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Database: UniProt/TrEMBL
Entry: A0A127Q740_9BURK
LinkDB: A0A127Q740_9BURK
Original site: A0A127Q740_9BURK 
ID   A0A127Q740_9BURK        Unreviewed;       949 AA.
AC   A0A127Q740;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-SEP-2017, entry version 10.
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   ORFNames=CPter91_3567 {ECO:0000313|EMBL:AMP05888.1};
OS   Collimonas pratensis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=279113 {ECO:0000313|EMBL:AMP05888.1, ECO:0000313|Proteomes:UP000074561};
RN   [1] {ECO:0000313|EMBL:AMP05888.1, ECO:0000313|Proteomes:UP000074561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter91 {ECO:0000313|EMBL:AMP05888.1,
RC   ECO:0000313|Proteomes:UP000074561};
RA   Song C., Schmidt R., de Jager V., Krzyzanowska D., Jongedijk E.,
RA   Cankar K., Beekwilder J., van Veen A., de Boer W., van Veen J.A.,
RA   Garbeva P.;
RT   "Exploring the genomic traits of fungus-feeding bacterial genus
RT   Collimonas.";
RL   Submitted (NOV-2015) 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; CP013234; AMP05888.1; -; Genomic_DNA.
DR   EnsemblBacteria; AMP05888; AMP05888; CPter91_3567.
DR   KEGG; cpra:CPter91_3567; -.
DR   PATRIC; fig|279113.9.peg.3537; -.
DR   KO; K01595; -.
DR   Proteomes; UP000074561; 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   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:UP000074561};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AMP05888.1}.
FT   ACT_SITE    157    157       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    597    597       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   949 AA;  105908 MW;  E282519B55F8E2FB CRC64;
     MAKQLNSAVQ VKKSPPNKDA PLKEDIRLLG RLLGDVLREQ EGDAVFEVVE TIRQTAVRFR
     RESDPQAGAD LDKLLKKLTR DQTNSVVRAF SYFSHLANIA EDQHHNRRRR AHLLAGSAAQ
     AGSVAHALSK LDDAGVSGAT VRNFLKDALI SPVLTAHPTE VQRKSILDAE REIARLLAER
     DRPLTAKELR DNTELLRGRI ATLWQTRMLR YTKLTVADEI ENALSYYRIT FLRELPALYD
     DIEGEIATQF PTRGRSATTE LAPFVQMGSW IGGDRDGNPN VNAGTMQRAL TRQSTTIFDF
     YLEEVHALGA ELSVSTLMVS VNQELLVLAE NSPDTSDHRS DEPYRRALIG IYARLASTAR
     ELGATNILRQ EVGAAAHYAA PQEFTQELQI IEDSLRAHHG SALIKPRLAT LKRASEIFGF
     HLASLDMRQS SDVHERVLTE LFAQAQVEGA YDKLSEEQKI DLLLAELAKP RLLYSPYIEY
     SDETVSELSI LRAAGEMRQR YGARSIRNYI ISHTETVSDL LEVLLLQQET GLLRPDGKNH
     AASTLEVMVI PLFETIPDLR RAAAIMEQFM ALPPVSRLIA KQGKLQEVML GYSDSNKDGG
     FLTSNWELYK AEIQLVRVFD RAGVKLRLFH GRGGTVGRGG GPSYQAILAQ PPGTVNGQIR
     LTEQGEIIAS KFSNPEIGRR NLELLVAATL EASLMPNTAD SKQMKKLGEF EELMDGLSER
     AYQSYRNLVY ETPGFTDYFF AATPIAEIAE LNIGSRPASR KSTRRIEDLR AIPWGFSWGQ
     CRLLLPGWYG FGSAIESWLE EGKDAKLKSQ KLATLRAMYK EWPFFATLLS NMDMVLSKTD
     LAVASRYAGL VTDRKLRNSI FKRIVDEHER TSSILSAITG AKDRLSGNPL LARSIKNRFA
     YLDPLNHLQV ELIKRHRSVT AAGRTTEERV KRGIHLSING IAAGLRNTG
//
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