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Database: UniProt/TrEMBL
Entry: Q0BCU8_BURCM
LinkDB: Q0BCU8_BURCM
Original site: Q0BCU8_BURCM 
ID   Q0BCU8_BURCM            Unreviewed;       998 AA.
AC   Q0BCU8;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-SEP-2017, entry version 80.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
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:SAAS00635171};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=Bamb_2469 {ECO:0000313|EMBL:ABI88025.1};
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670 {ECO:0000313|EMBL:ABI88025.1, ECO:0000313|Proteomes:UP000000662};
RN   [1] {ECO:0000313|Proteomes:UP000000662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD {ECO:0000313|Proteomes:UP000000662};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) 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}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00635164};
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:SAAS00635168}.
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DR   EMBL; CP000440; ABI88025.1; -; Genomic_DNA.
DR   RefSeq; WP_011657640.1; NZ_CP009798.1.
DR   STRING; 339670.Bamb_2469; -.
DR   EnsemblBacteria; ABI88025; ABI88025; Bamb_2469.
DR   KEGG; bam:Bamb_2469; -.
DR   PATRIC; fig|339670.21.peg.2446; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000000662; Chromosome 1.
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   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:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000662};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:ABI88025.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:ABI88025.1}.
FT   ACT_SITE    211    211       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    650    650       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   998 AA;  109755 MW;  9CC624BBFDB15FF6 CRC64;
     MKSSGSARTT RRNAALPSSD AQTGTIATAA NGRAKTATKP KDPIPRTKRT IKASGPAART
     AKPGVRTRED KDGPLFEDIR FLGRLLGDVV REQEGDTVFD VVETIRQTAV KFRREDDSEA
     AQTLEKKLRK LTPEQTVSVV RAFSYFSHLA NIAEDRHHNR RRRIHALAGS APQPGTVAYA
     LEQLKTTGNA SKRLLQRFFD DALIVPVLTA HPTEVQRKSI LDAQHDIARL LAERDQPLTA
     RERSYNESML RARVTALWQT RMLRDSRLTV GDEIENALSY YRATFLDELP ALYGDIEAAL
     AEHGLPARVP AFLQMGSWIG GDRDGNPNVT GPTLDEAINR QAAVILEHYL EQVHKLGAEL
     SVSNLLVGAN DAVKALAAAS PDQSPHRVDE PYRRALIGIY TRLAASARVR LGEGTVPVRS
     AGRGAPPVRA IPYADSEAFV ADLKVLTASL EEHHGASLAA PRLTPLVRAA EVFGFHLASI
     DLRQSSDIHE AVVAELFARA GVEADYAALA EEDKLRVLLA ALADPRPLRS PYLEYSALAQ
     SELGVFEKAR EVRAQFGARA VRNYIISHTE TVSDLVEVLL LQKETGLLEG PLGSHAKNGL
     MVIPLFETIP DLRDAARIMR EYFALPGIDA LIAHQGAEQE VMLGYSDSNK DGGFLTSNWE
     LYRAELALVD VFRERKITLR LFHGRGGTVG RGGGPTYQAI LSQPPGTVNG QIRLTEQGEV
     IASKFANPEI GRRNLETVVA ATLEASLLPQ SNAPAQLPAF EAAMQTLSDA AMASYRALVY
     ETPGFTDYFF SSTPITEIAE LNIGSRPASR KLQDPKNRKI EDLRAIPWGF SWGQCRLLLT
     GWYGFGSAVS AYLDGAPDEA ERTKRLTLLK KMNKTWPFFA NLLSNMDMVL AKTDLAVASR
     YAQLVADRKL RKHVFERIVA EWERTSQALA EITGHEGRLA TNPLLARSIK NRFPYLDPLN
     HLQVELIKRH RAGDTNARLR RGIHLTINGI AAGLRNTG
//
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