ID   I3ZC36_TERRK            Unreviewed;       934 AA.
AC   I3ZC36;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
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=Terro_0462 {ECO:0000313|EMBL:AFL86804.1};
OS   Terriglobus roseus (strain DSM 18391 / NRRL B-41598 / KBS 63).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Terriglobus.
OX   NCBI_TaxID=926566 {ECO:0000313|EMBL:AFL86804.1, ECO:0000313|Proteomes:UP000006056};
RN   [1] {ECO:0000313|EMBL:AFL86804.1, ECO:0000313|Proteomes:UP000006056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18391 / NRRL B-41598 / KBS 63
RC   {ECO:0000313|Proteomes:UP000006056};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Munk A.C.C.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "Complete genome of Terriglobus roseus DSM 18391.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003379; AFL86804.1; -; Genomic_DNA.
DR   RefSeq; WP_014784373.1; NC_018014.1.
DR   AlphaFoldDB; I3ZC36; -.
DR   STRING; 926566.Terro_0462; -.
DR   KEGG; trs:Terro_0462; -.
DR   PATRIC; fig|926566.3.peg.455; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_0; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000006056; 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; 2.
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};
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:AFL86804.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006056}.
FT   ACT_SITE        172
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        585
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   934 AA;  104692 MW;  8FF525DA60ECA4D8 CRC64;
     MAGLWQPANW SQRLAELEAS TPELKSAPLR RDVRSLGTLL GEVLREQVGE DLFEQVETLR
     RLAAERRQAE FDGDHALASS ALQQALLLVH TLPVDRAYQL ARAFGFYFEL INLAETNHRK
     RRRLAGGLRS DAEPQRGSLQ GTLRRMRKAG YTADEALELL RKICVTPVFT AHPTEVARRS
     VISKRHRIAQ LLEDLDRIPV SDEALEQLER GLLTEITGLW QTDDVRLQRP AVIDEVRMGL
     DYFNDSIFET LPTLYAEVRR ALHKEYGLDL ALTDLPTLVT FGSWIGGDRD GNPFVTPQVT
     REALAMSREV LRTHYRERLV EAAKHISSST QQAAASPALI AAVDDYLRQI PVAGEEMRAR
     FLCEQIRVLL TCMLARLGTE SELFIAPADT DRLPPYASAD ELLHDLSLIR ESLMENRGER
     IAESIIDPLI IEVRTYGLHL QTLDIRQHAK VHDAAVTEIT SWRADGSLPT PISEASAEVI
     DTFRTVAAVK RAGDPKSIRQ YVISGATSAE DVLKTIWLAR LGGVTVEHTE QDPGILIAPL
     FESIQDLQNA PDICRELWTN EAYQPLLESS GRRQEVMLGY SDSNKDGGMI ASTWEVWKAH
     RAVHTVAREC KVKLRLFHGR GGTVGRGGGP THRALYAQPL DSFNGQMRIT EQGEVLNFKY
     SDVVLAERNL ELMIAASLDA VARPDLRSCG GCSTHLTGAI EPAWEAAMDS LAEWSFERYR
     TDILDNPDTF DYFQQATPVA ELEHAKIGSR PAKRTGKRSL ADLRAIPWVF GWMQSRHTVP
     AWYGVGTAME RFTSDHADGL EQLQRMARDF PLFLDMVRNV ETALAKSDFG IAQMYASLVA
     DEELRNRVYP MLKDEFERTR SMILLITQQA DLLEQNAVLA QSIRLRNPYV DPMSWIQVDL
     LRRKREASEA DEGAINRAIT GTINGISAGL RNTG
//