ID A0A1Y6F2H4_9BACI Unreviewed; 919 AA.
AC A0A1Y6F2H4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=SAMN05444673_1736 {ECO:0000313|EMBL:SMQ69098.1};
OS Bacillus sp. OV166.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1882763 {ECO:0000313|EMBL:SMQ69098.1, ECO:0000313|Proteomes:UP000194454};
RN [1] {ECO:0000313|EMBL:SMQ69098.1, ECO:0000313|Proteomes:UP000194454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV166 {ECO:0000313|EMBL:SMQ69098.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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|HAMAP-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; FXWM01000001; SMQ69098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6F2H4; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000194454; Unassembled WGS sequence.
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; 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.
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:SMQ69098.1}.
FT ACT_SITE 150
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
FT ACT_SITE 577
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ SEQUENCE 919 AA; 105521 MW; 98449C90A74404CD CRC64;
MTIELKLNDS SLPLRQDVKL LAKMLGEILL NHGGTELLDK VEKIRLMCKT LREHFDQAIY
DALKEEIASL SAPLRKQVIR AFSMYFHLIN AAEQNHRIRR RRQYQLEDET IVQPASIESA
ILSLKENNIK EDVIQDILNT LSLELVITAH PTEATKRSIL EIQQRIAVIL KSLDHPLLTS
RERKKLEERL FNEVSILWQT DELRQTKPTV LDEVRNGLYY FDQTLFEVLP EIHQEVADCL
EKNYTQTQWE VPNFLRFGSW IGGDRDGNPN VTHDVTWETL NRQRRLVLKK YKNVLVDLMK
RYSHSTSRVE VSNDLLKLIE LEDTYLTDEK KWPIQTEVYR RAFAIIIERV KQVGKTDLGY
KSSDELLEDL FIIKKSLKKH HPAAHELMTI QKLIRQVQLF GFHLATLDIR NHSGEHEAAM
TEILRKVSIS DNYAGLAEDE KLKILQNILL DPRPLLLLNE DYSAETQEMI KVFQMIKKAH
EEFGKRSISV YLVSMTKSPS DLLEVLVLAK EAGIYRLHAD GTLESHLHVA PLLETIDDLT
AGPEIMETLF EMPVYRNHLQ IMGDQQEIML GYSDGSKDGG TLTANWKLYK AQIEIHEMAK
RYQIGLKFFH GRGGSLGRGG GPLNKSILSQ PAETIGDGVK ITEQGEVLSS RYLLEDIAYR
SLEQATSTLL LTATHISKEA KQGFQRDPIW VESIEEISSL ALTKYQSLVF GDPDFLAYFT
EATPLRELGD LNIGSRPMSR KNQGRFEDLR AIPWVFAWTQ SRQLLPAWYA AGTGLAGFVA
NGEQNLQMLQ QMYEKWPFFQ STIDNLQMAL MKADITTARE YLSLVKDQTI AERIFTNILE
EYETTKEVLL RITGDNELLD HTPNIKESVY RRNPYVDPLN FLQVELIKEL RNQEEPNEEL
LIEVLLTISG ISAGLRNTG
//
