ID A0A0Q7AYA4_9BURK Unreviewed; 933 AA.
AC A0A0Q7AYA4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-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 ORFNames=ASC76_03220 {ECO:0000313|EMBL:KQW40749.1};
OS Rhizobacter sp. Root404.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW40749.1, ECO:0000313|Proteomes:UP000051611};
RN [1] {ECO:0000313|EMBL:KQW40749.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW40749.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW40749.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW40749.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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}.
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:KQW40749.1}.
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DR EMBL; LMDS01000001; KQW40749.1; -; Genomic_DNA.
DR STRING; 1736528.ASC76_03220; -.
DR Proteomes; UP000051611; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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:KQW40749.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051611}.
FT COILED 166..193
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 157
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 585
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 933 AA; 103365 MW; 2866420C14E5DE1D CRC64;
MTRQAAAKRK TSTADAAEKN RPLVDDIRLL GRILGDVIRE QEGKAAFELV ERVRQLSVAY
RLKSDAQAGR ALDRLLKNIS GDQTVSVIRA FSYFSHLANI AEDRHHVRRR DHHERQGHLQ
EGSLAMTLER LAAADIRAAD IAQTLSHAYI SPVLTAHPTE VQRKSILDAE RTIAELVEQR
DALHTERERA ENEALIRARV TQIWQTRMLR TAKLTVGDEI ENALSYYRST FLRQIPKMYR
ELENALPGHP IASFFRMGNW IGGDRDGNPF VTADTLQMAL ARQAETVLRF YLTETHELGA
ELSISASLAP VTAPMQALAA QSPDQSVHRE DEPYRRALIG MYARLAATLE LFTGTEALRH
AVAPQHPYDS ADEFLADLKV IDASLAAHHA QALAAPRLKP LMRAVQVFGF HLATVDLRQS
SDKHEAVVAE LLKVARVEAD YSGLGEDARR ALLVQQLNDA RPLRVRAAAY SEHTLGELAI
FEAAVVMLAR YGRAAMRHYI ISHTEDVSDL LEVMLLLKEV GLLRGTLDDG AVSDLIVSPL
FETIGDLRNA APIMRAFYAL PGITAMMVRS GAEQDIMLGY SDSNKDGGSF TSNWELYRAE
IDLVALFGSL RQDHGITLRL FHGRGGTVGR GGGPSYQAIL AQPPGTVNGQ IRLTEQGEVI
ASKYAHPEIG RRNLETLVAA TLEATLLNPT KSAPKAFLEA AAAISDGSFK AYRKLVYETP
GFTEYFFSAT PIREIAELNI GSXPASRKAT RAIEDLRAIP WSFSWGQCRV ALPGWCGFGS
AIAQYLGKEP RQRAERLALL RKMHKQWPFF GTLLSNLDMV IAKSDLAIAA RYVELVEDKK
LGKKIFALIK AEWQATSDAL ALITGETNRL ASNPSLARSI EHRFPYLDPL NHLQVELMRR
YRQRKEGDPE NARVQTGIHI SINGVAAGLR NTG
//
