ID A0A0X1SXD4_PSEAA Unreviewed; 876 AA.
AC A0A0X1SXD4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AWM79_04035 {ECO:0000313|EMBL:AMB84521.1};
OS Pseudomonas agarici.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=46677 {ECO:0000313|EMBL:AMB84521.1, ECO:0000313|Proteomes:UP000063229};
RN [1] {ECO:0000313|EMBL:AMB84521.1, ECO:0000313|Proteomes:UP000063229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 2472 {ECO:0000313|EMBL:AMB84521.1,
RC ECO:0000313|Proteomes:UP000063229};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-2016) 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,
CC 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 ---------------------------------------------------------------------------
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; CP014135; AMB84521.1; -; Genomic_DNA.
DR RefSeq; WP_060782196.1; NZ_CP014135.1.
DR AlphaFoldDB; A0A0X1SXD4; -.
DR STRING; 46677.AWM79_04035; -.
DR Proteomes; UP000063229; 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 Pyruvate {ECO:0000313|EMBL:AMB84521.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000063229}.
FT ACT_SITE 138
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 543
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 876 AA; 97389 MW; A34D38AE9D8C3AA9 CRC64;
MSDIDVRLRE DVHLLGELLG NTIRDQHGDE FLDKIERIRK SAKADRSNCA SAQLSASLDD
LGDDELLPVA RAFNQFLNLA NIAEQYQLIH RRDESQPAPF ESRVLPELLA RLRAEGHGAE
FLARQLGRLD IELVLTAHPT EVARRTLIQK YDAIAAQLAL QDHRDLTGAE REQIRQRLQR
LIAEAWHTEE IRRTRPTPVD EAKWGFAVIE HSLWQAIPNY LRKADQALHA ATGLRLPLEA
APIRFASWMG GDRDGNPNVT AKVTREVLLL ARWMAADLYL RDVDHLAADL SMQQASEALR
AQAGDSAEPY RAVLKQLRER LRTTRQWAHA SLAVTQSASE AVLQNNSELL EPLQLCYQSL
HECGMGVIAD GPLLDCLRRA VTFGLFLVRL DVRQDASRHA GALSEITDYL GLGRYEDWNE
EARLTFLTSE LANRRPLLPA YFEPSVDTAE VLATCKEIAA APAASLGSYV ISMAGAASDV
LAVQLLLKES GVLRSMRVVP LFETLADLDN AGPVMERLLL LPGYRARLQG PQEVMIGYSD
SAKDAGTTAA AWAQYRAQER LVEICREQQV ELLLFHGRGG TVGRGGGPAH AAILSQPPGS
VAGRLRTTEQ GEMIRFKFGL PDIAEQNLNL YLAAVLEATL LPPPPPQPAW RSLMDQLAAD
GLSAYRAEVR DNPQFVEYFR QSTPEQELGR LPLGSRPAKR RAGGIESLRA IPWIFGWTQT
RLMLPAWLGW ETALRKALER GDGELLEQMR EQWPFFRTRI DMLEMVLAKA DGDIARSYDE
RLVQAELLPL GVHLRDLLSQ ACAVVLGLTG QSQLLARSPE TLEFIRVRNT YLDPLHLLQA
ELLARSRRQE AAQDSPLEQA LLVSVAGIAA GLRNTG
//
