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Database: UniProt/TrEMBL
Entry: A0A0S2SCW9_9GAMM
LinkDB: A0A0S2SCW9_9GAMM
Original site: A0A0S2SCW9_9GAMM 
ID   A0A0S2SCW9_9GAMM        Unreviewed;       877 AA.
AC   A0A0S2SCW9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   25-OCT-2017, entry version 17.
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   ECO:0000313|EMBL:ALP39471.1};
GN   ORFNames=ATO46_09765 {ECO:0000313|EMBL:KUE78638.1}, WL1483_52
GN   {ECO:0000313|EMBL:ALP39471.1};
OS   Aeromonas schubertii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=652 {ECO:0000313|EMBL:ALP39471.1, ECO:0000313|Proteomes:UP000058114};
RN   [1] {ECO:0000313|Proteomes:UP000058114}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WL1483 {ECO:0000313|Proteomes:UP000058114};
RA   Liu L.;
RT   "Complete Genome Sequence of Aeromonas schubertii strain WL1483.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KUE78638.1, ECO:0000313|Proteomes:UP000054876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43700 {ECO:0000313|EMBL:KUE78638.1,
RC   ECO:0000313|Proteomes:UP000054876};
RA   Liu L., Li Q., Zhang F., Shi B.;
RT   "Complete genome sequence of Aeromonas schubertii strain ATCC43700.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ALP39471.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WL1483 {ECO:0000313|EMBL:ALP39471.1};
RX   PubMed=26798095;
RA   Liu L., Li N., Zhang D., Fu X., Shi C., Lin Q., Hao G.;
RT   "Complete Genome Sequence of the Highly Virulent Aeromonas schubertii
RT   Strain WL1483, Isolated from Diseased Snakehead Fish (Channa argus) in
RT   China.";
RL   Genome Announc. 4:e01567-15(2016).
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; CP013067; ALP39471.1; -; Genomic_DNA.
DR   EMBL; LPUO01000054; KUE78638.1; -; Genomic_DNA.
DR   RefSeq; WP_050666330.1; NZ_LPUO01000054.1.
DR   EnsemblBacteria; ALP39471; ALP39471; WL1483_52.
DR   EnsemblBacteria; KUE78638; KUE78638; ATO46_09765.
DR   KEGG; asr:WL1483_52; -.
DR   PATRIC; fig|652.5.peg.117; -.
DR   KO; K01595; -.
DR   Proteomes; UP000054876; Unassembled WGS sequence.
DR   Proteomes; UP000058114; 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:UP000054876,
KW   ECO:0000313|Proteomes:UP000058114};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:ALP39471.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054876}.
FT   ACT_SITE    138    138       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    543    543       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   877 AA;  98887 MW;  EB1DE886AD8E08EC CRC64;
     MNEKYAALRA NVGLLGQLLG KSIKDHKGQA FLDKIETIRQ LAKSSRKGNE QDRQSLIDTL
     QTLSDEELLP VARAFSQFLN LANVAEQFHT ISRSFADQTG ASDPLEQLFT KLKASNLSQE
     AIVQAVRELD IDLVLTAHPT EVTRRTLIHK HVQLNDCLEA LELSDLLPQE RDRLINRVEQ
     LINQAWHTNE IREQRPTPVD EAKWGFAVIE NSLWPAIPEF MRHLDEQLQQ HLGVRLPLDA
     APVRFTSWMG GDRDGNPFVT AEVTAKVLEL GRWMAVSLFY KEIKELTSEL SMSDCNDELR
     ARVGNHNEPY RVVMRELREA LRETKEYLTA KVQGQQSENR DLVRTTAQLR EPLELCYHSL
     HASGMGNIAD GMLLDVLRKV ACFGIHLVKL DIRQDGERHA LALAELTRYL GIGDYAEWSE
     ENKQAFLLAE LNSRRPLVPA DWTPSDETRE TIETCRVIAA NDPDAFGIYI ISMAGAPSDV
     LAVQLLLKEA GCKFRMPVAP LFETQEDLMA GTRVMERLLS VDWYRGYIQG RQYVMIGYSD
     SAKDAGMMAA GWAQYAAMES LVALAEINQI RLTLFHGRGG TVGRGGAPAH QAILSQPPGS
     LRGGLRTTEQ GEMIRFKFGL PKVAINSLLL YTSAVLEGNL LPPPKPREEW RQVMELLSTV
     SCEHYRSIVR GHPDFVPYFR AATPELELGK LPLGSRPAKR KPNGGVESLR AIPWIFAWTQ
     NRLMLPAWLG AHKGLQQAID EGKLEVLEEM SRQWPFFRTR LEMLEMVFLK ADAWLAEYYD
     TRLVPEALWP LGQQLRRELA DSIALVLKLR PQGGLLDDQP WIQESIRLRN PYTDPLNVLQ
     AELLGRSRRD PDSLHPELDQ ALMVTIAGIA AGMRNTG
//
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