ID   M1M2X0_9PROT            Unreviewed;       941 AA.
AC   M1M2X0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   13-SEP-2023, entry version 55.
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   ORFNames=CDSE_0288 {ECO:0000313|EMBL:AGF46635.1};
OS   Candidatus Kinetoplastibacterium desouzaii TCC079E.
OC   Bacteria; Pseudomonadota; Betaproteobacteria;
OC   Candidatus Kinetoplastibacterium.
OX   NCBI_TaxID=1208919 {ECO:0000313|EMBL:AGF46635.1, ECO:0000313|Proteomes:UP000011547};
RN   [1] {ECO:0000313|EMBL:AGF46635.1, ECO:0000313|Proteomes:UP000011547}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCC079E {ECO:0000313|EMBL:AGF46635.1,
RC   ECO:0000313|Proteomes:UP000011547};
RX   PubMed=23345457;
RA   Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J., Matveyev A.V.,
RA   Teixeira M.M., Camargo E.P., Buck G.A.;
RT   "Genome evolution and phylogenomic analysis of candidatus
RT   kinetoplastibacterium, the betaproteobacterial endosymbionts of strigomonas
RT   and angomonas.";
RL   Genome Biol. Evol. 5:338-350(2013).
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; CP003803; AGF46635.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1M2X0; -.
DR   STRING; 1208919.CDSE_0288; -.
DR   KEGG; kde:CDSE_0288; -.
DR   PATRIC; fig|1208919.3.peg.72; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000011547; 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:AGF46635.1}.
FT   ACT_SITE        144
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        586
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   941 AA;  107983 MW;  97E841D66CA4E57F CRC64;
     MNSDMKQKTQ LQFEINLLEN ILKSVIQNCE GKRISNIVEN IRKVTAEVKK NKPNDNEPLE
     KLINELEGND PNIVARAFGY FLQLLNIAED LDQNRRTKYR SDIDNPKRGS LEHAVKKLDS
     HNVSASEIVA LIEDSCIMPV LTAHPTEIQR RSILDTHWKI AHKLSNRSFP QINNQQSDEN
     SELTGYITTL WQTRILRYSR LTVEDEIENA LSYYKSTFLH AIPKLYNDLS NIINSKYNKI
     IYSDPIYPFL RMGSWIGGDR DGNPYVDEKT LKQAVIRQST IIIEHYLKEI YSLKKELSIS
     TLLTRVDDEL LFLANRSNDS SPHLVDEPYR RALIGIYARL ASTSEKLIGR NLARRNSLPA
     HAYLNSEELY KDLTIIYKSL NNNNGNTITI LRLKNLLQSI KIFGFHLTTL DLRQNSDVHE
     RVIEELFQKA GVYLEGKNKY SELDENIKIV ILKKEINNNR PLISPWTQYS EETNKELNIL
     KTAAEIRSNF GEKTIQNTIV SHTESLSDLL EILLLQKETG LIPSLSNNLK QDNGLMVVPL
     FETINDLQNS SKIMGDWLDI PEVRTIIKET QHNTQEVMLG YSDSNKDGGF LTSNWALYQT
     ERDLVNVFNS RNIKLRLFHG RGGSVGRGGG SSFDAILSQP PGTVAGQIRL TEQGEVIQGK
     YNNEDIGKWH LELLLSATLE SSLCIDRKIS TQEDLYVKKY GHIMSFMSEY AQKTYRDLVY
     DNTGFAEYFF SSTPINEIAE LNIGSRPASR SKNQNIEDLR AIPWSFSWAQ CRLMLTSWYG
     VGSAIEEYLE YGSKITKKSK LERLHELKSM TEEWPAFKTL LSNIEMVLAK SNLKIASSYS
     ELVKNQKLRT SIFNKITNEH HKTINMLRLI TQRELLEDNP NLLAALHERF VFIDPLNFLQ
     IELIRRYRDK QNDLPSAEKE QIQRAIHLTI NGISAGLRNS G
//