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Database: UniProt
Entry: I7KCZ4_METBM
LinkDB: I7KCZ4_METBM
Original site: I7KCZ4_METBM 
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
//
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