ID   D5X259_THIK1            Unreviewed;       944 AA.
AC   D5X259;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 68.
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=Tint_1837 {ECO:0000313|EMBL:ADG31205.1};
OS   Thiomonas intermedia (strain K12) (Thiobacillus intermedius).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX   NCBI_TaxID=75379 {ECO:0000313|EMBL:ADG31205.1};
RN   [1] {ECO:0000313|EMBL:ADG31205.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 {ECO:0000313|EMBL:ADG31205.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C.,
RA   Heinhorst S., Woyke T.;
RT   "Complete sequence of Thiomonas intermedia K12.";
RL   Submitted (APR-2010) 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; CP002021; ADG31205.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5X259; -.
DR   STRING; 75379.Tint_1837; -.
DR   KEGG; tin:Tint_1837; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
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:ADG31205.1}.
FT   ACT_SITE        161
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        601
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   944 AA;  105145 MW;  ADB42A6DABCE7DF0 CRC64;
     MPIQPLFAMS TRPSAARNAS DPDAPLFDDI RLLGRLLGDL IREQEGQEMF DIVETVRQLS
     VKFHRDGDAK DRRALDKLLS SLSRDQAVSV IRAFSYFSIL ANIAEDHHVL RRAEQDAERG
     APPQRDSVRA ALETLKDSGV DRQQLLQFFD QALISPVLTA HPTEVQRKSV LDAERALARL
     LVERDATRLP QKRADIEDAM RARVVQLWQT RLLRYVKLKV SDEIKNALSF YGATFFSQFP
     RLYRNLERDI EALFPAGGQD LAKTDLPAFF RMGHWIGGDR DGNPFVTADT LSYALRMQSR
     TAIEFYMAEV HAIGGELSIS ALLASASPEL MALAEQSPDL SEHRSDEPYR RALIGMYARL
     AANLRKLAGV QALLPEVGSA EPYANADEFI ADLRIIHDSL HRHHAGPLAQ TRLDPLIRAA
     GVFGFRLATI DLRQSSDQHE AVLRELLAAA GLCPDYSHQD EAAKQALLIR CLNDPRPLRL
     PHHVYSDWAR SELAVFDRAY SARRDFGPRA IRQYIISHSE TVSDLLELLL LQKEAGLFHG
     TLGSHDSYAE LLVAPLFETI EDLRNAPAIM RDFYALPGIA GLVQRSGGEQ EIMLGYSDSN
     KDGGFFTSNW ELYCAEVALA EQFEQLKAEH GITLRLFHGR GGTVGRGGGP SFDAILAQPP
     GTVNGQIRLT EQGEVITSKY GNPEIGLRNL ETLVAATLQA TLLPQTKTAS KPPARFLDAA
     AALSEASMAA YRKLVYETPE FTDYFYSATP ISEIAELNIG SRPSSRKATR AIADLRAIPW
     GFSWGQCRVA LPGWYGFGSG VQAFLDANPD GLKLLQRMAK QWPFFATLLS NIDMVLAKTD
     LRVAQRYAEL VADSKTRQKV LKALQREWQL TTDMLTAITG NTERLADNPT LKRSIRARFP
     YIDPLNHLQI ELLHRFREGQ TDERTKRGIH LSINGIAAGL RNTG
//