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Database: UniProt/TrEMBL
Entry: A1WZE2_HALHL
LinkDB: A1WZE2_HALHL
Original site: A1WZE2_HALHL 
ID   A1WZE2_HALHL            Unreviewed;       883 AA.
AC   A1WZE2;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-SEP-2017, entry version 79.
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   OrderedLocusNames=Hhal_2291 {ECO:0000313|EMBL:ABM63054.1};
OS   Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS   halophila (strain DSM 244 / SL1)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=349124 {ECO:0000313|EMBL:ABM63054.1, ECO:0000313|Proteomes:UP000000647};
RN   [1] {ECO:0000313|Proteomes:UP000000647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647};
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., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Hoff W., Richardson P.;
RT   "Complete sequence of Halorhodospira halophila SL1.";
RL   Submitted (DEC-2006) 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:SAAS00730191}.
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; CP000544; ABM63054.1; -; Genomic_DNA.
DR   RefSeq; WP_011815076.1; NC_008789.1.
DR   ProteinModelPortal; A1WZE2; -.
DR   STRING; 349124.Hhal_2291; -.
DR   EnsemblBacteria; ABM63054; ABM63054; Hhal_2291.
DR   KEGG; hha:Hhal_2291; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238648; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   BioCyc; HHAL349124:GI3I-2344-MONOMER; -.
DR   Proteomes; UP000000647; 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:UP000000647};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:ABM63054.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:ABM63054.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000647}.
FT   ACT_SITE    145    145       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    551    551       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   883 AA;  100294 MW;  92399F06BB33971E CRC64;
     MEEHQDSDSA LREDIRDLGE LLGATLREQG GTELFETVER VRVLAKTARA GDDQAAQELE
     RTLSELPPEQ VTPVARAFSQ FLNLANIAEQ HHRVRRSREW ARTPEAQPLF GSLAETVPRL
     AADMEPEQLH EAICSMDINL VFTAHPTEVQ RRTMLQKYNR IAGLLDNRDR FGQTPTEVAE
     TRLALKREIT AAWHSDEIRR RRPTPQDEAR WGLAVVEQTL WDAVPRYLRS LDHTLREHTG
     RPLPLDCAPI TFGSWMGGDR DGNPNVTHRV TRDVAILSRW MAAYLYERDI QRLVSTLSLQ
     VCDDELRDEV GGEAWEPYRV VLKRLRARLR QTMRWAEAKL QGGRPPESDI LTEVEDLRQP
     LLRCYYSLQR VGAGVVAEGE LLDTIRRVSC FGLTLMPMDI RQHADRHTAA LDAITQAVGL
     GSYSEWDEET RQQWLFQELS HRRPLIPLDF KPEREVQEVL DTIHMLEEIG PDAVGAYIVS
     HASKPSDILA VELLQKECGL THPTRVVPLF ETRDTLARAA DTMEVLFKSD WYRQRIGGRQ
     EIMIGYSDST KDAGHLTATW TLYQAQEQLV ALSRRQRVDL TLFHGRGGSI GRGGGPTHAA
     ILAQPPGSVD GTLRVTEQGE VMQAKFGLPG IALRNLELYT TSVLEATVRP PEPPPKRWRE
     ILERLSDRAM TAYRQTVKER PEFMDYFQAA TPIDEISRLT IGSRPAKRAP DQMTVDSLRA
     IPWVFAWTQT RLMLPAWLGV GEALEEAIEE GLTEELQEMF ARWPFFEAFL DMVEMVVAKA
     EPGVNRLYEH ALVPDELHSV GDELRDRFAR TRDAVLTVTG HEEPLSDFPV VKRAVEVRNP
     YVDPLNLLQV ELLRRSRMCE DDSLRRGLQV VINGIAAGMR NTG
//
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