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Database: UniProt/TrEMBL
Entry: B2JEP0_PARP8
LinkDB: B2JEP0_PARP8
Original site: B2JEP0_PARP8 
ID   B2JEP0_PARP8            Unreviewed;      1030 AA.
AC   B2JEP0;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   28-MAR-2018, entry version 72.
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=Bphy_2180 {ECO:0000313|EMBL:ACC71355.1};
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC71355.1, ECO:0000313|Proteomes:UP000001192};
RN   [1] {ECO:0000313|Proteomes:UP000001192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC   {ECO:0000313|Proteomes:UP000001192};
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A.,
RA   Melkonian R., James E.K., Young J.P., Bena G., Hauser L., Land M.,
RA   Kyrpides N., Bruce D., Chain P., Copeland A., Pitluck S., Woyke T.,
RA   Lizotte-Waniewski M., Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad
RT   host range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
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; CP001043; ACC71355.1; -; Genomic_DNA.
DR   RefSeq; WP_012401561.1; NC_010622.1.
DR   STRING; 391038.Bphy_2180; -.
DR   EnsemblBacteria; ACC71355; ACC71355; Bphy_2180.
DR   GeneID; 27741869; -.
DR   KEGG; bph:Bphy_2180; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   BioCyc; BPHY391038:G1GBS-2246-MONOMER; -.
DR   Proteomes; UP000001192; 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   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:UP000001192};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:ACC71355.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ACC71355.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001192}.
FT   ACT_SITE    239    239       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    681    681       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1030 AA;  113693 MW;  C8418134C221BD0C CRC64;
     MTSSGSARPA RRTTASPDAA PASAASTAKA TKAEKARKAT QALDSRKTGK STKTKAIKAK
     APVNGASRRI KADVKPSKAI RHDAPASAVK DDGRTREDKD QPLFEDIRYL GRLLGDVVRE
     QEGDEVFDVV ETIRQTAVRF RREDDSVAAQ ALDKKLRALS PEQTVSVVRA FSYFSHLANI
     AEDRHRNRRH RIHDLAGSTS QPGTIAHALD RLVEANAAAT PVLQQFFNDA LIVPVLTAHP
     TEVQRKSILD AQHDIARLLA ERDQPLTARE HLQNDSLLRA RVTSLWQTRM LRDSRLTVAD
     EIENALSYYR ATFLEEIPQL YADIEEALVE HGLDARLPPF FQMGSWIGGD RDGNPNVTGE
     TLENAITRQA AVIFEHYLEQ VHKLGAELSV SNLLAGASDE LKALAQASPD HSPHRTDEPY
     RRALIGMYTR LAASARVRLG EGVVPVRSAG PGIPPIRAVP YGDSSEFVRD LHVLIDSLAE
     HHGASLATPR LSPLTRAAEV FGFHLASIDL RQSSDIHEAV IAELFKRAGV ESDYAALSEA
     EKLRVLLAEL AQPRLLRSPY VDYSNLVKSE LGVLEQARVT REKFGARAVR NYIISHTETV
     SDLVEVMLLQ KEAGLLQGTL GSATHPARAG LMVIPLFETI PDLRNAPHIM RDLLALPGID
     AIIENQGNEQ EVMLGYSDSN KDGGFLTSNW ELYRAELALV SLFNERGITM RLFHGRGGTV
     GRGGGPTYQA ILSQPPGTVD GQIRLTEQGE VIASKFGNPD IGRRNLETVV AATLEASLLP
     HGSAPKSQLP EFEETMQVLS DAAMASYRAL VYETPGFTDY FFSSTPIAEI AELNIGSRPA
     SRKLQDPKQR KIEDLRAIPW GFSWGQCRLL LTGWYGFGSA VAGWLDAAGA NMERERRLNQ
     LRKMHKVWPF FSNLLSNMDM VLAKTDLAVA SRYAALVTDK KLRKHVFERI VAEWERTSNV
     LSEITGQKER LSDNPLLARS IKNRFPYLDP LNHLQVELLK RHRAGDTNVR VRRGIHLTIN
     GIAAGLRNTG
//
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