CAPPA_THEPD
ID CAPPA_THEPD Reviewed; 464 AA.
AC A1RZN3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=Tpen_1265;
OS Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=368408;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2475 / Hrk 5;
RX PubMed=18263724; DOI=10.1128/jb.01949-07;
RA Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT biosynthetic pathways without genome reduction.";
RL J. Bacteriol. 190:2957-2965(2008).
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; CP000505; ABL78663.1; -; Genomic_DNA.
DR RefSeq; WP_011752928.1; NC_008698.1.
DR AlphaFoldDB; A1RZN3; -.
DR SMR; A1RZN3; -.
DR STRING; 368408.Tpen_1265; -.
DR EnsemblBacteria; ABL78663; ABL78663; Tpen_1265.
DR GeneID; 4600480; -.
DR KEGG; tpe:Tpen_1265; -.
DR eggNOG; arCOG04435; Archaea.
DR HOGENOM; CLU_517433_0_0_2; -.
DR OMA; QSAFRYD; -.
DR OrthoDB; 23334at2157; -.
DR Proteomes; UP000000641; 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..464
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000309617"
SQ SEQUENCE 464 AA; 51243 MW; 174AF466FC739834 CRC64;
METPRLMCTQ HPDSTVKVPV QEEVEEAVRS FLVYGCDEVM SDYEGKLTPY AQPKEIVVKA
GELGVPVGEG FYVTVRAPNP RLEDFDRVDL ALEAAVLANY YSYKRLGVQA VRWVVLPMTD
SAETVRLVQR LLARKTRVLC EEVGQPCEQA QLVPLLEDVD SLLRVREILR DLHSALAELG
SDPGVLRVFL GKSDSALKAG HIASALSLLY ALGESAKAGE ELGLEVKPIL GGGSPPFRGG
VNNPRLVGVE VQRYRGYSTV TVQSAVRYDA SFSEYQEVRS KLLGGAGGEP GDAGGRVAEL
ARLAASMYRS LASKYLDFVN EYARSVPTTR DRVSWREYGR ALELEDKLFS APRAIVYTAA
WYSLGVPPTF LDADFVLEAY RGDFLDEVLG YLPGLEEEWR YDAQFYLPRL AGERLGEELV
KKVDEALDAM GLRPEPLEPY EKLARTAPAE LRALLLGKVR GFLG