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Database: UniProt/TrEMBL
Entry: A0A0S3U0E0_9CYAN
LinkDB: A0A0S3U0E0_9CYAN
Original site: A0A0S3U0E0_9CYAN 
ID   A0A0S3U0E0_9CYAN        Unreviewed;      1014 AA.
AC   A0A0S3U0E0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-SEP-2017, entry version 13.
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=LEP3755_14800 {ECO:0000313|EMBL:BAU10987.1};
OS   Leptolyngbya sp. NIES-3755.
OC   Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae;
OC   Leptolyngbya.
OX   NCBI_TaxID=1752064 {ECO:0000313|EMBL:BAU10987.1};
RN   [1] {ECO:0000313|EMBL:BAU10987.1, ECO:0000313|Proteomes:UP000062150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-3755 {ECO:0000313|EMBL:BAU10987.1,
RC   ECO:0000313|Proteomes:UP000062150};
RA   Hirose Y.;
RT   "Complete genome sequence of Leptolyngbya sp. NIES-3755.";
RL   Submitted (DEC-2015) 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: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; AP017308; BAU10987.1; -; Genomic_DNA.
DR   RefSeq; WP_068382253.1; NZ_AP017308.1.
DR   EnsemblBacteria; BAU10987; BAU10987; LEP3755_14800.
DR   KEGG; len:LEP3755_14800; -.
DR   PATRIC; fig|1752064.3.peg.1537; -.
DR   KO; K01595; -.
DR   Proteomes; UP000062150; 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; 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:UP000062150};
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:BAU10987.1}.
FT   ACT_SITE    203    203       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    662    662       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1014 AA;  116699 MW;  80E577BE1CD46F5A CRC64;
     MSSTRPSSDE FSTSLTTASE DVTAMMSDLF LRHRLRIVED LWEAVLRQEC GQELVDLLNQ
     LRRMCSPEGQ ATTFTGSEVL QVVEKLDLNE AIRAARAFAL YFQLINIVEQ HYEQRDQQLQ
     YRMAREGHGQ PDPKHERQAY ATEEDAGRPE ADFLERSLHE AASRREIGTF HWLFPRLKQL
     NVPPQLIQKL INQLDVWLVF TAHPTEIVRH TIRDKQRRIA KILRQLDSVE DSLKAIGLSS
     SWEADSLRDQ LTEEIRLWWR TDELHQFKPT VLDEVDHALH YFREVIFDAI PHLYQRLEEA
     VHGSFPKMQM PRRNFCQFGS WVGADRDGNP SVTPQVTWQT ACYQRRLVLE RYVNSIQSLS
     ELLSLSLHWS DVLPDLLESL EQEQQRMPEV YDRLSIRFRQ EPYRLKLAYI CKRLENTLER
     NQILSNIDGL QQEMPEYDET KIYRSGDDFL TELRLIQSNL AATGLSCRDL DHLICQVEIF
     GFNLAHLDIR QESPRHSETM NEVVEYLQVL PKAYNDMSEE ERCQWLISEL KTRRPLIPSE
     LPFSDRTREA IATFRMVRKL QQEFGIDICR TYIISMSHDV SDLLEVLLFA KEAGLYDPAT
     GFGTIQVVPL FETVEDLQKA PGIMRGVFDL PFYKALLAGG FESIGVTTAL QEVMLGYSDS
     NKDSGFLSSN WEIHKAQQAL QSIADEHGVV LRIFHGRGGS VGRGGGPAYE AILAQPGHSV
     NGRIKITEQG EVLASKYSLP ELALYNLETV TTAVIQGSLL QNKFDEIAPW QQVMEELAAR
     SRKHYRSLIY EQPDFIDFFH QVTPIEEISQ LQISSRPARR GGKKDLASLR AIPWVFSWTQ
     SRFLLPSWYG VGTALQGFLD EAPEKHMQLL RHFYFKWPFF KMAISRVEMT LSKVDLQIAS
     HYVDELTQPE DRERFAPVFE QIRNEYLLTR ELVLTITGHN RLLDGDPELQ RSVQLRNGTI
     VPLGFLQVSL LKRLRQHKTL AASGVVRSRY SKGELLRGAL LTINGIAAGM RNTG
//
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