CAPPA_CALMQ
ID CAPPA_CALMQ Reviewed; 512 AA.
AC A8MBK0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=Cmaq_1916;
OS Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS IC-167).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Caldivirga.
OX NCBI_TaxID=397948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Caldivirga maquilingensis IC-167.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000852; ABW02733.1; -; Genomic_DNA.
DR RefSeq; WP_012186952.1; NC_009954.1.
DR AlphaFoldDB; A8MBK0; -.
DR SMR; A8MBK0; -.
DR STRING; 397948.Cmaq_1916; -.
DR EnsemblBacteria; ABW02733; ABW02733; Cmaq_1916.
DR GeneID; 5709298; -.
DR KEGG; cma:Cmaq_1916; -.
DR eggNOG; arCOG04435; Archaea.
DR HOGENOM; CLU_517433_0_0_2; -.
DR OMA; QSAFRYD; -.
DR OrthoDB; 23334at2157; -.
DR Proteomes; UP000001137; 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..512
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_1000088477"
SQ SEQUENCE 512 AA; 57872 MW; E8B4DF81D2E0A96F CRC64;
MRIIPRTMCT QHPDYANVPQ WVVNDFIKGD DEVYEAYMNY SIYDCQETMW DFEGKDVDIY
VVRKLLENYG GFFINKVLGE DIYLTYRLPN PNVEASDRKI FAEALETIPM AYDLARVFYG
KPVKAIFEVI FPLTSSSRDL IMTLRYYERI VAGKCSVELD DGLKVSDVIG EVEPKTIEVI
PLVEDMESLV RIDSIIEGYV KVAKPQYLRV FIARSDPAMN YGLIPAVLLA KIALSRVYAI
GNSLGLSIYP IIGVGPTPFR GNFNPRNVNN TLKEYPGVYT FTVQSAFRYD YPVDNAKDAI
NLINNSKPTE PVILSSDEEE LALTIIRQYT DRYQAEVEGL ANAVNYIAQL LPPRRTRRLH
IGLFGYGRGF RGVTLPRAIA FVGALYSIGI PPEILGLSTL LKLNERQWGV LEGNYVNLWS
DLSDAAQYIC MECIEQLPSM KSELRVSKET IAMVLEDIKA IDELGVKVSS PGFEQRKHAL
LTKLFLESVN NSYINDAKAY LLDMAKVRRA IG