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Database: UniProt/SWISS-PROT
Entry: CAPPA_PYRAE
LinkDB: CAPPA_PYRAE
Original site: CAPPA_PYRAE 
ID   CAPPA_PYRAE             Reviewed;         460 AA.
AC   Q8ZT64;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   07-JUN-2017, entry version 76.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_01904};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_01904};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_01904};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_01904};
GN   Name=ppcA {ECO:0000255|HAMAP-Rule:MF_01904};
GN   OrderedLocusNames=PAE3416;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630
OS   / NBRC 100827).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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:0000255|HAMAP-Rule:MF_01904}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000255|HAMAP-
CC       Rule:MF_01904}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01904};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01904}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01904}.
DR   EMBL; AE009441; AAL64899.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q8ZT64; -.
DR   SMR; Q8ZT64; -.
DR   STRING; 178306.PAE3416; -.
DR   EnsemblBacteria; AAL64899; AAL64899; PAE3416.
DR   KEGG; pai:PAE3416; -.
DR   PATRIC; fig|178306.9.peg.2568; -.
DR   eggNOG; arCOG04435; Archaea.
DR   eggNOG; COG1892; LUCA.
DR   HOGENOM; HOG000009826; -.
DR   InParanoid; Q8ZT64; -.
DR   KO; K01595; -.
DR   OMA; YIQPRDI; -.
DR   OrthoDB; POG093Z01LI; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Carbon dioxide fixation; Complete proteome; Lyase; Magnesium;
KW   Reference proteome.
FT   CHAIN         1    460       Phosphoenolpyruvate carboxylase.
FT                                /FTId=PRO_0000309607.
SQ   SEQUENCE   460 AA;  51486 MW;  A2FD72765E7E385C CRC64;
     MYIPCLMCTQ HPDSTVKITA GEEVDEAVVA FLAYGCDEVM VDYEGKATPY SQPRDVASKA
     LALGLPLGER FFITPRVPNP RLEDFERSML SLEAAVLANS YSQRAAGVQA VKWVVLPMTE
     DVETMAFVYK ALDMKARDLA ELNAVKRDSS IELIPLVEDA MRQIKIESFI KALFRTAAQS
     GRILEHMRIF LGISDSAVRH GHMASALAMV KALGQISEIN RDGEFKISPI VGMGSPPFRG
     GLNNPHLAVP EAAQYAGYKT ATIQSAVRYD VSYAEYQKVR EAILSVYTPR RLHVEEAWIT
     KASELYREAI RPYIGKIAEL ANAIPSTRDR VSWREYGRVI EGVEWRVPRA IVYTATWYFA
     GVPPTLLDAR FIAWAYKNDL LDDVLRALPA TVEEWKFESR FYSRERAEKT LGGEIVKDID
     NAFDILGIKP EPDRTYITLL NSADTQPHAI ALGRIRGFLG
//
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