ID   CAPP_THEVB              Reviewed;        1011 AA.
AC   P0A3X5; Q94QB2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=Phosphoenolpyruvate carboxylase;
DE            Short=PEPC;
DE            Short=PEPCase;
DE            EC=4.1.1.31;
GN   Name=ppc; OrderedLocusNames=tll1912;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC   Thermosynechococcaceae; Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR   EMBL; BA000039; BAC09464.1; -; Genomic_DNA.
DR   RefSeq; NP_682702.1; NC_004113.1.
DR   RefSeq; WP_011057749.1; NC_004113.1.
DR   AlphaFoldDB; P0A3X5; -.
DR   SMR; P0A3X5; -.
DR   STRING; 197221.gene:10748518; -.
DR   EnsemblBacteria; BAC09464; BAC09464; BAC09464.
DR   KEGG; tel:tll1912; -.
DR   PATRIC; fig|197221.4.peg.2000; -.
DR   eggNOG; COG2352; Bacteria.
DR   Proteomes; UP000000440; 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; Lyase; Magnesium; Reference proteome.
FT   CHAIN           1..1011
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166640"
FT   ACT_SITE        207
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        658
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1011 AA;  116427 MW;  0A11D4D01FE9E7FE CRC64;
     MTSVLDVTNR DRLIESESLA ARTLQERLRL VEEVLVDVLA AESGQELVDL LRRLGALSSP
     EGHVLHAPEG ELLKVIESLE LNEAIRAARA FNLYFQIINI VEQHYEQQYN RERAAQEGLR
     RRSVMSEPIS GVSGEGFPLP HTAANATDVR SGPSERLEHS LYEAIPATQQ YGSFAWLFPR
     LQMLNVPPRH IQKLLDQLDI KLVFTAHPTE IVRQTIRDKQ RRVARLLEQL DVLEGASPHL
     TDWNAQTLRA QLMEEIRLWW RTDELHQFKP EVLDEVEYTL HYFKEVIFAV IPKLYRRLEQ
     SLHETFPALQ PPRHRFCRFG SWVGGDRDGN PYVKPEVTWQ TACYQRNLVL EEYIKSVERL
     INLLSLSLHW CDVLPDLLDS LEQDQRQLPS IYEQYAVRYR QEPYRLKLAY VLKRLQNTRD
     RNRALQTYCI RRNEAEELNN GQFYRHGEEF LAELLLIQRN LKETGLACRE LDDLICQVEV
     FGFNLAALDI RQESTCHAEA LNEITAYLGI LPCPYTELSE AERTRWLLSE LSTRRPLIPG
     ELPFSDRTNE IIETFRMVRQ LQQEFGTDLC NTYIISMSHE VSDLLEVLLF AKEAGLFDPA
     TGASTLQAIP LFETVEDLKH APAVLTQLFS LPFCRSYLGS NSTPFLQEVM LGYSDSNKDS
     GFLSSNWEIY KAQQQLQKIA ESFGFQLRIF HGRGGSVGRG GGPAYAAILA QPAQTIKGRI
     KITEQGEVLA SKYSLPELAL FNLETVATAV IQASLLRSSI DEIEPWHEIM EELATRSRQC
     YRHLIYEQPE FIEFFNEVTP IQEISQLQIS SRPTRRGGKK TLESLRAIPW VFSWTQTRFL
     LPAWYGVGTA LKEFLEEKPA EHLSLLRYFY YKWPFFRMVI SKVEMTLAKV DLEIARYYVQ
     ELSQPQNREA FCRLYDQIAQ EYRLTTELVL TITGHERLLD GDPALQRSVQ LRNRTIVPLG
     FLQVSLLKRL RQHNSQTTSG AILRSRYGRG ELLRGALLTI NGIAAGMRNT G
//