CC -!- SUBUNIT: Homotetramer.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR EMBL; D42166; BAA07723.1; -; Genomic_DNA.
DR AlphaFoldDB; P51060; -.
DR SMR; P51060; -.
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; PTHR30523; 1.
DR Pfam; PF00311; PEPcase; 1.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; SSF51621; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 1: Evidence at protein level;
KW Carbon dioxide fixation; Direct protein sequencing; Lyase; Magnesium.
FT CHAIN 1..857
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000166643"
FT ACT_SITE 144
FT /evidence="ECO:0000250"
FT ACT_SITE 530
FT /evidence="ECO:0000250"
SQ SEQUENCE 857 AA; 95633 MW; 14C72BC063A03F35 CRC64;
MSDPFEALKA EVDLLGRLLG EAIRKVSGER FFALVEEVRL LSKARRQGDG AAAEVLSQRV
ERMPVEEMEA LVRAFTHYFH LVNLAEERHR VRVNRLRTEG ETLENPRPEG FLALAKALKE
RGLSLEEAEA HLNRLALLLT FTAHPTETRR RTLRHHLERL QEELEGGDRE RLLARVVLLY
ATEEVRKARP SVEDEIKGGL YYLPTTLWRA IPKVVEGLEA ALERVYGKRP HLRSPVRFRS
WMGGDRDGNP YVTPEVTAFA GRYAREVAKG RYLEELEALV RDLSLSEARI PVPKEVREGG
EGVERFPGEP YRRYFAALYR ALEGEALSTE GLARALKVAE KGLEGVGLAQ VAQAFLRPLE
ARLSAFGLEL APLDLREESG KLLEAAAELL RLGGVHPDFL ALSPEEKEAL LTEELKTARP
LLPVGEVPQG EALRVALGAL RAWGDKGAHV VSMTHHPADL LAVFLLAREV GLYRPGKPLP
FDVVPLFETL EDLERAPEVL RRLLANPVFR AHAQGRGGVE VMIGYSDSNK DAGFLMANLA
LYQAQEALHA VGEAQGIPVF FFHGRGTSTA RGGGPAGRAI AGLPPKSVGH RLRLTEQGEA
LADRYAHPDL AVRHLEQLLY HFAQAALGDG VEPKAHWREA LGEAGERSMA RYRALLSQEG
FFPFFEAFTP IREIGELPIA SRPVYRHGRV RDIRDLRAIP WVMAWTQVRL LLPGWYGLSA
LEGLPMPLLR EMYREWPFFA TTLESAAMAL AKADLGIAER YLKLVPEGLQ GFYHHLAEEY
RRTVALLEAI FEAPLLHNQK TLERQIALRN PYVDPINFVQ VELLARYRAP GGREDEGVRR
ALLLSLLGVA AGLRNAG
