ID   E6SHW2_THEM7            Unreviewed;      1136 AA.
AC   E6SHW2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 71.
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=Tmar_1738 {ECO:0000313|EMBL:ADU51842.1};
OS   Thermaerobacter marianensis (strain ATCC 700841 / DSM 12885 / JCM 10246 /
OS   7p75a).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Clostridiales Family XVII. Incertae Sedis; Thermaerobacter.
OX   NCBI_TaxID=644966 {ECO:0000313|EMBL:ADU51842.1, ECO:0000313|Proteomes:UP000008915};
RN   [1] {ECO:0000313|EMBL:ADU51842.1, ECO:0000313|Proteomes:UP000008915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a
RC   {ECO:0000313|Proteomes:UP000008915};
RX   PubMed=21304738;
RA   Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA   Del Rio T.G., Tice H., Cheng J.F., Tapia R., Goodwin L., Pitluck S.,
RA   Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Schneider S., Rohde M., Goker M., Pukall R., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Detter J.C.;
RT   "Complete genome sequence of Thermaerobacter marianensis type strain
RT   (7p75a).";
RL   Stand. Genomic Sci. 3:337-345(2010).
RN   [2] {ECO:0000313|Proteomes:UP000008915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a
RC   {ECO:0000313|Proteomes:UP000008915};
RX   DOI=10.4056/sigs.1373474;
RA   Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J., Tapia R., Goodwin L., Pitluck S.,
RA   Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Schneider S.,
RA   Rohde M., Goker M., Pukall R., Woyke T., Bristow J., Eisen J.,
RA   Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Detter J.;
RT   "Complete genome sequence of Thermaerobacter marianensis type strain
RT   (7p75aT).";
RL   Stand. Genomic Sci. 3:337-345(2010).
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; CP002344; ADU51842.1; -; Genomic_DNA.
DR   RefSeq; WP_013496143.1; NC_014831.1.
DR   AlphaFoldDB; E6SHW2; -.
DR   STRING; 644966.Tmar_1738; -.
DR   KEGG; tmr:Tmar_1738; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000008915; 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; 3.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 3.
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:UP000008915}.
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          812..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        708
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1136 AA;  122339 MW;  3F789C2A41053B2E CRC64;
     MADSTAVYPS GHGAPEHGEP AYRSRSEEDL YPLLKQEVDL LGRALGEAIR RLSGDRLFEL
     EEDIRARTKH LRQHPGDEAA RKALRAQVGS LSVTEAEGLI RAFSTYFHLV NLAEERHRVR
     VNRQRERAST PDHPRPESLL ALVGQLKARG LSYDDVVRLL ASARLVLTFT AHPTETRRRT
     LRHHLLELNR TLDRLERGEA QLPEVLARVT LLWTTRELRP APPRVEDEVR GGLYYLPTTL
     WEAVPRLMDA LEQAVAAYYG RRPVLPPPLA FRSWIGGDRD GNPFVTPEVT AWAQGYARAE
     IARKYAEGLA ALTRDLSVAE ERALLPPLPS LQGAAIALLA GGAGVTQPER ADAAGERGDG
     PAGGPGAGTA AAPDPGPDAE AGGGHPRAAR TVNGTPGRFL GEPYRQFVYR LQRAWAARTV
     PEEVWGDGAG AGGGATIAVQ RPFTVETPAT LPGLRHEGEG EGKGRPERPD PLVCPDRAND
     ANRPDTPARP PRSGPRDESD SAADPGDLAG LLHQVERGLE AAGLGEAAAT LVRPLRWRAQ
     VFGEAMAPLD VREHAEAHGR AVAELLEAGG VMPAADYLAL DPAAREERLT RELATPRPLA
     PVGYVPRTRE LAVALGALRA WQGRGAYIIS GCRGPADVLE VFVLAREAGL YRPGQPLPFD
     VVPLFETLAD LEAAPAAMER LLRNPVFGAH ARARGGCEVM IGYSDSSKDA GYLAANWALY
     RAQEGITAVA RAAGIPVSFF HGRGTSTARG GGGTAGRAIA SLPPGTVGRR LRLTEQGEAL
     ADRYAHPELA LRNLEQLLYH FLLAAARDTA VPDQAASDPD ERGPAVRPGS PVAPGHAVAG
     SDEPSPVAGP GSPAPSALQP ASSGETGGRS SVAPEVPPRG SARSESPVRF EDPRRAQEPL
     AGGGSAAVPP VWREAMDRAA ARSAEAYRQL LAEPGFFEFF EHFTPIREIA ALKIASRPVA
     RTGRARRVQD LRAIPWVMAW TQVRLLLPGW YGLAEGLAAV PRDLRQEMFA RWPFFRSVLD
     GAALALAKAD LAVAREYLRL VPEPLAGRFF PRLEQAFLRT RELLEETFGG PLLAHHPVLA
     RQTALRNPYV DPISYLQVEL LARYRSAPPD DPQRPALERA LLLSILGIAA GLRNAG
//