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Database: UniProt/TrEMBL
Entry: B3Q9M3_RHOPT
LinkDB: B3Q9M3_RHOPT
Original site: B3Q9M3_RHOPT 
ID   B3Q9M3_RHOPT            Unreviewed;       936 AA.
AC   B3Q9M3;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   22-NOV-2017, entry version 69.
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=Rpal_1972 {ECO:0000313|EMBL:ACF00495.1};
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960 {ECO:0000313|EMBL:ACF00495.1, ECO:0000313|Proteomes:UP000001725};
RN   [1] {ECO:0000313|EMBL:ACF00495.1, ECO:0000313|Proteomes:UP000001725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1 {ECO:0000313|EMBL:ACF00495.1,
RC   ECO:0000313|Proteomes:UP000001725};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Emerson D., Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-2008) 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; CP001096; ACF00495.1; -; Genomic_DNA.
DR   RefSeq; WP_012495325.1; NC_011004.1.
DR   ProteinModelPortal; B3Q9M3; -.
DR   EnsemblBacteria; ACF00495; ACF00495; Rpal_1972.
DR   KEGG; rpt:Rpal_1972; -.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000001725; 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:UP000001725};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:ACF00495.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ACF00495.1}.
FT   ACT_SITE    164    164       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    598    598       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   936 AA;  104141 MW;  8837A2484C376DA9 CRC64;
     MSSLNLSAGP EPVSERPDDA AAIEAETRLR NDIRLLGRIL GDTVREQEGQ SVFDLVENIR
     QTSIRFHRDD DKTARAELAA ILDGMSIQDT MRIVRAFSYF SHLANIAEDQ NNIRQMRAGS
     TAGSAPRAGL LAKTLAHARQ EGISAAELRK FFATALVSPV LTAHPTEVRR KSTMDREMQI
     AGLLDQRDRV QLTADEWADN EEWLRRAVET LWKTNLLRRT KLTVLDEVTN GLSFYDYTFL
     REVPRLHSAL EDRLADAAKA EGANAEGELA SFLRMGSWIG GDRDGNPFVT AEVLHGTLKL
     QSTRVLRYYL EELHELGSEL SLASHLAGTT DTVKALAETS PDTSPHRKYE PYRLAVSGIY
     ARLAATALKL EVENLRTPVG EAEPYASAQD FKTDLDAIHL SLTTHHSGVI ARGRLRQLRR
     AIDCFGFHLA SLDMRQNSAV HERTVGELMD AARPGTSYAV LDEEARIALL ISELRSTRPL
     TSMFVKYSDE TVGELAVFRE AAKAHATYGA AAIPQCIISM TKGVSDLLEV AVLLKEVGLI
     DPSGRSAINV VPLFETIEDL QACAKIMDRL LSIPEYRRLV DSRGSVQEVM LGYSDSNKDG
     GFVTSGWELY KAEIGLIEIF EHHGVRLRLF HGRGGSVGRG GGPSYDAIVA QPGGAVNGQI
     RITEQGEIIT SKYSNVEVGR NNLEILAAAT LEASLLQPKR VAPHRDYLEA MEQLSALAFK
     AYRGLVYETD GFVDYFWAST VINEISTLNI GSRPASRKKT RAIEDLRAIP WVFSWAQCRL
     MLPGWYGFGS AVSAWVTEHP DKGIAFLQAM YQEWPFFRTL LSNMDMVLSK SSIGIASRYA
     ELVEDTAIRD RIFGRIRAEW HSSIDYLLAI MQQDHLLQSN PLLERSIRHR FPYLDPLNHV
     QVQLLREHRT HDPDEQVLRG VQLTINGISA GLRNSG
//
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