ID   I0I7D1_CALAS            Unreviewed;       918 AA.
AC   I0I7D1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
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   ECO:0000313|EMBL:BAM01169.1};
GN   OrderedLocusNames=CLDAP_31290 {ECO:0000313|EMBL:BAM01169.1};
OS   Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 /
OS   STL-6-O1).
OC   Bacteria; Chloroflexota; Caldilineae; Caldilineales; Caldilineaceae;
OC   Caldilinea.
OX   NCBI_TaxID=926550 {ECO:0000313|EMBL:BAM01169.1, ECO:0000313|Proteomes:UP000007880};
RN   [1] {ECO:0000313|EMBL:BAM01169.1, ECO:0000313|Proteomes:UP000007880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1
RC   {ECO:0000313|Proteomes:UP000007880};
RA   Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA   Hanada S., Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC
RT   102666).";
RL   Submitted (FEB-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; AP012337; BAM01169.1; -; Genomic_DNA.
DR   RefSeq; WP_014434395.1; NC_017079.1.
DR   AlphaFoldDB; I0I7D1; -.
DR   STRING; 926550.CLDAP_31290; -.
DR   KEGG; cap:CLDAP_31290; -.
DR   PATRIC; fig|926550.5.peg.3386; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_0; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000007880; 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 {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:BAM01169.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007880}.
FT   ACT_SITE        148
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        579
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   918 AA;  105357 MW;  25E5E39EA6983B3D CRC64;
     MNEAQQQRLS ANIHLLGDML GETIIEQEGQ AVFELEEQIR ALAKAWRAGD ASAGEAIKAL
     MPSLIEDLPR TIAVLKAFTT YFQLVNLAED EQRIEILRDR AREAQMTGVP MRETLYESIA
     RLREEGLSAE DVQRILDNLY IVPVLTAHPT ETKRQTILTK LRTISDTLEQ ITSPGLLPSE
     ERELRERLRE DIALLWQSDE TRDRPPTVMD EVRTGLYFYE VTIFKLIPKI YEELERSLAE
     VYPGVKFRIP PFLRYGSWIG GDRDGNPNVT LSVTEEALRA MKETVLKQYN IAIDELYQHL
     IPAITRVNIS DELRESIAAD LKLVPEEEVE VLERFRMEPY RQKLIMMFRR LRATRAENER
     PWDDRERNPR AYRNVDEFMN DLRIIERSLL ANKGERLARG RLATLIRQVE VFGFHLATLD
     MRQHSSRHRD AIAEIFATYA ICPDYQALSE ADKVSLLTRE ILNPRPLTAQ LHFSEPTNET
     VALFRLMRRA KQEVDEDAVQ TYIISMTNSV SHVLEVLLLV KDAGLMGRID IVPLFETVSD
     LDAAPHIMAT LFENPAYRRH LELRGWRQQV MIGYSDSNKD GGYLRANWML FLAQRTLARL
     CDQFKVQLTL FHGRGGTLGR GGGPANRAIL AQPPESVRGR VRLTEQGEVI SLRYSNMALA
     RRHLEQLVNA VILTAGKRPH FPKEEEWAQR MDKLSDIAFR KYRSLVTKPG FITYFHEATP
     IDHISALNIG SRPARRKATQ DISDLRAIPW VFAWTQSRVN LPTWYGVGAA LEAWCRGGED
     AEKLAELREM YRQWPLFTNI LDNVQMGLAK ADMAIASLYS ELTDETTRSA IFTDILDEFQ
     RTERMVLLVV ESDHLLSKEP VLRRSIKVRN PYVDPMNYIQ VALLHRLKTE RDPERRRRLT
     AAVLSSVNGI AAGLQNTG
//