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Entry: K9SK55_9CYAN
LinkDB: K9SK55_9CYAN
Original site: K9SK55_9CYAN 
ID   K9SK55_9CYAN            Unreviewed;       978 AA.
AC   K9SK55;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   07-JUN-2017, entry version 34.
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=Pse7367_2737 {ECO:0000313|EMBL:AFY70992.1};
OS   Pseudanabaena sp. PCC 7367.
OC   Bacteria; Cyanobacteria; Synechococcales; Pseudanabaenaceae;
OC   Pseudanabaena.
OX   NCBI_TaxID=82654 {ECO:0000313|EMBL:AFY70992.1, ECO:0000313|Proteomes:UP000010386};
RN   [1] {ECO:0000313|EMBL:AFY70992.1, ECO:0000313|Proteomes:UP000010386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7367 {ECO:0000313|EMBL:AFY70992.1,
RC   ECO:0000313|Proteomes:UP000010386};
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., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y.,
RA   Chain P., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA   Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A.,
RA   Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Pseudanabaena sp. PCC 7367.";
RL   Submitted (MAY-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; CP003592; AFY70992.1; -; Genomic_DNA.
DR   RefSeq; WP_015165948.1; NC_019701.1.
DR   EnsemblBacteria; AFY70992; AFY70992; Pse7367_2737.
DR   KEGG; pseu:Pse7367_2737; -.
DR   PATRIC; fig|82654.3.peg.3200; -.
DR   KO; K01595; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000010386; 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; 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:UP000010386};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:AFY70992.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AFY70992.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010386}.
FT   ACT_SITE    167    167       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    628    628       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   978 AA;  112337 MW;  19B8087125A52664 CRC64;
     MSSPTFSLSE SLIQIVNQET DLRLSDSRLR YRIKIIEELW QSVLVQECGQ GMVDLLLQLR
     SMCSPEGQAP QYPAQEVLKV VESLSLEESI TAARAFAIYF QLINIIEQQY EQEEQQQAQI
     DRIKGESKFL DGTFRWLFPE LKRQNVPPRF IQDLIDKLDI RLVFTAHPTE IVRHTIRDKQ
     RQIAVMLKEL DRLTDGTYSD DIDYGQMMPL SWEAENLREQ IADEIRLWWH TDELNQSKPT
     VIDEADYTLH YFDEVLYDAI PDLYERVEKA LTETFPHLNP PKYNFCKFGS WVGSDRDGNP
     SVKPDITWRT ACYQRGLVIE KYISSVNGLV RLLSVSQNLI DISTDLLTSL GQDQTHMPEV
     YNQFAVRYRQ EPYRLKLQYI LKRLRNTRDR NDRLNEIGWQ AADQVMPIKP TDHSVYSGAK
     DFETELRLVA NSLKGSGLHC KALQTLIRQV EVYGFHLANL DIRQESRKHS GAITEITSSL
     KILDTPYDQL SESEKVNWLT KELQTLRPLI PADLHFGDFT NEIIETFRML AKLQQEFSIE
     ICNTYIISMS ESVSDVLEVL LLAKEAGLYN PATGTGSVSV VPLFETVEDL QGAKRIMQEL
     FDLRLYRNYL NHHEHRQEVM LGYSDSNKDS GFLSSNWEIY KAQLSLQKLA EQYGIWLCIF
     HGRGGSVGRG GGPTYQAILA QPGRSIKGAI KITEQGEVLA SKYSLLEIAL HNLETVATGV
     IQAALLPSSS DTLGSWLQTL EDLATRSRQV YRELIHENPN LVDFFHEVTP IEEISHLQIS
     SRPARRSAGK KDLSSLRAIP WVFSWTQSRF LLPSWYGVGT AIDEFLQQHP EHLTLMQFFY
     EKWPFFRTTI SKVEMTLAKS DLQIARHYVR ELAPAAKQEL YMQLFEQIAN EYYRTCKIIL
     QITGHHQLLD GDPSLQRSVQ LRNGSIVPLG FIQAALIKRL RQYNSDPINL RSRYSRTELL
     RGALLTINGI AAGMRNTG
//
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