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Database: UniProt/TrEMBL
Entry: K9WJ55_9CYAN
LinkDB: K9WJ55_9CYAN
Original site: K9WJ55_9CYAN 
ID   K9WJ55_9CYAN            Unreviewed;      1050 AA.
AC   K9WJ55;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   20-DEC-2017, entry version 37.
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   ORFNames=Mic7113_4767 {ECO:0000313|EMBL:AFZ20440.1};
OS   Microcoleus sp. PCC 7113.
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Microcoleus.
OX   NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ20440.1, ECO:0000313|Proteomes:UP000010471};
RN   [1] {ECO:0000313|EMBL:AFZ20440.1, ECO:0000313|Proteomes:UP000010471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ20440.1,
RC   ECO:0000313|Proteomes:UP000010471};
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 Microcoleus sp. PCC 7113.";
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}.
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; CP003630; AFZ20440.1; -; Genomic_DNA.
DR   RefSeq; WP_015184575.1; NC_019738.1.
DR   EnsemblBacteria; AFZ20440; AFZ20440; Mic7113_4767.
DR   KEGG; mic:Mic7113_4767; -.
DR   PATRIC; fig|1173027.3.peg.5292; -.
DR   KO; K01595; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000010471; 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; 3.
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:UP000010471};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:AFZ20440.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AFZ20440.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010471}.
FT   COILED      219    239       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    210    210       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    697    697       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1050 AA;  119892 MW;  E6FB1DBD1D7921EB CRC64;
     MSSLIHSSDQ EIAASSTSEL FLRHRLKVVE DLWGSVLLSE CGQELVDLLK QLRDLCSPEG
     QATDLPESSV PKVIEKLDLN AAIRASRAFA LYFQLINIVE QHYEQRDQQL SRRATSKTST
     SHQAVPPKQA FPKTNGNLAM GSSNMLNSET HNADPMADFL ERSWQDNAAS KRESGTFHWL
     FPHLQQLNVP PQQIQRMIEN LDIRLVFTAH PTEITRHTIR AKQRRIARIL KQLDQAEEAT
     RSLGLTSSWE IEGYTEQLME EIRLWWRTDE LHQFKPSVLD EVDYTLHYFQ EVLFEAIPQL
     YHRMKQALNS SFPWLTPPVH NFCKFGSWVG SDRDGNPSVT PQVTWETACY QRGLVLEKYM
     QSVGTLINLL SLSLHWSDVL PELLDSLEQD RSQMPELYEQ LAIRYRQEPY RLKLSYVQQR
     LENTRDRNRR LYNLYDGKPL QQDLNETNNS GVYRSGAEFL AELRLIERSL AVTGLSCQEL
     ENLICQVEIY GFNLAHLDIR QESSRHCDTI NEIAEYLQIL PKPYNELSEA ERTQWLTAEL
     KTRRPLIPAE APFSEKTSET IETFRMLRQL QQEFGAQVCQ TYIISMSHEA SDLLEVLLLA
     KEAGLYDPAT GKSSVQVVPL FETVEDLKRA PGVMKSLFEL PLYRACLAGG YEALNVEPCS
     DHPQPTNMPS RGALSEQPST LSPNLQEVML GYSDSNKDSG FLSSNWEIHK AQKALQKIAE
     EYGISLRIFH GRGGSVGRGG GPAYEAILAQ PGHSINGRIK ITEQGEVLAS KYSLPELALY
     HLETVTTAVI QASLLRTGFD DIEPWTQIME ELATRSRAHY RDLIYEQPDL LDFFHQVTPI
     QEISQLQISS RPSRRGGKKD FSSLRAIPWV FSWTQTRFLL PSWYGVGTAL KAFLDEDPEE
     NLKLLRYFYF KWPFFKMVVS KVEMTLAKVD LQIAHHYVRE LSSPENLERF ERLFDQIASE
     FNLTRDLILS IAGHKRLLDG DPELQRSVQL RNGTIVPLGF LQVSLLKRLR QHSNQTASGT
     IIHSRYSKGE LLRGALLTIN GIAAGMRNTG
//
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