ID A0A2B2CCC6_9BACI Unreviewed; 919 AA.
AC A0A2B2CCC6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=COJ96_08595 {ECO:0000313|EMBL:PFP29738.1};
OS Bacillus sp. AFS073361.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033511 {ECO:0000313|EMBL:PFP29738.1, ECO:0000313|Proteomes:UP000223997};
RN [1] {ECO:0000313|EMBL:PFP29738.1, ECO:0000313|Proteomes:UP000223997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS073361 {ECO:0000313|EMBL:PFP29738.1,
RC ECO:0000313|Proteomes:UP000223997};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFP29738.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NUZU01000013; PFP29738.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B2CCC6; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000223997; 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:PFP29738.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000223997}.
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; 105477 MW; 64C882F07AF9A805 CRC64;
MTTEVKVNDS SLPLRRDVKL LGKILGDILI NHSGSALFDK VEKIRLMCKT LRENFDQSIY
NALKEEISSL DAPMRKQVIR AFSMYFHLIN AAEQNHRMRR RRQYQLQEER VVQPASIESA
ILLLKENNIE EEVIQDTLNT LSLELVITAH PTEATKRSIL EIQQRIADIL KNLDHPLLTR
RERKKLEESL FNEVSILWQT DELRQNKPTV LDEVRNGLYY FDQTLFEVLP EIHQEVAECL
EKNFTNTQWE VPNFLRFGSW IGGDRDGNPN VTHDVTWETL KRQRRLVLKK YKKALVELMK
RYSHSTSRVE VSEDLLTLIE QEDTYLTDDK KWPNKGEAYR RAFAIIIERV KQVGKTDLGY
KSSEELLEDL YVIKRSLKKH HPAGHESKII QKLIRQVQLF GFHLATLDIR NHSGEHEAAI
TEILRKVSIT ENYAGLSEEE KLKILQNILL DPRPLLLLNE DYSTETQEMI KVFQTIKKAH
EEFGKRAISV YLVSMTKSPS DLLEVLVLAK EAGIYRLHAD GTLESHLHVA PLLETIDDLT
AGPKIMETLF EMPIYRNHLQ ILGDQQEIML GYSDGSKDGG TLTANWKLYK AQIEIHEMAK
RYQIGLKFFH GRGGSLGRGG GPLNKSILSQ PAETIGDGVK ITEQGEVLSS RYLLEDIAYR
SLEQATSTLL LAVAHISKEA EQGFQRDPIW VESIEEISSL ALTKYQSLVF GDSDFLTYFT
EATPLKEIGD LNIGSRPMSR KNQGRFEDLR AIPWVFAWTQ SRQLLPAWYA AGTGLTGFAA
KSEQNLPILQ DMYEKWPFFR STIDNLQMAL MKADITTARE YLSLVEDQNM AERIFTNILE
EYERTKEILL RITGDNELLD HTPNIKESVF RRNPYVDPLN FLQVELIKEL RSQGGSNEDL
LIEVLLTISG ISAGLRNTG
//