ID   H9ZSL5_THETH            Unreviewed;       858 AA.
AC   H9ZSL5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
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=TtJL18_1445 {ECO:0000313|EMBL:AFH39325.1};
OS   Thermus thermophilus JL-18.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=798128 {ECO:0000313|EMBL:AFH39325.1, ECO:0000313|Proteomes:UP000007388};
RN   [1] {ECO:0000313|EMBL:AFH39325.1, ECO:0000313|Proteomes:UP000007388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL-18 {ECO:0000313|EMBL:AFH39325.1,
RC   ECO:0000313|Proteomes:UP000007388};
RX   PubMed=23405355; DOI=10.1128/genomeA.00106-12;
RA   Murugapiran S.K., Huntemann M., Wei C.L., Han J., Detter J.C., Han C.S.,
RA   Erkkila T.H., Teshima H., Chen A., Kyrpides N., Mavrommatis K.,
RA   Markowitz V., Szeto E., Ivanova N., Pagani I., Lam J., McDonald A.I.,
RA   Dodsworth J.A., Pati A., Goodwin L., Peters L., Pitluck S., Woyke T.,
RA   Hedlund B.P.;
RT   "Whole Genome Sequencing of Thermus oshimai JL-2 and Thermus thermophilus
RT   JL-18, Incomplete Denitrifiers from the United States Great Basin.";
RL   Genome Announc. 1:E00106-E00112(2013).
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; CP003252; AFH39325.1; -; Genomic_DNA.
DR   RefSeq; WP_014629932.1; NC_017587.1.
DR   AlphaFoldDB; H9ZSL5; -.
DR   STRING; 798128.TtJL18_1445; -.
DR   KEGG; ttl:TtJL18_1445; -.
DR   PATRIC; fig|798128.4.peg.1404; -.
DR   HOGENOM; CLU_006557_2_0_0; -.
DR   Proteomes; UP000007388; 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 {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00595}; Coiled coil {ECO:0000256|SAM:Coils};
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:AFH39325.1}.
FT   COILED          151..178
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        531
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   858 AA;  96702 MW;  B7C91D8268E9B73C CRC64;
     MSQDPFALLK AEVDLLGRLL GEAIWTLSGE RFFALVEEVR ALAKARRQGD EAAGEALLAR
     VEGLSTEEAE ALVRAFTHYF HLVNLAEERH RVRVNRLRAQ AETLESPRPE GFLALAKALK
     ERGLSLEEAE AHLNRLELLL TFTAHPTETR RRTLRHHLEA LQRELEAGER ERLAARVALL
     YGTEEVRKAR PTVEDEIKGG LYYLPTTLWE AVPRVVAGLE AALERVYGRR PRLKSPVRFR
     SWIGGDRDGN PFVTPEVTAF AGRYAREVAR RRFLEALEDL VRDLSLAETR IPVPREVRER
     GEGVERFPGE PYRRYFAALY RALEREEATT EGLLAALKAA ERGLREVGLG RVAEAFLDPL
     EARLSAFGLE LAPLDLREES GRLLEAAAEL LRVGGVHPDF LALPQEERER LLTEELKTAR
     PLLPVGEAPK GEALRVALGA LRVWRDKGAH VVSMTHHPAD LLAVFLLARE VGLYRPGRPL
     PFDVVPLFET LEDLKRAPEV VRRLLKNPVF RAHAEGRGGV EVMIGYSDSN KDAGFLMANL
     ALYEAQEALS RVGEEVGLPV YFFHGRGTST ARGGGPAGRA IASLPPRSVG RRIRLTEQGE
     ALADRYSHPD LAVRHLEQML YHFALAALDP GQEPEARWRE ALAQAAEEST RRYRALLQEE
     GFFDFFEAFT PIREIGELPI ASRPVYRRGR VRDIRDLRAI PWVMAWTQVR VLLPGWYGLS
     ALEELPLDLL REMYRGWPFF ASTLEAAAMA LAKADMGVAR LYLRLVPEPL RFFYRRLAEE
     HARTVALLEA IFQAPLLHNQ RTLERQIRLR NPYVDPINIV QVELLRRYRA PGGKEDEALR
     RALLLSILGV AAGLRNAG
//