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Database: UniProt/TrEMBL
Entry: I3YCK6_THIV6
LinkDB: I3YCK6_THIV6
Original site: I3YCK6_THIV6 
ID   I3YCK6_THIV6            Unreviewed;       934 AA.
AC   I3YCK6;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   20-DEC-2017, entry version 40.
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=Thivi_2806 {ECO:0000313|EMBL:AFL74724.1};
OS   Thiocystis violascens (strain ATCC 17096 / DSM 198 / 6111) (Chromatium
OS   violascens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Chromatiaceae; Thiocystis.
OX   NCBI_TaxID=765911 {ECO:0000313|EMBL:AFL74724.1, ECO:0000313|Proteomes:UP000006062};
RN   [1] {ECO:0000313|EMBL:AFL74724.1, ECO:0000313|Proteomes:UP000006062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17096 / DSM 198 / 6111
RC   {ECO:0000313|Proteomes:UP000006062};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K.,
RA   Liu Z., Frigaard N.-U., Bryant D., Woyke T.;
RT   "Complete sequence of Thiocystis violascens DSM 198.";
RL   Submitted (JUN-2012) 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; CP003154; AFL74724.1; -; Genomic_DNA.
DR   EnsemblBacteria; AFL74724; AFL74724; Thivi_2806.
DR   KEGG; tvi:Thivi_2806; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000006062; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006062};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:AFL74724.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AFL74724.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006062}.
FT   COILED      281    301       {ECO:0000256|SAM:Coils}.
FT   COILED      834    854       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    149    149       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    592    592       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   934 AA;  107326 MW;  83709A443B7D7634 CRC64;
     MLIPMNEITQ DQALERDVQL FTALLGEVLR EHSRKRVLVI VERLREGFMQ LREQEDAELR
     EKLMKRIEGL DPQTLSEVIR AFTIYFGLVN TAEELNAHLA RMDRISAGQR LWVGSFDDTV
     RQFQEDGISP EHFQSLLEHL LYLPVFTAHP TEAKRRTIME TFRRIFLVGQ DLRRRKLNDE
     EIEEKLQEIL TQIQILWKTD EVRVHKPQVI DEVRQGLYFF RESLFEAVPL VYRFLEKAVR
     RVYGANHGVK VPSFIRFGSW IGGDRDGNPF VTPETTELTV RMHAELVLEE YLERIRKLRR
     MLSHSSGFCE PSPALLDSLD ADEDYWVATM GQSLRRFLNE PYRRKLAMMS HRLGANLARI
     RARIENRDAD HVSRGYGSDR DFLADLYLIR DSLIHHGDAS AAAGPLQDLI RLAETFGFHL
     VHLDIRQEST RHTEAITELF ARQAGAPFYQ AFTEEQRLMA LSETIAHPHP FVIDKATLTP
     ETRETLEVFE VIARLRAEIG EKVFGQYVIS MTHAASHVME AMLLARLAGL AGKDRQGWFC
     NLQISPLFET IDDLEHIDQV MGTLFDHPTY QALLKASGNQ QEVMLGYSDS CKDGGILSSG
     WNLFEAQKKI IALADDRGVS CRLFHGRGGT VGRGGGPTHE AILAQPVDTV HGQIKFTEQG
     EVLSYRYANP ETARYELTMG ISGLIKASRC LIEPPVEERN DYLGIMDELS RHGEEAYRKL
     IRETEGFLDY FYECTPLDGI ALLNIGSRPS HRKKADRSLG SIRAIPWVFG WGQSRHTLPA
     WFSIGHAIER YRNNDLERLA KLQKMYQDWP YFRALLSNTQ MSLFKAEMRI AREYVNLAEN
     REQAESIYRL IEDEYNRTLT QVLNVAGLLG LMEETPELRH SLARRNQYLD PLSYIQVAVL
     GRYRAEPEED KRAEWLDPLL RSINAIAAGM RNTG
//
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