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Database: UniProt/TrEMBL
Entry: K9RAQ8_9CYAN
LinkDB: K9RAQ8_9CYAN
Original site: K9RAQ8_9CYAN 
ID   K9RAQ8_9CYAN            Unreviewed;      1019 AA.
AC   K9RAQ8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-SEP-2017, entry version 33.
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=Riv7116_1977 {ECO:0000313|EMBL:AFY54516.1};
OS   Rivularia sp. PCC 7116.
OC   Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Rivularia.
OX   NCBI_TaxID=373994 {ECO:0000313|EMBL:AFY54516.1, ECO:0000313|Proteomes:UP000010380};
RN   [1] {ECO:0000313|EMBL:AFY54516.1, ECO:0000313|Proteomes:UP000010380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7116 {ECO:0000313|EMBL:AFY54516.1,
RC   ECO:0000313|Proteomes:UP000010380};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A.,
RA   Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Pagani I., Pati A., Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X.,
RA   Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Rivularia sp. PCC 7116.";
RL   Submitted (AUG-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}.
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; CP003549; AFY54516.1; -; Genomic_DNA.
DR   RefSeq; WP_015118091.1; NC_019678.1.
DR   EnsemblBacteria; AFY54516; AFY54516; Riv7116_1977.
DR   KEGG; riv:Riv7116_1977; -.
DR   PATRIC; fig|373994.3.peg.2094; -.
DR   KO; K01595; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000010380; 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; 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; 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:UP000010380};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:AFY54516.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AFY54516.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010380}.
FT   ACT_SITE    198    198       {ECO:0000256|HAMAP-Rule:MF_00595}.
FT   ACT_SITE    666    666       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1019 AA;  116802 MW;  9BE7E1F2DD05DD4B CRC64;
     MSTVLYTDAQ AVNIYPASDL FLRHRLQIVE EVWELVLREE CGQQMVDLLR QLRDLCSPEG
     QATDNQASSV SSLIENLSIN EAIRAARGFA LYFQLINIVE QDYEQKQQLT RYEEEERSGE
     KETLPPIIYS SNQQVEDVHL NSGVNADLLV KSWQAKPNSK DKGTFAELFP KLFKLNVPPA
     QIQRLIAQLD VRLVFTAHPT EIVRPTIREK QRRVVDLLQN LDASEKRSGN TSAGVYSWET
     TQLRSQLLEE IRLWWRTDEL HQFKPSVLDE VDYALHYFQE VLFEAIPQLY QRLEYSLNST
     FSRLEPPSKS FCQFGSWVGS DRDGNPSVTP EITWQTACYQ RHMVLNKYID SAKGLIELLS
     VSLHWSDVLP DLLESLEIEQ SQMSEVYDEL ALRYRQEPYR LKLAYVVKRL ENTRERNSAL
     RKREIIKDDK APIYRSVSEF LADLRLIQRN LSETGLKCQQ LENLLTQVEI FGFNLTQLDI
     RQESTRHSDA IGEILEYLGI LDQKYDDLPE EEKIAWLTKE LQTRRPLIPA QLPFGDKTNE
     IVETMRLVHS LQKEFGCNIC QTYIISMCRS VSDVLEVLLL AKEAGLYDPG TAVGTIRVIP
     LFETVEDLQR SRQVMKDLFS LPLYRALLAG GYEVYEEGKE TKQEGESSPL YPNLQEIMLG
     YSDSNKDSGF LSSNWEIHKA QKSLQHIAEQ YGLGVRIFHG RGGSVGRGGG PAYEAILAQP
     GKSINGRIKI TEQGEVLASK YSLPDLALYN LETITTAVIQ ASLLRAGFDD IEPWNEIMEE
     LAARSRSHYR DLIYEQPDFI DFFNQVTPIE EISQLQISSR PARRPSGKKG LSSLRAIPWV
     FSWTQTRFLL PAWYGVGTAL QEFLNEAPED HIQLLQCFYR KWPFFKMVIS KVEMTLAKVD
     LQMGRHYVEE LSKDEDKQRF DRVFNQISSE YYLTRNLVLK ITGHERLLDG DPVLQRSVQL
     RNGTIVPLGF IQVSLLKRLR DSKNNASSGV IHSRYSKGEL LRGALLTING IAAGMRNTG
//
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