ID J7QT34_METSZ Unreviewed; 936 AA.
AC J7QT34;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 ECO:0000313|EMBL:CCJ07240.1};
GN OrderedLocusNames=BN69_1789 {ECO:0000313|EMBL:CCJ07240.1};
OS Methylocystis sp. (strain SC2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylocystaceae; Methylocystis.
OX NCBI_TaxID=187303 {ECO:0000313|EMBL:CCJ07240.1, ECO:0000313|Proteomes:UP000005263};
RN [1] {ECO:0000313|EMBL:CCJ07240.1, ECO:0000313|Proteomes:UP000005263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:CCJ07240.1,
RC ECO:0000313|Proteomes:UP000005263};
RX PubMed=23045511; DOI=10.1128/JB.01446-12;
RA Dam B., Dam S., Kube M., Reinhardt R., Liesack W.;
RT "Complete Genome Sequence of Methylocystis sp. Strain SC2, an Aerobic
RT Methanotroph with High-Affinity Methane Oxidation Potential.";
RL J. Bacteriol. 194:6008-6009(2012).
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; HE956757; CCJ07240.1; -; Genomic_DNA.
DR RefSeq; WP_014891269.1; NC_018485.1.
DR AlphaFoldDB; J7QT34; -.
DR STRING; 187303.BN69_1789; -.
DR KEGG; msc:BN69_1789; -.
DR PATRIC; fig|187303.17.peg.1943; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_5; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000005263; 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}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 598
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 936 AA; 103335 MW; 6961B4A74C8D25DA CRC64;
MQLEAQAQEN LVTAAPPAGA DPEALKGDES LIEDIRLLGR LLGDAVREHE GSAAFERIET
IRRLSVAASR NGDAEADRNL DALLRSLTAE EARTVIRAFS YFSHLANIAE DLHPLQQRAR
AQASGAFTGA PSLATTFARL RKAAVGAGRI AQALARGWIS PVLTAHPTEV RRKSLLDAEH
AIFKLLAARE HMRGKAERAQ NEMQLRARVS QLWQTELLRH SRLTVRDEIE NTLSYYRSTF
LREIPRLYAD IEQRLDGLRV PPFLRMGAWV GGDRDGNPNV TAESLSTALR MQCETVLRFY
LIEVHELGAE LSISRRYAGC TKALEALAAR SGDDNPHRDD EPYRRALIGV YSRLAGTLEK
LTGGQAARHA VAPGAPYANS WALLADLVTI DASLRVHHSE VIATQRLEPL IRAVEVFGFH
LATLDLRQSS DRHEETIAEL LNVARVVDDY VALPEAEKQA LLLRLLSDPR PVRLPGATYS
DRATSELTIM ERAREMRRLY GDEAIRHYII SHTETVSDLL EVLLLQKECG LMRGTLDPRD
AQRVIADLII VPLFETIDDL RNAAPIMQEF YALPGVLKLV VNSGGQQDVM LGYSDSNKDG
GILTSIWELY RASTALAEFF ASAPNVTLRL FHGRGGTVGR GGGPSYDAIL AQPPGTVNGQ
IRLTEQGEVI AAKYANPQIG HVNLELLVAA TLEATLLSAH KTPAPEFLEA AEELSQAGMA
AYRGLVYGTE GFVDFFFSST PISEIASLNI GSRPASRKPS RRIEDLRAIP WSFSWAQARV
ALPGWYGFGS AIAHFIAEDE KARLALLRRM SEEWPFFRAL LSNIDMILSK TDMSIAHHYA
GLVEDKALAA RIFGMIEAEH ARANDALEKL LGSKERLADN PTLARSIRHR FPYIAPLNYL
QVELIRRHRA GERGEDIREG ILMSINGVAA GLRNTG
//
