ID   F8IFS7_ALIAT            Unreviewed;       906 AA.
AC   F8IFS7;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
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:AEJ44161.1};
GN   OrderedLocusNames=TC41_2257 {ECO:0000313|EMBL:AEJ44161.1};
OS   Alicyclobacillus acidocaldarius (strain Tc-4-1) (Bacillus acidocaldarius).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=1048834 {ECO:0000313|EMBL:AEJ44161.1, ECO:0000313|Proteomes:UP000000292};
RN   [1] {ECO:0000313|EMBL:AEJ44161.1, ECO:0000313|Proteomes:UP000000292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tc-4-1 {ECO:0000313|EMBL:AEJ44161.1,
RC   ECO:0000313|Proteomes:UP000000292};
RX   PubMed=21914900; DOI=10.1128/JB.05709-11;
RA   Chen Y., He Y., Zhang B., Yang J., Li W., Dong Z., Hu S.;
RT   "Complete Genome Sequence of Alicyclobacillus acidocaldarius Strain Tc-
RT   4-1.";
RL   J. Bacteriol. 193:5602-5603(2011).
RN   [2] {ECO:0000313|Proteomes:UP000000292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tc-4-1 {ECO:0000313|Proteomes:UP000000292};
RA   Chen Y., He Y., Dong Z., Hu S.;
RT   "The complete genome sequence of Alicyclobacillus acidocaldarius sp. Tc-4-
RT   1.";
RL   Submitted (JUN-2011) 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; CP002902; AEJ44161.1; -; Genomic_DNA.
DR   RefSeq; WP_014465004.1; NC_017167.1.
DR   AlphaFoldDB; F8IFS7; -.
DR   STRING; 1048834.TC41_2257; -.
DR   KEGG; aad:TC41_2257; -.
DR   PATRIC; fig|1048834.4.peg.2135; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000000292; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyruvate {ECO:0000313|EMBL:AEJ44161.1}.
FT   ACT_SITE        141
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        565
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   906 AA;  103424 MW;  70F37B785349BBA9 CRC64;
     MANDAPLHRD IRVLGDLLGE VLVEQCGRRV FDHVESIRLA AKAFRADPSP ETRAALQAAV
     SAVEPEHRND VIHAFSVYFQ LVNLAEQNHR LRRHRDYDRS QQVLRGSFRE AMRTLAHRGM
     TADDIEALLQ EVGIELVLTA HPTEALRRTV LDKHTKIAAF LEEMDDPRKT PRELDVLRER
     IRTEIVALWQ TRSVRKQRIT VLDEVRNGLY FLDQILFDVL PRVHQKLEQA VEEQFGRQLL
     ELPPLIRFGS WMGGDRDGNP NVTSDITWQT LVLHCDLALN KYEQKLRELG RDLSVSVDRA
     GADEDLLASL GHENDEPYRA LINRMLERLS NTRKRLHGER VDGPDYASPD EMMEDVERMA
     RSLAHHRGQR MVDAWLRPFL LQLRIFGFHM VTLDIRQHSG VHEQAVAELL QTAGLVDDYA
     SLGEEERVRI LSECLASPRP IRNPYHVYSD LTTEALAVFD CVRRGHETFG PRCVQDYLIS
     MTQGASDLLE VLLLAKESGL FGWPDGPKAP PKSDLNVVPL FETIEDLESA AGIMRSLFEN
     PVYRRHLEMR GWQQEIMLGY SDSNKDGGYL TANWSLYMAQ KHLIRLAEAY GVRIKFFHGR
     GGALGRGGGP VEQSILAQPT EALRGHVKIT EQGEVISQRY GHPGIAERSL ESSAAAVLVG
     ATREDTEEWA ERHPRWFQLL DRASEISFRA YRKLVFEHPV FLEYFHRATP IDEIGRMNIG
     SRPSRRSQSA RIEDLRAIPW VFSWTQSRHL LPAWYGFGSA MEAVMREDPH ALDDLRRMYE
     VWPFFRTLVD NLQMALAKAD MLVAREYAQL AGAAGEAIFP LVEEEYARTE RAVLDITGYR
     QLLDNRPVIR DSISLRNPYV DPLSFFQVRL LAELRRDDLS PEEREAELAD ALQTINGIAA
     GLRNTG
//