CAPPA_METTH
ID CAPPA_METTH Reviewed; 483 AA.
AC O27026;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Phosphoenolpyruvate carboxylase;
DE Short=PEPC;
DE Short=PEPCase;
DE EC=4.1.1.31;
GN Name=ppcA; OrderedLocusNames=MTH_943;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=15262949; DOI=10.1128/jb.186.15.5129-5137.2004;
RA Patel H.M., Kraszewski J.L., Mukhopadhyay B.;
RT "The phosphoenolpyruvate carboxylase from Methanothermobacter
RT thermautotrophicus has a novel structure.";
RL J. Bacteriol. 186:5129-5137(2004).
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:0000269|PubMed:15262949}.
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:0000269|PubMed:15262949};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15262949};
CC -!- ACTIVITY REGULATION: Inhibited by NaCl, KCl, ATP, ADP, GTP and
CC aspartate. Unlike E.coli, not regulated by acetyl-CoA.
CC {ECO:0000269|PubMed:15262949}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 mM for KHCO(3) {ECO:0000269|PubMed:15262949};
CC KM=0.46 mM for phosphoenolpyruvate {ECO:0000269|PubMed:15262949};
CC pH dependence:
CC Optimum pH is 6.8. {ECO:0000269|PubMed:15262949};
CC Temperature dependence:
CC Optimum temperature is 62 degrees Celsius.
CC {ECO:0000269|PubMed:15262949};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15262949}.
CC -!- SIMILARITY: Belongs to the PEPCase type 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85441.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000666; AAB85441.1; ALT_INIT; Genomic_DNA.
DR PIR; D69226; D69226.
DR RefSeq; WP_048060929.1; NC_000916.1.
DR AlphaFoldDB; O27026; -.
DR SMR; O27026; -.
DR STRING; 187420.MTH_943; -.
DR EnsemblBacteria; AAB85441; AAB85441; MTH_943.
DR GeneID; 24854079; -.
DR KEGG; mth:MTH_943; -.
DR PATRIC; fig|187420.15.peg.927; -.
DR HOGENOM; CLU_517433_0_0_2; -.
DR OMA; QSAFRYD; -.
DR BioCyc; MetaCyc:MON-14528; -.
DR SABIO-RK; O27026; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IDA:UniProtKB.
DR GO; GO:0015977; P:carbon fixation; IDA:UniProtKB.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IDA:UniProtKB.
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 Pfam; PF14010; PEPcase_2; 1.
DR PIRSF; PIRSF006677; UCP006677; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR TIGRFAMs; TIGR02751; PEPCase_arch; 1.
PE 1: Evidence at protein level;
KW Carbon dioxide fixation; Direct protein sequencing; Lyase; Magnesium;
KW Reference proteome.
FT CHAIN 1..483
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000309600"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 55078 MW; DA053C2E9C7F565A CRC64;
MKVPRCMSTQ HPDNVNPPFF AEEPELGGED EIREAYYVFS HLGCDEQMWD CEGKEVDNYV
VKKLLTKYQA FFRDHVLGED LRLTLRVPNP TVERAEAKIL LETLESIPRS YDTASLFYGM
DAAPVFEVIL PMTSSSSCLN RIHSYYLDFV KGKERLQLAD GVTVKEWIGE FRPDEINVIP
LFEDHEGMLN AAKITGEYLD GKDIQEQRVF LARSDPAMNY GMISATLLNR IALSDFRDLE
EESGVKLYPI IGMGSAPFRG NLRPDNVEDV TWEYRGAYTF TVQSSFKYDH EPSDVIRGIK
KLRSVKPGRA AEIERESVLE IISAYCREYR RQVMDLVDII NRVARYVPGR RKRKLHIGLF
GYSRSMGNVS LPRAITFTAA LYSLGVPPEL LGFNALSSGD LEFIEEVYPG LGRDLHDAAR
YANPESPFLS PEVKSSFEEY LEPEYDEGHM KTTEEIIRAL RINRTANLQE LILEAASQRK
FLG
