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Database: UniProt/TrEMBL
Entry: A0A0D5LBW8_9BURK
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ID   A0A0D5LBW8_9BURK        Unreviewed;       994 AA.
AC   A0A0D5LBW8;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   22-NOV-2017, entry version 17.
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   ORFNames=BW21_2956 {ECO:0000313|EMBL:AJY41159.1};
OS   Burkholderia sp. 2002721687.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1468409 {ECO:0000313|EMBL:AJY41159.1, ECO:0000313|Proteomes:UP000032645};
RN   [1] {ECO:0000313|EMBL:AJY41159.1, ECO:0000313|Proteomes:UP000032645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2002721687 {ECO:0000313|EMBL:AJY41159.1};
RX   PubMed=25931592;
RA   Johnson S.L., Bishop-Lilly K.A., Ladner J.T., Daligault H.,
RA   Jaissle J., Frey K.G., Koroleva G.I., Bruce D.C., Coyne S.R.,
RA   Broomall S.M., Li P., Teshima H., Gibbons H.S., Palacios G.F.,
RA   Rosenzweig C.N., McMurry K., Redden C.L., Xu Y., Currie B., Mayo M.,
RA   Minogue T.D., Chain P.S.;
RT   "Complete genome sequences for 59 burkholderia isolates, both
RT   pathogenic and near neighbor.";
RL   Genome Announc. 3:0-0(2015).
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: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; CP009549; AJY41159.1; -; Genomic_DNA.
DR   RefSeq; WP_043282073.1; NZ_CP009549.1.
DR   EnsemblBacteria; AJY41159; AJY41159; BW21_2956.
DR   KEGG; bul:BW21_2956; -.
DR   PATRIC; fig|1468409.3.peg.3296; -.
DR   KO; K01595; -.
DR   Proteomes; UP000032645; 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_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:UP000032645};
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:AJY41159.1}.
FT   ACT_SITE    204    204       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    646    646       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   994 AA;  108938 MW;  7FF88FB394E4DEAC CRC64;
     MKSSGSARAT RRNAVSSSSA PANAELPARR AAKPARKRNG AAVRTIAPTN AASAKPQGRT
     REDKDRPLFE DIRYLGRLLG DVVREQEGDA VFDIVETIRQ TAVKFRREDD KAAAQTLEKM
     LRKLTPDQTV SVVRAFSYFS HLANIAEDRH HNRRRRIHAL AGSAPQAGTV AYALDRLRQA
     GDASPKTIKQ FFEGALIVPV LTAHPTEVQR KSILDAQHDI ARLLAERDQP LTARELAHNE
     ALLRARVTTL WQTRMLRDAR LTVADEIENA LSYYRATFLD ELPALYADIE EALAEHGLPA
     RVPAFFQMGS WIGGDRDGNP NVTATTLDEA ITRQAAVIFE HYLEQVHKLG AELSASNLLV
     GASDALKALA AASPDQSPHR VDEPYRRALI GVYTRLAASA RVRLGEGAVP VRSAGRGAAP
     VRATPYADAE EFVADLRVLT DSLALHHGES LATPRLAPLT RAAEVFGFHL ASIDLRQSSD
     IHEAVIAELL ARGGVEPDYA ALPEADKLRV LLAALADPRP LRSPYLDYSD LAKSELGVLE
     RARAIRAQFG ARAVRNYIIS HTETVSDLVE VLLLQKETGL FEGTLGTPHA NARNGLMAIP
     LFETIADLRN ASDIMREFFA LPGVGELLAH QGHEQEVMLG YSDSNKDGGF LTSNWELYRG
     ELALVDLFHE RGIKLRLFHG RGGTVGRGGG PTYQAILSQP PGTVNGQIRL TEQGEVIASK
     FSNPEIGRRN LETVVAATLE ATLAPHSNAP KQLPAFEAAM QALSDAAMAS YRALVYETPG
     FTDYFFSSTP ITEIAELNIG SRPASRKLQD PKNRRIEDLR AIPWGFSWGQ CRLLLTGWYG
     FGSAVAAYLD GAPDAAERGK RVALLKKMNK TWPFFANLLS NMDMVLAKTD LAVASRYAQL
     VADKKLRKHV FERIVAEWHR TADALAEITG TEARLAANPL LARSIKNRFP YLDPLNHLQV
     ELIKRHRAGD SNARLRRGIH LTINGIAAGL RNTG
//
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