ID A0A1H6Z1W6_9GAMM Unreviewed; 914 AA.
AC A0A1H6Z1W6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN04487997_3431 {ECO:0000313|EMBL:SEJ45387.1};
OS Frateuria terrea.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Frateuria.
OX NCBI_TaxID=529704 {ECO:0000313|EMBL:SEJ45387.1, ECO:0000313|Proteomes:UP000199420};
RN [1] {ECO:0000313|EMBL:SEJ45387.1, ECO:0000313|Proteomes:UP000199420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26515 {ECO:0000313|EMBL:SEJ45387.1,
RC ECO:0000313|Proteomes:UP000199420};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FNYC01000008; SEJ45387.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6Z1W6; -.
DR STRING; 529704.SAMN02927913_3511; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000199420; 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:SEJ45387.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199420}.
FT ACT_SITE 149
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 581
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 914 AA; 100618 MW; FDE6064836F264D7 CRC64;
MEASRDVDYL PHDGPLREDV GRLGRLVGLM LAEQGGEAFF ERVEAVRQAA IRRRREGEPV
AALSGALDDL QTDEAEALAR AFATYFQAVN TAERVHRIRR RRDYQREGRA PQPESLLDVL
GRLKAEGVGA DELLGWLARL WIEPVFTAHP TEAVRRSLLE KEQAIVRALV DGFDPGRTPQ
ERAEDEDRIY MALSTGWQTA EASPVRPTVQ DEHHHVGFYL ANPIYRIVPA LYESLADALQ
SVYGVATPLP RLLGFASWVG GDMDGNPNVG ADTIAASLAT QRAHVLEHYV SDVAGLARLL
SQTEGRVAVD AQLAARLADY RERFPQAAAR IRPRHADMPY RCLLTLIGAR LEATGENDHA
EGYASPAELL DDLQLIDRSL LAHRGLHAGA YAVRRLIWRV RTFGFHLARL DVRQDSRVHD
DALAALLGDD AWPDQPAEER ARQLSAYAAG QARFAIGHAE VVTGLYDVFV TLGDARRRYG
NDAIGLYVIS MARSAADVLA VLALARYGGL VAPVASSRVS PGDETGSSVP LDIAPLFETI
DDLVHAPATL QALLGDPVYR AHLQSRGDRQ WVMLGYSDSG KDGGTLASRW ALQRAQVELL
EVAKDVGIRL VFFHGRGGSA SRGGGRMAPA LMSSPRGSVA GVLRVTEQGE VIHRKYGIRA
LALRNLEQTA SAVLRASLRP REEEPREAAW RERMEVLAAY SRRHYRALVD REGFVDYFRS
ATPIDVVERM TLGSRPASRR SMRGVQDLRA IPWVFAWTQC RSIITGWYGL GSALEQGAAD
FGEPGLIEMA RDWPFLANAL DDVAMVLAKC DLDIAEAFSR LAGDLHAPFF ASIGEEFERT
RRWLLKLKGD DTLLADNPRL AVSIRLRNPY VDPMSLLTVD LLERWRAGGS QDEALLRALV
ACVNGVSQGL QNTG
//
