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Database: UniProt/TrEMBL
Entry: C7RT89_ACCPU
LinkDB: C7RT89_ACCPU
Original site: C7RT89_ACCPU 
ID   C7RT89_ACCPU            Unreviewed;       918 AA.
AC   C7RT89;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   28-MAR-2018, entry version 65.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=CAP2UW1_1517 {ECO:0000313|EMBL:ACV34832.1};
OS   Accumulibacter phosphatis (strain UW-1).
OC   Bacteria; Proteobacteria; Betaproteobacteria;
OC   Candidatus Accumulibacter.
OX   NCBI_TaxID=522306 {ECO:0000313|EMBL:ACV34832.1, ECO:0000313|Proteomes:UP000001619};
RN   [1] {ECO:0000313|EMBL:ACV34832.1, ECO:0000313|Proteomes:UP000001619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UW-1 {ECO:0000313|EMBL:ACV34832.1,
RC   ECO:0000313|Proteomes:UP000001619};
RG   US DOE Joint Genome Institute;
RA   Martin H.G., Ivanova N., Kunin V., Warnecke F., Barry K., He S.,
RA   Salamov A., Szeto E., Dalin E., Pangilinan J.L., Lapidus A., Lowry S.,
RA   Kyrpides N.C., McMahon K.D., Hugenholtz P.;
RT   "Complete sequence of chromosome of Candidatus Accumulibacter
RT   phosphatis clade IIA str. UW-1.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595, ECO:0000256|SAAS:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946753}.
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DR   EMBL; CP001715; ACV34832.1; -; Genomic_DNA.
DR   RefSeq; WP_015766053.1; NC_013194.1.
DR   STRING; 522306.CAP2UW1_1517; -.
DR   EnsemblBacteria; ACV34832; ACV34832; CAP2UW1_1517.
DR   KEGG; app:CAP2UW1_1517; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000001619; 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_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946757};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001619};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:ACV34832.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ACV34832.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001619}.
FT   ACT_SITE    148    148       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    581    581       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   918 AA;  101697 MW;  2BC6791B5AEA8DC0 CRC64;
     MTEAFPEDKD LPLREDIRLL GRLLGDTLRA QEGEATFELV ERIRVSAIRF HRDEDSGARQ
     ELAAILDSLS RDQTQTVVRA FSHFSHLANI AEDQHHIRRS RAHLIAGSPP HAGSLAHALA
     RARAAGCDVA QLYGFFDDAS IVPVLTAHPT EVQRKSTLNG QRAIAHLLHR RDNSRLTPDE
     QESLDEGLRR AVLALWQTRM LRTTRLMVLD EVANGLSYYD YTFLRELPRL YCWLEDHLAA
     ADGGRPASEL PGFLQLGSWM GGDRDGNPFV TAPVTRAALR LQSACALRFH LDEIHALGAE
     LSLAEGLVSV SDALQSLADS SPDTAAARSD EPYRRALTGI YARLAATARK LDGLEPERHP
     VGESAPYANC GEFAADLDVI HRSLVANGSQ LLARGRLRTL RRAARVFGFH LAALDLRQNS
     EVHERVVGEL LEAASPGTNY REHDEAGRVE LLLREISSTR PLASSHLAYS DETRGELEIF
     RTAADAHRAF GSQAVQNYII SKTDGVSDLL EVALLLKECG LLLPQSRELA VNIVPLFETI
     PDLRNCPRVM DEVLSLPAYR RLVASRGDLQ EVMLGYSDSN KDGGFLTSGW ELYRAEIALV
     EVFARHGVKL RLFHGRGGSV GRGGGPSYQA ILAQPGGAVQ GRLRLTEQGE VIASKYSNPE
     VGRRNLEILA SAVLEATLLA APDPAPQPEY LEAMAMLSQS AYRAYRGLVY ETEGFERYFW
     ESTVIAEIAH LNIGSRPASR KKTTAIEDLR AIPWVFSWAQ CRLMLPGWYG FGTAVREFLA
     VHPEGLEVLQ RMHHEWGFFR TLLSNMDMVL AKTDLAIAAR YAELVTDPAL RAAIFPRLKA
     EWQATIDALL AISGQQCLLE DNPLLARSIR NRFPYLDPLN HLQIELIRRL RAGNEDERVK
     RAIHLTINGI AAGLRNSG
//
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