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Database: UniProt/TrEMBL
Entry: A0A088XJ87_9BURK
LinkDB: A0A088XJ87_9BURK
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ID   A0A088XJ87_9BURK        Unreviewed;       952 AA.
AC   A0A088XJ87;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   28-MAR-2018, entry version 20.
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=DM82_444 {ECO:0000313|EMBL:AIO65219.1};
OS   Burkholderia oklahomensis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=342113 {ECO:0000313|EMBL:AIO65219.1, ECO:0000313|Proteomes:UP000029424};
RN   [1] {ECO:0000313|EMBL:AIO65219.1, ECO:0000313|Proteomes:UP000029424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EO147 {ECO:0000313|EMBL:AIO65219.1,
RC   ECO:0000313|Proteomes:UP000029424};
RA   Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA   Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S.,
RA   Gu W., Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA   Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA   Scholz M.B., Teshima H., Xu Y.;
RL   Submitted (JUN-2014) 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: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; CP008726; AIO65219.1; -; Genomic_DNA.
DR   EnsemblBacteria; AIO65219; AIO65219; DM82_444.
DR   KEGG; bok:DM82_444; -.
DR   KO; K01595; -.
DR   Proteomes; UP000029424; 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:UP000029424};
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:AIO65219.1}.
FT   ACT_SITE    162    162       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    604    604       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   952 AA;  104844 MW;  0C267FC16F3D7A8A CRC64;
     MNAARPASAA PAKPHGRTRE DKDRPLFEDI RYLGRLLGDV VREQEGDDVF HVVETIRQTA
     VKFRREDDSA AAQTLEKMLR KLTPEQTVSV VRAFSYFSHL ANIAEDRHHN RRRRIHALAG
     SAPQAGTVAY ALDKLKEAGD ASPKVIKRFF EGALIVPVLT AHPTEVQRKS ILDAQHDIAH
     LLAERDQPLT AREFAHNEAL LRARVTTLWQ TRMLRDARLT VADEIENALS YYRATFLDEL
     PALYADIEEA LAEHGLPARV PAFFQMGSWI GGDRDGNPNV TAATLDEAIN RQAAVIFEHY
     LEQVHKLGAE LSVSNLLVGA NDALKALAAA SPDQSPHRVD EPYRRALIGV YTRLAASARV
     RLGEGAVPVR SAGRGAAPVR ATPYADAEEF AADLRVLTDS LALHHGESLA TPRLAPLMRA
     AEVFGFHLAS IDLRQSSDIH EAVIAELLAR GGVEPDYAAL AEADKLRVLL AALADPRPLR
     SPYLDYSDLA KSELGVLERA HAIRAQFGPR AVRNYIISHT ETVSDLVEVL LLQKETGLFE
     GTLGTPHANA RNGLMAIPLF ETIADLRNAP DIMREFFALP GVGELVAHQG HEQEVMLGYS
     DSNKDGGFLT SNWELYRAEL ALVDLFSERG IKLRLFHGRG GTVGRGGGPT YQAILSQPPG
     TVNGQIRLTE QGEVIASKFA NPEIGRRNLE TVVAATLEAT LLPHRNAPKQ LPAFEAAMQA
     LSDAAMASYR ALVYETPGFT DYFFSSTPIT EIAELNIGSR PASRKLQDPK NRKIEDLRAI
     PWGFSWGQCR LLLTGWYGFG SAVAAFLDGT KDVAERAKRV ALLKKMNKTW PFFAHLLSNM
     DMVLAKTDLA VASRYAQLVA DKKLRKHVFE RIVSEWHRTS DALAEITGSD ARLAANPLLA
     RSIKNRFPYL DPLNHLQVEL IKRHRSGDTN ARLRRGIHLT INGIAAGLRN TG
//
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