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Database: UniProt/TrEMBL
Entry: E8NAT2_MICTS
LinkDB: E8NAT2_MICTS
Original site: E8NAT2_MICTS 
ID   E8NAT2_MICTS            Unreviewed;       890 AA.
AC   E8NAT2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   22-NOV-2017, entry version 44.
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   ECO:0000313|EMBL:BAJ75949.1};
GN   OrderedLocusNames=MTES_2985 {ECO:0000313|EMBL:BAJ75949.1};
OS   Microbacterium testaceum (strain StLB037).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=979556 {ECO:0000313|EMBL:BAJ75949.1, ECO:0000313|Proteomes:UP000008975};
RN   [1] {ECO:0000313|EMBL:BAJ75949.1, ECO:0000313|Proteomes:UP000008975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StLB037 {ECO:0000313|EMBL:BAJ75949.1,
RC   ECO:0000313|Proteomes:UP000008975};
RX   PubMed=21357489; DOI=10.1128/JB.00180-11;
RA   Morohoshi T., Wang W.-Z., Someya N., Ikeda T.;
RT   "Genome sequence of Microbacterium testaceum StLB037, an N-
RT   acylhomoserine lactone-degrading bacterium isolated from potato
RT   leaves.";
RL   J. Bacteriol. 193:2072-2073(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=StLB037;
RA   Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT   "Genome sequence of Microbacterium testaceum StLB037.";
RL   Submitted (FEB-2011) 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, ECO:0000256|SAAS:SAAS00946761}.
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; AP012052; BAJ75949.1; -; Genomic_DNA.
DR   RefSeq; WP_013586074.1; NC_015125.1.
DR   STRING; 979556.MTES_2985; -.
DR   EnsemblBacteria; BAJ75949; BAJ75949; MTES_2985.
DR   GeneID; 32512901; -.
DR   KEGG; mts:MTES_2985; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000008975; 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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PTHR30523; 2.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 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:UP000008975};
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:BAJ75949.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008975}.
FT   ACT_SITE    161    161       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    556    556       {ECO:0000256|HAMAP-Rule:MF_00595}.
SQ   SEQUENCE   890 AA;  98051 MW;  0978FDE805F656B9 CRC64;
     MRELTPTEAI DLVGRFEAGQ ELPEQMRADV RLLGSLLGRV LQESGSPGLY DDVERLRTAT
     IQAYTDETPE AFERAAAIAD GFSIERADEV ARAFTAYFHL VNLVEEHQRV RILRERGDRP
     SRSGTPDTIA TAFERLSSEV GEETALARLQ ALRFHPVFTA HPTEARRRAI STSIRRLSEL
     LSEHDDAPDG GTESRRAERR MLEEIDTLWR TAPLRREKPS PVDEVRSVMS VFDETLYTAV
     PRVYRRIDDI LQGEHAGSRA PIVKPFVRVG SWVGGDRDGN PFVTASVTRK AAAIASEHVL
     LGLERTTQRV GRGLTLDAET TPPSDALVAL WHRLRAADED AAAEIAERSP DEPHRRILLL
     LARKIAATRT RDADLAYRDP EHLLADLRTV QDSLVAAGAA RQAYGALQRL VWQVETYGFH
     LTELEVRQHS AVHRKVLDEL RAGGARSEQT DEVLEVFRSI AYVQERFGPR AAGRYIVSFT
     QSAEDLANVH ELASYAMGPG ETLPVLDVIP LFETFADLQA APGILAEIVS HPSFVSRLDA
     TGRRLEVMLG YSDSSKDVGP VAANLALYEA QAKISTWAEA EGIELTLFHG RGGALGRGGG
     PANSAILAQP PHSVDGRFKL TEQGEVIFAR YGDADIAMRH IDQVAAAVLT ASSPSIERRN
     RGAAEAFADV AKTMDVASRE RFFALVKAPG FAPWFATVTP MEELGHLALG SRPARRGLSV
     ESLEDLRAIP WVFSWTQARI NLAGWFGLGT ALDAVGDEQR LRDAYEQWPL FRTMIDNVAM
     SLAKADERIA RRYLALGDRD DLAQLVMDEM LLTRSWVERI TGGGLLGNKP VLQRAVKMRS
     PYVDALSLLQ LRALRALRDA STESETPDAE HQRLLLLSVS GVAAGLQNTG
//
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