ID A0A0Q6Z7R9_9BRAD Unreviewed; 925 AA.
AC A0A0Q6Z7R9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=ASC80_01890 {ECO:0000313|EMBL:KQW22171.1};
OS Afipia sp. Root123D2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW22171.1, ECO:0000313|Proteomes:UP000051348};
RN [1] {ECO:0000313|EMBL:KQW22171.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW22171.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW22171.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW22171.1,
RC ECO:0000313|Proteomes:UP000051348};
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:KQW22171.1}.
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DR EMBL; LMDP01000001; KQW22171.1; -; Genomic_DNA.
DR RefSeq; WP_056292391.1; NZ_LMDP01000001.1.
DR AlphaFoldDB; A0A0Q6Z7R9; -.
DR STRING; 1736436.ASC80_01890; -.
DR Proteomes; UP000051348; 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:KQW22171.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051348}.
FT ACT_SITE 153
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 587
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 925 AA; 102590 MW; BD43808469AE97F1 CRC64;
MDMDIETDSV SAEAEAMLRA DIRLLGRILG DTVRNQEGEA VFDLVERIRQ TSIRFHRDDD
KPARQELEAI LDGMSTGETV RIVRAYSYFS HLANIAEDQN HIRQTRSQNL AGPSRQAGTL
AGAVARAREA GIGAEELRGF FDGALVSPVL TAHPTEVRRK STIDREMEIA TLLDRCQRTQ
LTADERDAAD EQLRRAVLTL WQTNLLRRTK LTVLDEVANG LSFYDYTFFT QLPRLLCALE
DRLQPEGAAD QTHTSRELAP FLRMGSWIGG DRDGNPFVTA DVLRETLHMQ CAQVLKFYLG
ELHDLGGELS LASQLVDVSP ELQALAERSP DTSAHRSGEP YRRAVSGIYA RLAATAHLLG
VETRRPPVGE AAAYANVAEF KADLDIINRS LIANRSGVIA RGRLRLLRRA VDCFGFHLAS
LDMRQNSAVH ERTIAELFET VAPGTSYRAL SEQDRIALLV GELATARPLV SPFVSYSEET
RDELAVLHAA AGAHATFGES VIPQSIVSMT EGVSDLLEIA VLLKEVGLID PRGASSLNVV
PLFETIDDLR QCAEVMDRLL SLPAYRALVD SRGGVQEVML GYSDSNKDGG FVTSGWELYK
AEIGLIDVFA RHGVRLRLFH GRGGSVGRGG GPSYDAILAQ PGGAVNGQIR ITEQGEIISS
KYSNPEVGRH NLEILTAATM EASLLQPPHS VPRAEHFAVM ETLSSLAYTA YRGLVYETEG
FEEYFWASTV INEISTLNIG SRPASRTKTR RIEDLRAIPW VFSWAQCRLM LPGWYGFGSA
VEAFVKQHPE KGIAFLRGLY QEWPFFRTLL SNMDMVLSKS SIAIASRYAE LVPDQKLRDS
IFQRIRTEWQ TSIRALLEIM DQDRLVAGNP LLERSIRNRF PYLDPLNHVQ LELLRAYRAQ
DPDPQVLRGI QLTINGISAG LRNSG
//
