ID   C1F4Y2_ACIC5            Unreviewed;       947 AA.
AC   C1F4Y2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
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:ACO34609.1};
GN   OrderedLocusNames=ACP_3068 {ECO:0000313|EMBL:ACO34609.1};
OS   Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM
OS   7670 / NBRC 15755 / NCIMB 13165 / 161).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Acidobacterium.
OX   NCBI_TaxID=240015 {ECO:0000313|EMBL:ACO34609.1, ECO:0000313|Proteomes:UP000002207};
RN   [1] {ECO:0000313|EMBL:ACO34609.1, ECO:0000313|Proteomes:UP000002207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 /
RC   NCIMB 13165 / 161 {ECO:0000313|Proteomes:UP000002207};
RX   PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP001472; ACO34609.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1F4Y2; -.
DR   STRING; 240015.ACP_3068; -.
DR   KEGG; aca:ACP_3068; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_0; -.
DR   InParanoid; C1F4Y2; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002207; Chromosome.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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}; Kinase {ECO:0000313|EMBL:ACO34609.1};
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:ACO34609.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002207};
KW   Transferase {ECO:0000313|EMBL:ACO34609.1}.
FT   ACT_SITE        171
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        595
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   947 AA;  105962 MW;  FBB6A15FE0E43C0B CRC64;
     MPQLWKPANW SDRLAELEAR TGDLKEAPLR RDVRSLGMLL GEVLREQAGD AFFQRVEDLR
     LNAIRRRETQ AEGQQQQADA LMQSTVAGVH SLPVDEAYYL TRAFAFYFDL INLAETNHRK
     RRRRSLQLHN SEAQRGSLRG TLRAMREAGI TAEEALAYLS RIFVVPVFTA HPTEVARRSV
     LFKRRRIGEF LAHLDSIPLP DEEMQDLENA VTAEITALWQ SDEVRSRRPE VADEIKMGLD
     YYEVSIFETL PRLYEEVSAA LASEYGLTLD AASLPLMLGF GSWIGGDRDG NPFVTPQVTR
     EAIHEARTRL LDFYLTRVQQ LIDLLTTSAQ QLPVSDELRT RLDNYLAEIR VGEDVLFGPR
     FQFELYRRYL ACVRARLLRT AGHAAPNADS LEASLAALPP YCSAHDLMED LSVLRRSLAA
     HRGERIAETL VDPFLLLVRT FGLHLHTLDV RQHARIHRKA LEECSAWQAG SNENAVEIPQ
     HLSPSTLDVL DTMRAIQEVK ASCSPEAIRQ YVISGAASAS DVTAVLWLAR LAGINPAGRD
     GDPGLMPVPL FESIEDLRNA PEVCRELWTN PAYRELLASW GNTQEIMLGY SDSNKDGGML
     TSTWEIFRAH RALHQVAHEC GITLRLFHGR GGTVGRGGGP THRSIYAQPV DAFDGQIRIT
     EQGEVLNFKY SDVVLAERNL ELMIAASLDA LARPNARQPD GHQTGVLEPA WESAFDELSS
     LAYDFYREQI LHDPEVLQYF EQATPVSELE HAKIGSRPSR RGGKMSFDSL RAIPWVFGWT
     QSRLLIPAWF GVGHAFTAFL QKPGGAELLR EMLTEFPLFI DLVRNVEMAL AKADLGIASL
     YSSLVPDAGL RERVFTKLKA EFERTREALL TIAQQDDLLQ NNPVLARSIR LRNPYVDPMS
     LIQVDLLRRK RALVASSNGA ASPELDAIHR AIAGTINGIS AGLRNTG
//