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Database: UniProt/TrEMBL
Entry: A0A0K1S8Q1_9CHRO
LinkDB: A0A0K1S8Q1_9CHRO
Original site: A0A0K1S8Q1_9CHRO 
ID   A0A0K1S8Q1_9CHRO        Unreviewed;      1018 AA.
AC   A0A0K1S8Q1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   05-JUL-2017, entry version 15.
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   ORFNames=VL20_5586 {ECO:0000313|EMBL:AKV70408.1};
OS   Microcystis panniformis FACHB-1757.
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Microcystaceae; Microcystis.
OX   NCBI_TaxID=1638788 {ECO:0000313|EMBL:AKV70408.1};
RN   [1] {ECO:0000313|EMBL:AKV70408.1, ECO:0000313|Proteomes:UP000068167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FACHB-1757 {ECO:0000313|EMBL:AKV70408.1,
RC   ECO:0000313|Proteomes:UP000068167};
RX   PubMed=26823957; DOI=10.1186/s40793-016-0130-5;
RA   Zhang J.Y., Guan R., Zhang H.J., Li H., Xiao P., Yu G.L., Du L.,
RA   Cao D.M., Zhu B.C., Li R.H., Lu Z.H.;
RT   "Complete genome sequence and genomic characterization of Microcystis
RT   panniformis FACHB 1757 by third-generation sequencing.";
RL   Stand. Genomic Sci. 11:11-11(2016).
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: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; CP011339; AKV70408.1; -; Genomic_DNA.
DR   EnsemblBacteria; AKV70408; AKV70408; VL20_5586.
DR   KEGG; mpk:VL20_5586; -.
DR   PATRIC; fig|1638788.3.peg.5632; -.
DR   KO; K01595; -.
DR   Proteomes; UP000068167; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-HAMAP.
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; 2.
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:UP000068167};
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:AKV70408.1}.
FT   ACT_SITE    193    193       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    665    665       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1018 AA;  116940 MW;  C216CC2C32738A4F CRC64;
     MSVLVPSTET EQDIFSTSNL FLQQRLKLIE DLWKEVLVSE CGQELVDLLE LLRHLCSEEG
     QVTDDSPEAM IAKMIEDLEL GEAIKVTRAF ALYFQLINII EQHYEQRDQQ LLRRTVIGEE
     NESPKTDPPQ KSLLATIVGA DWLEKTLNES DHSGPKSGLF HWLFPYLKQV NVPPQEIQRL
     LDQLDIRLVF TAHPTEIVRH TIRIKQRRIS GILEKLDQAE EIFRSMGLTN SREAQTVTKQ
     LKEEIRFWWR TDELHQFKPT VVDEVDYALH YFDEVLFDSL PQLTLRLQQS LQSSFPRLQA
     PKNNFCRFGS WVGGDRDGNP SVTPEVTWKT CCYQRNLVIK KYLDAIRDLT SILSASLHWC
     HVLPELLDSL DRDKQQMPEI YSQLAIRYRQ EPYRLKLAFI QKRLENTRDR NNRLNDPEER
     QLLTKLNETN IYRSGSEFLA ELQLLQRSLL QTGLSCQELD RLIAQVEIFG FVLTQLDFRQ
     ESTRHAECIE EIAAYLGVLP KPYGQLTESE KIAWLVAELK TRRPLIPREM PFSERTCETI
     ETLRVLRSLQ GEFGLEICQT YIISMTNEAS DVLEVLLLAQ EAGLYDPATS RSSLRIVPLF
     ETVDDLKHAP GIMQTLFELP LYRAALAGGY DHLGALNGEE VTPEPAILEP GNLQEIMVGY
     SDSNKDSGFL SSNWEIHKAQ KALQKTAKQY GLDLRLFHGR GGSVGRGGGP AYAAILAQPR
     GTINGRIKIT EQGEVLASKY SLPELALYNL ETAVTAVIQA SLLGSGFDDL EPWNRIMEEL
     ATRSRQTYRS LIYEEPDFLD FFLSVTPIPE ISLLQISSRP ARRKSGQQDL STLRAIPWVF
     SWTQTRFLLP AWYGLGTALQ MFLDDSPNRN LELLRHFYHK WPFFQMVISK AEMTLSKVDL
     QIAYHYVSEL SKQEDRERFQ RLFERIKEEY NRTSEIVLQI TGEKNLLDND PNLQRSVQLR
     NGSIVPLGFL QVSLLKRLRQ YNSQAQSGVI HFRYSKEELL RGALMTINGI AAGMRNTG
//
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