ID I7KCZ4_METBM Unreviewed; 485 AA.
AC I7KCZ4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_01904};
DE Short=PEPC {ECO:0000256|HAMAP-Rule:MF_01904};
DE Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_01904};
DE EC=4.1.1.31 {ECO:0000256|HAMAP-Rule:MF_01904};
GN Name=ppcA {ECO:0000256|HAMAP-Rule:MF_01904,
GN ECO:0000313|EMBL:CCJ36381.1};
GN OrderedLocusNames=BN140_1458 {ECO:0000313|EMBL:CCJ36381.1};
OS Methanoculleus bourgensis (strain ATCC 43281 / DSM 3045 / OCM 15 / MS2)
OS (Methanogenium bourgense).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=1201294 {ECO:0000313|EMBL:CCJ36381.1, ECO:0000313|Proteomes:UP000009007};
RN [1] {ECO:0000313|Proteomes:UP000009007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43281 / DSM 3045 / OCM 15 / MS2
RC {ECO:0000313|Proteomes:UP000009007};
RX PubMed=22965103; DOI=10.1128/JB.01292-12;
RA Maus I., Wibberg D., Stantscheff R., Eikmeyer F.G., Seffner A., Boelter J.,
RA Szczepanowski R., Blom J., Jaenicke S., Konig H., Puhler A., Schluter A.;
RT "Complete genome sequence of the hydrogenotrophic, methanogenic archaeon
RT Methanoculleus bourgensis strain MS2T, isolated from a sewage sludge
RT digester.";
RL J. Bacteriol. 194:5487-5488(2012).
CC -!- FUNCTION: Catalyzes the irreversible beta-carboxylation of
CC phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon
CC dicarboxylic acid source for the tricarboxylic acid cycle.
CC {ECO:0000256|HAMAP-Rule:MF_01904}.
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|HAMAP-Rule:MF_01904};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01904};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01904}.
CC -!- SIMILARITY: Belongs to the PEPCase type 2 family. {ECO:0000256|HAMAP-
CC Rule:MF_01904}.
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DR EMBL; HE964772; CCJ36381.1; -; Genomic_DNA.
DR AlphaFoldDB; I7KCZ4; -.
DR STRING; 1201294.BN140_1458; -.
DR KEGG; mbg:BN140_1458; -.
DR PATRIC; fig|1201294.9.peg.1607; -.
DR HOGENOM; CLU_517433_0_0_2; -.
DR BioCyc; MBOU1201294:BN140_RS07260-MONOMER; -.
DR Proteomes; UP000009007; 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 HAMAP; MF_01904; PEPcase_type2; 1.
DR InterPro; IPR007566; PEP_COase_arc-type.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR NCBIfam; TIGR02751; PEPCase_arch; 1.
DR Pfam; PF14010; PEPcase_2; 1.
DR PIRSF; PIRSF006677; UCP006677; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01904};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01904, ECO:0000313|EMBL:CCJ36381.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01904};
KW Pyruvate {ECO:0000313|EMBL:CCJ36381.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009007}.
SQ SEQUENCE 485 AA; 54857 MW; 0369FAFE317A5C0B CRC64;
MLRIPQCMST QHPDNVNLPF FAESPELGGE DEVQEAYYAY SHLGCTEQMW DCEGKEVDNF
VVRKLLSRYD AFFREKRLGR DVFLTLRVPN PEVETAEAKI LLETLESIPR SYDTACLFYG
DECPPIFEVI LPMTASHTAI DNIYRYYTDI VVGKQERSLG EGGMTIADWI GRFRPDRINV
IPLFEEMDHM LDAHNAVRRY LEGKDITHQR VFLARSDPAM NYGIVSAVLL NKIALQHLQE
VSEETGTGIY PIIGVGSAPF RGGLSPRTVD QVTAEYPSVH TFTVQSAFKY DYPLEEVQNA
VRRLEERRPG RPRPVDEAAA LDLIERYTRA YERRLGPLAP LINRVARYVP ERRKRKLHIG
LFGYARSTGG ITLPRAIKFT AALYSVGFPP EILGLDALDD TDIGFVRETY VNFDENLKAA
ARYLNTETGL VPRELAARVA DLVDIEPDEE HAEVTAEIAR ALRENDIGKL SALVLQAAHC
RKFLG
//