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Database: UniProt/TrEMBL
Entry: L0E9V1_THECK
LinkDB: L0E9V1_THECK
Original site: L0E9V1_THECK 
ID   L0E9V1_THECK            Unreviewed;       935 AA.
AC   L0E9V1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   22-NOV-2017, entry version 35.
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=Theco_0339 {ECO:0000313|EMBL:AGA56567.1};
OS   Thermobacillus composti (strain DSM 18247 / JCM 13945 / KWC4).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Thermobacillus.
OX   NCBI_TaxID=717605 {ECO:0000313|EMBL:AGA56567.1, ECO:0000313|Proteomes:UP000010795};
RN   [1] {ECO:0000313|Proteomes:UP000010795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18247 / JCM 13945 / KWC4
RC   {ECO:0000313|Proteomes:UP000010795};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Anderson I.,
RA   Woyke T.;
RT   "Complete sequence of chromosome of Thermobacillus composti KWC4.";
RL   Submitted (JAN-2012) 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; CP003255; AGA56567.1; -; Genomic_DNA.
DR   RefSeq; WP_015253331.1; NC_019897.1.
DR   EnsemblBacteria; AGA56567; AGA56567; Theco_0339.
DR   KEGG; tco:Theco_0339; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000010795; 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:UP000010795};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AGA56567.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010795}.
FT   ACT_SITE    156    156       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    591    591       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   935 AA;  107419 MW;  1DCFF65DCB062613 CRC64;
     MSDQAATQTA QSRPQVSSLL RRDVRYLGNI LGEVLVHQGG QQLLEVVERI REMSKTLRAS
     FDPKLHEEFK QLVESLNPEI RHQVIRAFAI YFQLVNIAEQ IHRIRRKRDY ERSAGAAVQP
     GSIESAVKDL KERGVPVEIV REMIKGISLE LVMTAHPTEA TRRAVLDIHK RMACDVLELD
     NPTLTNRERE RLRDKLLNEV LTLWQTDELR SRKPTVLDEV QNGLFYFDQT LFDVLPDVYE
     ELERCLDKYY PGERWHVPTY LRFGSWIGGD RDGNPSCTSD VTWETFNRHR HLTVSKYRAE
     LRKLMSLLSF STSIVKVSEE LIESIRRDCE AIGDLANLDR WRNDKEPYRI KIGYMLQKLA
     NMKREELKGT PARYNSAEEL KQDLKIIDRS LRYHFADYVA DTHIRKLIRQ VELFGFHLTT
     LDIRQHSKEH ENAIAEILAK MKITPDYAAL DEEEKIRLLD QLLNDPRPLT SPHIEYSDST
     RECLNVFHTV YRAQQEFGVD CVRSYLISMT QGASDMLEVL LFAKEVGLFR RDEDGKVVCT
     LQPVPLFETI DDLHAAPGIM QRVFDLPIYR ASVEAMGQLQ EIMLGYSDSN KDGGVVTANW
     ELRVALNEIT ETGNRYGVKL KFFHGRGGAL GRGGMPLNYS ILAQPPHTIG GGIKITEQGE
     VLSSRYAMQG IAYRSLEQAT SALITAARLA KYPEQNSDKN AEYESIAKEL SERAMKKYQD
     LIFRDPDFLT FFKESTPLNE IGELNIGSRP SKRKNSDRFE DLRAIPWVFA WTQSRFLLPA
     WYAAGTAMAE YVGGDEAKLD KLRRAYVEFP FFRTLIDNLQ MALAKADMHI AKEYAGMIKD
     PAIRDRIFGM IEREYELTTE MILRVTGQKE ILDNVPIIQE SIRLRNPYVD PLSYLQVQLL
     TELRALRVRG EDDPHLLREV LLTINGIAAG LRNTG
//
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