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Database: UniProt/TrEMBL
Entry: A5UWX2_ROSS1
LinkDB: A5UWX2_ROSS1
Original site: A5UWX2_ROSS1 
ID   A5UWX2_ROSS1            Unreviewed;       952 AA.
AC   A5UWX2;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   22-NOV-2017, entry version 74.
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=RoseRS_2753 {ECO:0000313|EMBL:ABQ91125.1};
OS   Roseiflexus sp. (strain RS-1).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=357808 {ECO:0000313|EMBL:ABQ91125.1, ECO:0000313|Proteomes:UP000006554};
RN   [1] {ECO:0000313|Proteomes:UP000006554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS-1 {ECO:0000313|Proteomes:UP000006554};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Roseiflexus sp. RS-1.";
RL   Submitted (APR-2007) 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; CP000686; ABQ91125.1; -; Genomic_DNA.
DR   RefSeq; WP_011957469.1; NC_009523.1.
DR   ProteinModelPortal; A5UWX2; -.
DR   STRING; 357808.RoseRS_2753; -.
DR   EnsemblBacteria; ABQ91125; ABQ91125; RoseRS_2753.
DR   KEGG; rrs:RoseRS_2753; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000006554; 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; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 2.
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:UP000006554};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:ABQ91125.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ABQ91125.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006554}.
FT   ACT_SITE    148    148       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    588    588       {ECO:0000256|HAMAP-Rule:MF_00595}.
SQ   SEQUENCE   952 AA;  106995 MW;  C546F869F3FB4E19 CRC64;
     MSHVTRRENE RLSATIRFLG NLLGEVIRNQ AGEEAFRLVE QLRTLGKELR NGEPDRADAS
     LRALASQMTV TDVQTVIKAF NAYFLLVNLA EQMQRVWILR DREQASPTAP RTESIAAAIA
     EIHAHNVSAV TVQEWLETAR IQPVFTAHPT EARRRTALEK VRRLATLLDR RSGGLQGFEL
     EENTLRIREE IVSLWQTDEV RVVKPTVIDE VKNGLFYFES GLFDLIPRLY RELEYALRTA
     YPDHEWRVPP LLRYGAWMGG DRDGNPNVTH AVTLQTVRLL RAAAVQRHIT TIEELSHRLG
     QSTRQAPVSE ELRASLANDA ALFPDVADML TQRNPYELYR QKCTYIREKL LRTLNDANTA
     SLDWGRSDPP PNGAYLRSDD LLADLRVMEQ SLRANNAAVV ADGALRDLIR QVEVFGLHTA
     TLDIRQHSER HTAALAEVLA SAGVCADYTA LNETERIDLL SREIGNPRPL IPAHLDYSPD
     TVEVIQTFRT IAAILNRLSP EAIETYIVSM TRGASDLLAP LLLAKEAGLF RPFRFSRLNI
     APLFETGADL TCCDTILEAC LSLPVYRDHL ALRGNLQEVM IGYSDSNKDV GYVAANWALY
     QAQRKLRDFG RRYGIHMRLF HGRGGAIGRG GGPANHAILA QPPGSIGNQI KITEQGEVIA
     DRYGLPLLAH RHIEQVMNAV LRAGLLQRDD PPAEWMQALE RLADLSQRHY RALVYERNDF
     VPYFHNVTPI TEISRLNIGS RPASRRNTGR IEDLRAIPWV FSWMQSRHTL PGWYGMGFAL
     ETFVYKGDGI DLDMSGDSGN VTGDGTTDHV GSAIDRLALL QEMYARWSFF RVMIDNAQMI
     LGKADLHIAA RYAELAPDRE AAASIFAAIR DEYGRTDRMI RQIARIERLL DNSPVLQHSI
     QRRNPYIDPM SYLQIELLRR LRAAPDGPQH AAIEDAILLS ISGLAAGLMN TG
//
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