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Database: UniProt/TrEMBL
Entry: A0A160VTH5_9EURY
LinkDB: A0A160VTH5_9EURY
Original site: A0A160VTH5_9EURY 
ID   A0A160VTH5_9EURY        Unreviewed;       469 AA.
AC   A0A160VTH5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   25-OCT-2017, entry version 11.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_01904};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_01904};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_01904};
DE            EC=4.1.1.31 {ECO:0000256|HAMAP-Rule:MF_01904};
GN   Name=ppcA {ECO:0000256|HAMAP-Rule:MF_01904};
GN   ORFNames=CHITON_0092 {ECO:0000313|EMBL:CUX76871.1};
OS   Thermococcus chitonophagus.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=54262 {ECO:0000313|EMBL:CUX76871.1, ECO:0000313|Proteomes:UP000093069};
RN   [1] {ECO:0000313|EMBL:CUX76871.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1 {ECO:0000313|EMBL:CUX76871.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01904}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-
CC       Rule:MF_01904}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01904};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01904}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 2 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01904}.
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DR   EMBL; LN999010; CUX76871.1; -; Genomic_DNA.
DR   RefSeq; WP_068575722.1; NZ_LN999010.1.
DR   EnsemblBacteria; CUX76871; CUX76871; CHITON_0092.
DR   GeneID; 33321006; -.
DR   KEGG; tch:CHITON_0092; -.
DR   KO; K01595; -.
DR   Proteomes; UP000093069; Chromosome i.
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 {ECO:0000256|HAMAP-Rule:MF_01904};
KW   Complete proteome {ECO:0000313|Proteomes:UP000093069};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01904, ECO:0000313|EMBL:CUX76871.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01904};
KW   Pyruvate {ECO:0000313|EMBL:CUX76871.1}.
SQ   SEQUENCE   469 AA;  54019 MW;  9CDE7B9BFAE53C3A CRC64;
     MIPRIMSTQH PDNYSIPFFS HSPVLGGEDE ITEAFYAYSV LGADEQMWDF EGKEVDEFVV
     KKLLERYPMF FRKNILGKDL RLTPRVPNPT VEKAEAKLLL ETLQGITRAA DYARLFYNDS
     IAPIFEVILP MTTSSAELER VYSLYKRIVS ISDELIHDVT VREWIGEFYP KEIRVIPLFE
     TKSALLKSSR IVKEYLDGKD FEYQRVFFAR SDPAMNYGLI TAVTYVKKAL YELSKLEEEL
     SIPLYPIVGV GGPPFRGGMR PDNVDAVLRE YPSVQTYTIQ SSFKFDNPAR EVVKAVDKIK
     ATKRGKPIPV EIPDFLMEYE VEYQSQIKIL APHIRRMASK IPDRRRRKLH IGLFGYARKV
     NGQALPRAIK FTASLYSIGL PPELLALNAI SDKQLEKISE YYLNVYEDLE FAMQFFSYKV
     AEEVGLKKLA DRIREFKPDI HEEYVREAES VFKGEGDVMK LAQMRGFLG
//
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