ID A2SK67_METPP Unreviewed; 934 AA.
AC A2SK67;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
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 OrderedLocusNames=Mpe_A3003 {ECO:0000313|EMBL:ABM95956.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM95956.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM95956.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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; CP000555; ABM95956.1; -; Genomic_DNA.
DR RefSeq; WP_011830579.1; NC_008825.1.
DR AlphaFoldDB; A2SK67; -.
DR STRING; 420662.Mpe_A3003; -.
DR KEGG; mpt:Mpe_A3003; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_4; -.
DR Proteomes; UP000000366; 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:ABM95956.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000366}.
FT ACT_SITE 154
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 586
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 934 AA; 103374 MW; F3AEAF3836547EB2 CRC64;
MATAKTPRSA DRGADKNRPL IEDIRLLGRI LGDVIREQEG ALAFELIERI RQLAVAYRLK
RDTQAGRALD RLLKNLSVEQ AVSVVRAFSY FSHLANLAED RHHVRRREHH EQLGHVQEGS
LAMSFERLAK RGVRATEIAE LLGHAYLSPV LTAHPTEVQR KSVLDAERAV AELIGARDTL
PTQRERAANE AMLRARVTQL WQTRLLRTSK LSVANEIDNA LSYYQSTFLR QIPRLYAELE
ALLPGFEVAP FFRMGNWIGG DRDGNPNVTA ETLRLALARH SETVLRFYLT EVHELGAELS
ISALLVQVTP ELQALADRSG DHNAHRLDEP YRRALIGVYA RLAGTLTALT GTEALRHAVA
PSTPYATAEE LLADLRTVEA SLASHHGAAL AAARLKPLIR AVQVFGFHLA TVDLRQSSDQ
HEAVLAELMA GARIEADYAA MPEEAKVALL LGLLNDARSL QVRGAVYSER TRGELAIFEA
AREGRALYGH AAIRHCIISH TETVSDLLEV LVLQKEAGLL QGTLDTDARC DLIVVPLFET
ITDLRQAAPI MREFYALPGV LPLVLRSGAD QYCEQDVMLG YSDSNKDGGF FTSNWELYRA
ETALVELFEP LKREHGLTLR LFHGRGGTVG RGGGPSYQAI LAQPPGTVNG QIRLTEQGEV
IASKYANPEI GRRNLETLVA ATLEATLLPP KRHAPKLFLD TADTLSQLSM AAYRKLVYET
PGFADYFFAA TPIREIAELN IGSRPASRKA TRAIEDLRAI PWGFSWGQCR VALPGWYGFG
SAVEGFLGDA PKQRKERLAL LQRMHAQWPF FGTLLSNIDM VLAKSDLAIA TRYVELVPDK
RAAKKIFAAV QAEWQRTDAV LAAITGEPRR LAGNAALARS IEHRLPYIDP LNHLQVELMR
RYRAQQGRGE LHERVQRGIH MSINGVAAGL RNSG
//
