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 25-MAY-2022, entry version 87.
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}; OrderedLocusNames=PAE3416;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
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-carbon
CC dicarboxylic acid source for the tricarboxylic acid cycle.
CC {ECO:0000255|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:0000255|HAMAP-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. {ECO:0000255|HAMAP-
CC Rule:MF_01904}.
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DR EMBL; AE009441; AAL64899.1; -; Genomic_DNA.
DR AlphaFoldDB; 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 HOGENOM; CLU_517433_0_0_2; -.
DR InParanoid; Q8ZT64; -.
DR OMA; IYGCDEV; -.
DR Proteomes; UP000002439; 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 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; Lyase; Magnesium; Reference proteome.
FT CHAIN 1..460
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="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
