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Database: UniProt/SWISS-PROT
Entry: CAPPA_METTH
LinkDB: CAPPA_METTH
Original site: 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   07-JUN-2017, entry version 85.
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 /
OS   JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   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.,
RA   Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D.,
RA   Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R.,
RA   Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S.,
RA   McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M.,
RA   Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum
RT   deltaH: functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   ENZYME 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-
CC       carbon dicarboxylic acid source for the tricarboxylic acid cycle.
CC       {ECO:0000269|PubMed:15262949}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000269|PubMed:15262949}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:15262949};
CC   -!- ENZYME 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
CC         {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=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; AE000666; AAB85441.1; ALT_INIT; Genomic_DNA.
DR   PIR; D69226; D69226.
DR   RefSeq; WP_048060929.1; NC_000916.1.
DR   SMR; O27026; -.
DR   STRING; 187420.MTH943; -.
DR   EnsemblBacteria; AAB85441; AAB85441; MTH_943.
DR   GeneID; 24854079; -.
DR   KEGG; mth:MTH_943; -.
DR   PATRIC; fig|187420.15.peg.927; -.
DR   eggNOG; arCOG04435; Archaea.
DR   eggNOG; COG1892; LUCA.
DR   KO; K01595; -.
DR   OMA; PAMNYGL; -.
DR   OrthoDB; POG093Z01LI; -.
DR   BioCyc; MetaCyc:MONOMER-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; Complete proteome; Direct protein sequencing;
KW   Lyase; Magnesium; Reference proteome.
FT   CHAIN         1    483       Phosphoenolpyruvate carboxylase.
FT                                /FTId=PRO_0000309600.
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
//
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