ID A0A0S2SCW9_9GAMM Unreviewed; 877 AA.
AC A0A0S2SCW9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
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:ALP39471.1};
GN ORFNames=ATO46_09765 {ECO:0000313|EMBL:KUE78638.1}, WL1483_52
GN {ECO:0000313|EMBL:ALP39471.1};
OS Aeromonas schubertii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=652 {ECO:0000313|EMBL:ALP39471.1, ECO:0000313|Proteomes:UP000058114};
RN [1] {ECO:0000313|Proteomes:UP000058114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WL1483 {ECO:0000313|Proteomes:UP000058114};
RA Liu L.;
RT "Complete Genome Sequence of Aeromonas schubertii strain WL1483.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KUE78638.1, ECO:0000313|Proteomes:UP000054876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43700 {ECO:0000313|EMBL:KUE78638.1,
RC ECO:0000313|Proteomes:UP000054876};
RA Liu L., Li Q., Zhang F., Shi B.;
RT "Complete genome sequence of Aeromonas schubertii strain ATCC43700.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ALP39471.1, ECO:0000313|Proteomes:UP000058114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WL1483 {ECO:0000313|EMBL:ALP39471.1,
RC ECO:0000313|Proteomes:UP000058114};
RX PubMed=26798095;
RA Liu L., Li N., Zhang D., Fu X., Shi C., Lin Q., Hao G.;
RT "Complete Genome Sequence of the Highly Virulent Aeromonas schubertii
RT Strain WL1483, Isolated from Diseased Snakehead Fish (Channa argus) in
RT China.";
RL Genome Announc. 4:e01567-15(2016).
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; CP013067; ALP39471.1; -; Genomic_DNA.
DR EMBL; LPUO01000054; KUE78638.1; -; Genomic_DNA.
DR RefSeq; WP_050666330.1; NZ_LPUO01000054.1.
DR STRING; 652.WL1483_52; -.
DR KEGG; asr:WL1483_52; -.
DR PATRIC; fig|652.5.peg.117; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000054876; Unassembled WGS sequence.
DR Proteomes; UP000058114; 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:ALP39471.1}.
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 877 AA; 98887 MW; EB1DE886AD8E08EC CRC64;
MNEKYAALRA NVGLLGQLLG KSIKDHKGQA FLDKIETIRQ LAKSSRKGNE QDRQSLIDTL
QTLSDEELLP VARAFSQFLN LANVAEQFHT ISRSFADQTG ASDPLEQLFT KLKASNLSQE
AIVQAVRELD IDLVLTAHPT EVTRRTLIHK HVQLNDCLEA LELSDLLPQE RDRLINRVEQ
LINQAWHTNE IREQRPTPVD EAKWGFAVIE NSLWPAIPEF MRHLDEQLQQ HLGVRLPLDA
APVRFTSWMG GDRDGNPFVT AEVTAKVLEL GRWMAVSLFY KEIKELTSEL SMSDCNDELR
ARVGNHNEPY RVVMRELREA LRETKEYLTA KVQGQQSENR DLVRTTAQLR EPLELCYHSL
HASGMGNIAD GMLLDVLRKV ACFGIHLVKL DIRQDGERHA LALAELTRYL GIGDYAEWSE
ENKQAFLLAE LNSRRPLVPA DWTPSDETRE TIETCRVIAA NDPDAFGIYI ISMAGAPSDV
LAVQLLLKEA GCKFRMPVAP LFETQEDLMA GTRVMERLLS VDWYRGYIQG RQYVMIGYSD
SAKDAGMMAA GWAQYAAMES LVALAEINQI RLTLFHGRGG TVGRGGAPAH QAILSQPPGS
LRGGLRTTEQ GEMIRFKFGL PKVAINSLLL YTSAVLEGNL LPPPKPREEW RQVMELLSTV
SCEHYRSIVR GHPDFVPYFR AATPELELGK LPLGSRPAKR KPNGGVESLR AIPWIFAWTQ
NRLMLPAWLG AHKGLQQAID EGKLEVLEEM SRQWPFFRTR LEMLEMVFLK ADAWLAEYYD
TRLVPEALWP LGQQLRRELA DSIALVLKLR PQGGLLDDQP WIQESIRLRN PYTDPLNVLQ
AELLGRSRRD PDSLHPELDQ ALMVTIAGIA AGMRNTG
//
