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Database: UniProt/TrEMBL
Entry: E1SMG8_FERBD
LinkDB: E1SMG8_FERBD
Original site: E1SMG8_FERBD 
ID   E1SMG8_FERBD            Unreviewed;       879 AA.
AC   E1SMG8;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   28-MAR-2018, entry version 52.
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=Fbal_0309 {ECO:0000313|EMBL:ADN74523.1};
OS   Ferrimonas balearica (strain DSM 9799 / CCM 4581 / PAT).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Ferrimonadaceae; Ferrimonas.
OX   NCBI_TaxID=550540 {ECO:0000313|EMBL:ADN74523.1, ECO:0000313|Proteomes:UP000006683};
RN   [1] {ECO:0000313|EMBL:ADN74523.1, ECO:0000313|Proteomes:UP000006683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9799 / CCM 4581 / PAT {ECO:0000313|Proteomes:UP000006683};
RX   PubMed=21304747;
RA   Nolan M., Sikorski J., Davenport K., Lucas S., Del Rio T.G., Tice H.,
RA   Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Tapia R., Brettin T.,
RA   Detter J.C., Han C., Yasawong M., Rohde M., Tindall B.J., Goker M.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Ferrimonas balearica type strain (PAT).";
RL   Stand. Genomic Sci. 3:174-182(2010).
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; CP002209; ADN74523.1; -; Genomic_DNA.
DR   RefSeq; WP_013343829.1; NC_014541.1.
DR   STRING; 550540.Fbal_0309; -.
DR   EnsemblBacteria; ADN74523; ADN74523; Fbal_0309.
DR   KEGG; fbl:Fbal_0309; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238648; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   BioCyc; FBAL550540:G1GN9-330-MONOMER; -.
DR   Proteomes; UP000006683; 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   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:UP000006683};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:ADN74523.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ADN74523.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006683}.
FT   ACT_SITE    140    140       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    547    547       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   879 AA;  98945 MW;  B5CDC5CB452865C1 CRC64;
     MTDMYAPLKA NVHLLGDILG ETIEAEHGAA FLNLIEEVRQ LSKASRQGDT EAQSKMLALL
     SELPDEQLVP FASAFNQFLN LANIAEQFHT ISRNCDELVC VPDPVDLLLG RLFNGKAQLK
     PDQLIDELEK LEIDLVLTAH PTEVTRRTLI SKYSALIECL SERENPQLSE RETKRNQLRM
     RQLVAQIWHT NEIRKQRPTP VDEARWGMAT VETSLWHAVP EFLRQLNEQV EEHAGRQLPP
     HVAPVRFSSW MGGDRDGNPF VTAKVSEEVL LRNRCTATRL YLEDINQLIG ELSMTDCDQA
     IRAMVGDHRE PYRILLRQLR EKLSDTQDYL MARLDGQQPK TNPSTLIWHK KDLLEPLELI
     YQSLLDQGMR LIANGLLLDT LRRIHCFGLT LVRVDIRQSS DRHASAIAEI TRYLGLGDYL
     HWSEAEKQSF LLRELASRRP LLPHQWQASA DTQEVLDTCR LIGQQSPEAL GSYVISMASE
     ASDVLAVALL LKECDCNFAL PIVPLFETLS DLDNAPAVMR NLLQIDWYLG YCRGKQQVMI
     GYSDSAKDAG VMAASWAQYR AQEALVSVCK DAGVALTLFH GRGGSIGRGG GPAHEAILSQ
     PPGSVDSRLR VTEQGEMIRF KFGLPEVAVQ SLALYTSAVL EATLLPPLAP KPEWRSLMDS
     IADDSVRAYR QIVQDEPDFV PYFRAATPEL ELSALPLGSR PAKRRADGGV ESLRAIPWIF
     AWTQNRLMLP AWLGAGESLQ NAIDQGHQET LQEMFLNWPL FRTRLSMLEM VYAKSEPNLS
     RYYEQILVKP ELHGLGEKLR QSLEIGVRSV LNLTQEQGLM DLTPWNKESV ALRHPYIDPL
     NFLQAELLRR CRQEPEDPAL QQALMITIAG IAAGLRNTG
//
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