ID A0A0T9RA65_9GAMM Unreviewed; 878 AA.
AC A0A0T9RA65;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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:CNI51104.1};
GN ORFNames=ERS008667_03603 {ECO:0000313|EMBL:CNI51104.1};
OS Yersinia similis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=367190 {ECO:0000313|EMBL:CNI51104.1, ECO:0000313|Proteomes:UP000038204};
RN [1] {ECO:0000313|EMBL:CNI51104.1, ECO:0000313|Proteomes:UP000038204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y233 {ECO:0000313|EMBL:CNI51104.1,
RC ECO:0000313|Proteomes:UP000038204};
RA Murphy D.;
RL Submitted (MAR-2015) 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}.
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DR EMBL; CQBK01000034; CNI51104.1; -; Genomic_DNA.
DR RefSeq; WP_025382080.1; NZ_CQBK01000034.1.
DR AlphaFoldDB; A0A0T9RA65; -.
DR KEGG; ysi:BF17_08490; -.
DR PATRIC; fig|367190.3.peg.1641; -.
DR Proteomes; UP000038204; 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; 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:CNI51104.1}.
FT ACT_SITE 137
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 545
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 878 AA; 98369 MW; B056A92AA0935DEA CRC64;
MNEQYSAMRS NVSMLGTLLG DTIKEALGEH ILDRVETIRK LSKSSRAGNE ASRQELLTTL
QNLSNDELLP VARAFSQFLN LTNTAEQYHS ISPHGEAASN PEALAQLFTR LKDKKLSDQD
MRSAVDDLSI ELVLTAHPTE ITRRTLIHKL VEVNTCLSQL DHNDLADYER NKIMRRLRQL
VAQSWHTDEI RKLRPSPVDE AKWGFAVVEN SLWEGVPAFL REFNEQLENS LDYRLPVEAV
PIRFTSWMGG DRDGNPNVTA EITRHVLLLS RWKATDLFLR DIQVLVSELS MSECTPELRE
LAGGEEVLEP YRQLMKNVRT QLTNTQTYLE ARLKGERVLP PHDLLVSNDQ LWEPLYACYQ
SLKACGMEII ANGQLLDTLR RVRCFGVPLV RIDVRQESTR HTDAIAELTR YLGLGDYESW
SESDKQAFLV RELNSKRPLV PLKWEPSAET QEVLETCRVI AEAPQGSIAA YVISMAKVPS
DVLAVHLLLK EAGCPFTLPV APLFETLDDL NNADDVMTQL LGIDWYRGLI QGKQMVMIGY
SDSAKDAGVM AASWAQYRAQ DALIKTCEKA GIMLTLFHGR GGSIGRGGAP AHAALLSQPP
GSLKGGLRVT EQGEMIRFKF GLPEVTISSL ALYAGAILEA NLLPPPEPKK EWIEVMDLLS
DASCDMYRGY VRENPEFVRY FRSATPELEL GKLPLGSRPA KRRPNGGVES LRAIPWIFAW
TQNRLMLPAW LGAGAGLQKA IDAGKRDVLA TMCRDWPFFS TRIGMLEMVF AKADLWLAEY
YDQRLVDKSL WPLGQQLRDQ LAADIKVVLA IANDDHLMAD LPWIAESIAL RNVYTDPLNV
LQAELLHRSR QQEHPDACVE QALMVTIAGV AAGMRNTG
//
