ID A0A1P8KCB2_9BURK Unreviewed; 944 AA.
AC A0A1P8KCB2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=RS694_14700 {ECO:0000313|EMBL:APW43660.1};
OS Rhodoferax saidenbachensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=1484693 {ECO:0000313|EMBL:APW43660.1, ECO:0000313|Proteomes:UP000186110};
RN [1] {ECO:0000313|EMBL:APW43660.1, ECO:0000313|Proteomes:UP000186110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22694 {ECO:0000313|EMBL:APW43660.1,
RC ECO:0000313|Proteomes:UP000186110};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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; CP019239; APW43660.1; -; Genomic_DNA.
DR RefSeq; WP_029709126.1; NZ_CP019239.1.
DR AlphaFoldDB; A0A1P8KCB2; -.
DR STRING; 1484693.RS694_14700; -.
DR KEGG; rsb:RS694_14700; -.
DR eggNOG; COG2352; Bacteria.
DR Proteomes; UP000186110; 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:APW43660.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186110}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 599
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 944 AA; 105315 MW; 99A603F6436E33B7 CRC64;
MKNAPLSTPA STPAKRSKDK ERPLVEDIRF LGRILGDVIR EQEGVEAFEL IEQIRTLSVA
FRRDADQEAD KALKKLLKGL SGDQTVSVIR AFTYFSHLAN LAEDRHHIRR RAVHEREGDT
QEGSVEVAMA RLRWAGISTK TISNTLAKSY VSPVLTAHPT EVQRKSILDA ERDIAQLLTA
RDEIKQLAAA FDSKKDALSP RELAANEAQM RARVMQLWQT RLLRFSKLTV ADEIENALSY
YESTFLREIP KLYAELEGLL GNQPVHSFLR MGQWIGGDRD GNPNVSAQTL EYALRRQAEV
ALRHYLTEVH LLGGELSISA MLAECSPEMQ ALAERSPDQN EHRKDEPYRR ALTGVYARLA
ATLKDLTGTE AARHAVAPQN AYLLAEDFVA DLRILESSLS AHHGAALVAQ RLHPLIRAVE
VFGFHLATVD LRQSSDKHEE VVAELLATAR IEANYSALDE QAKRVLLLGL LQDARSLRVQ
GVEYSAHAVG ELAIFEMAKR MRKNFGVQAI RHYIISHTET VSDLLEVLLL QREVGLLRGT
LDTQAVADLI VVPLFETIED LRNAAPIMRE FYALPGVADL VKRSGCEQDI MLGYSDSNKD
GGIFTSNWEL YRAEIALVEL FDVLAAEHNI QLRMFHGRGG TVGRGGGPSY QAILAQPPGT
VRGQIRLTEQ GEVIGSKYAN PEIGRRNLET LVAATLEATL LQPTKSATKA FLEAAAELSQ
ASMAAYRALV YETPGFTEYF FSSTPIREIA ELNIGSRPAS RKASQRIEDL RAIPWGFSWG
QCRLTLPGWF GFGSAVQKFI QQGTAAQQKE RLALLQKMYK QWPFFRTLLS NMDMVMAKSD
LALASRYSEL VADARLRKKI FTAIEAEWQA TAQALGSITG EKQRLANNAA LQRSIRHRFP
YIDPLHHLQV ELVRRYREGK ADERVQRGIH ISINGIAAGL RNTG
//
