ID   A0LRW1_ACIC1            Unreviewed;       915 AA.
AC   A0LRW1;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 101.
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=Acel_0397 {ECO:0000313|EMBL:ABK52171.1};
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC   Acidothermus.
OX   NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK52171.1, ECO:0000313|Proteomes:UP000008221};
RN   [1] {ECO:0000313|EMBL:ABK52171.1, ECO:0000313|Proteomes:UP000008221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B
RC   {ECO:0000313|Proteomes:UP000008221};
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(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; Evidence={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; CP000481; ABK52171.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0LRW1; -.
DR   STRING; 351607.Acel_0397; -.
DR   KEGG; ace:Acel_0397; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   InParanoid; A0LRW1; -.
DR   Proteomes; UP000008221; 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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 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:ABK52171.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008221}.
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        582
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   915 AA;  100646 MW;  BA667FC5C3853563 CRC64;
     MPAVGPIPAC RGRIDPDTAR ADRSSCTSDA TLTHVPPTSD AAPPALSIRE QARQEMPEQL
     RRDVRLLGEL LGQVLREYGG QQLLDDVEAL RRAVIAARTG AGRIEDVEEL VARWPLSRAE
     EVARAFTVYF HLANLAEEHH RVRVLRSRDG LGTAGDSLAA SVSEVRALYG EERLAELLAG
     LRVHPVLTAH PTEARRRAVV SAIARAGEQL DRLDDPRAGE SERADARRRL LEEIDILWRT
     AHLRSTAVDP LDEVRTAMSA FDETLFRVMP ALYRGLDHLL LGEESGARRP AAPAFLRLGS
     WVGGDRDGNP LVTASVTRAA MAIQAEHVLL ALERAATRIG RTLTASAETT PPNTALQDAL
     AEARRRLPSV VEELEIRAPG EPHRVYTLYA AARVRARRRG EPTGYRHAGE FLADLRLVQE
     SLVQSGAHRL AFGELQHLIW QVETFGFHLA ELEIRQHSAI HAKALADLDS GGPRWEMTDE
     VLETFRTIRW LQDEYGVDAC RRYVISFTRS AEDIAAVYRL ADRATDGSPP VLDVVPLFET
     EEDLRHCVPT LEAALDIPEV RARLAANGRR MEVMLGYSDS AKDVGPVSAT LALYDAQQAL
     ADFARRHDVQ LTLFHGRGGA LGRGGGPANR AILSQAPGSV DGRFKVTEQG EVIFARYGNP
     VIARRHLDQV TAAVLLASTP AVMERVAAAE RKYRPVFEAV SRAARTEYRG LVETPGFAEY
     FAAVSPLPEI GALRIGSRPV RRSAGTDLAD LRAIPWNFSW AQTRVNLPGW YGIGSGFAAV
     GDVDALRAAY AEWPLFTTMV DNVEMSLAKT DRDIAQRHLA LGNRPDIADR ILAEYDRSVE
     WVLRVLGTTR LLETHRVLGQ AVQLRNPYVD ALSHLQLRAL AALRRGIPDE AERDRTLRLL
     LLSINGVAAG LQNTG
//