ID A0A290ZJ80_9RHOO Unreviewed; 918 AA.
AC A0A290ZJ80;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=CCZ27_02760 {ECO:0000313|EMBL:ATE59022.1};
OS Thauera sp. K11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=2005884 {ECO:0000313|EMBL:ATE59022.1, ECO:0000313|Proteomes:UP000217984};
RN [1] {ECO:0000313|EMBL:ATE59022.1, ECO:0000313|Proteomes:UP000217984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K11 {ECO:0000313|EMBL:ATE59022.1,
RC ECO:0000313|Proteomes:UP000217984};
RA Xi L., Qiao N.;
RT "Thauera phenolivorans sp. nov., a phenol derivative-degrading bacterium
RT isolated from activated sludge and an emended description of the genus
RT Thauera.";
RL Submitted (SEP-2017) 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; CP023439; ATE59022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A290ZJ80; -.
DR KEGG; thk:CCZ27_02760; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000217984; 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:ATE59022.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217984}.
FT ACT_SITE 145
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 580
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 918 AA; 101438 MW; FB0C9690F5768FF8 CRC64;
MTQDKDAPLR EDIRLLGRLL GDTVRDQQGA AVFDLIERIR QNSVRFRRDD DIAARRELDD
MLDALSREQT IQVVRAFSYF SHLANIAEDQ HHIRRSRAHL IAGSAPREGS LAHALQRAFD
SGSANAVSLQ AFFETALVSP VLTAHPTEVQ RKSILNCETV LARLLDERDR VQLTPEESEA
NLEALRRAVL TLWQTRMLRS ARLSVIDEVN NGLSYFETTF LRELPRLYAS LEDHLAGAAG
AGAMPAELPA FLQVGSWIGG DRDGNPYVTA EVLECALAMQ AEVALNYYLD ELHFLGSQLS
LALGLVSASD ALLALAERSP DQSPHRSDEP YRRAISGIYA RLAATYQALL GHAPVRHAIA
EAEPYPGAGA LSEDLDILHR SLVANGSAAL ARGRLRHLRR AVKVFGFHLA PVDLRQNSDV
HERVVAELLE VARPGTGYRE RDEAGRCALL LDELATARPL ASPHVKYSDE TESELAIFHA
ARRAHLRYGT AAIRQCIISK TDDVSDLLEL AVLLKEAGLL RPVDKALDVN LVPLFETIGD
LENAAGVMDR LFSLPGYREL LASACDDAQE VMLGYSDSNK DGGFMTSGWA LYKAEGELVD
VFARHGVRLR LFHGRGGSVG RGGGPSYQAI LAQPEGAVQG QIRLTEQGEV IGAKYGNPEV
GRRNLEVLVA ATLETSLRPA GTGPTPQAFL DAMQTLSDEA FAAYRGLVYE TPGFEQYFWE
STVISEIAGL NIGSRPASRK KGTRIEDLRA IPWVFSWAQC RLMLPGWFGF GRAVKRFLAA
RPDDGLALLQ RMHREWSFFA TLLSNMDMVL AKSDLAIASR YAELVKDVAL RESIFGRIRG
EWHDTVEVLL AITGQQELLD DNPLLKRSIR NRFPYLDPLN HVQVELLRRH REQGEDERIR
LGIHISINGI AAGLRNSG
//
