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Database: UniProt/TrEMBL
Entry: K9QKA1_9NOSO
LinkDB: K9QKA1_9NOSO
Original site: K9QKA1_9NOSO 
ID   K9QKA1_9NOSO            Unreviewed;      1016 AA.
AC   K9QKA1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   07-JUN-2017, entry version 32.
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=Nos7107_5328 {ECO:0000313|EMBL:AFY45813.1};
OS   Nostoc sp. PCC 7107.
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=317936 {ECO:0000313|EMBL:AFY45813.1, ECO:0000313|Proteomes:UP000010381};
RN   [1] {ECO:0000313|EMBL:AFY45813.1, ECO:0000313|Proteomes:UP000010381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7107 {ECO:0000313|EMBL:AFY45813.1,
RC   ECO:0000313|Proteomes:UP000010381};
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 genome of Nostoc sp. PCC 7107.";
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; CP003548; AFY45813.1; -; Genomic_DNA.
DR   RefSeq; WP_015115994.1; NC_019676.1.
DR   EnsemblBacteria; AFY45813; AFY45813; Nos7107_5328.
DR   KEGG; nos:Nos7107_5328; -.
DR   PATRIC; fig|317936.3.peg.5794; -.
DR   KO; K01595; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000010381; 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:UP000010381};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:AFY45813.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AFY45813.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010381}.
FT   ACT_SITE    199    199       {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   1016 AA;  117222 MW;  9D72768CC0470C3A CRC64;
     MSSLLYSVSH AANYYPASEL FLRRRLQIVE ELWENVLRQE CGQKMVDLLR QLRDLCSPEG
     QATNDQAASA VKLIEQLNIN EAIRAARAFA LYFQLINIIE QEYEQKQQLT RYSEIEIESK
     NAETVSDSSY SSNDKEDDAF VNTGIGSDLL AKNWVNKMHN KQKGTFATLF PHLYDLNVPP
     QQIQRLISQL DVRLVFTAHP TEIVRHTIRD KQRQVVNLLQ QIDAVENRVG AYPWESGELR
     EKLLEEIRLW WRTDELHQFK PTVLDEVDYA LHYFQEVLFD GIPQLHKRFK YALSKTFDWL
     EPPRKNFCAF GSWVGSDRDG NPSVTPEITW KTACYQRKMV LERYIQSVKK LIELLSISMH
     WSDVLPDLLE SLELDQSHLS DIYDALALRY RQEPYRLKLA YVLRRLENTR DRNLALYKRE
     TPTNEDAPMY RSGADFLAEL RLIQHNLSET GLSCRELENL ICQVEIFDFN LTQLDIRQES
     TRHSDALNEI LEYLQVLPQA YDDLTEEQRV AWLTAELQTR RPLIPAELPF SEKTNDVIET
     FRILRSLQQE FGVNICQTYI ISMCRQVSDV LEVLLLAKEA RLFDPAIAVG TVQVVPLFET
     VEDLQRSRSI MRQLFELPLY RALLAGGYEN IQQRLATPES SPHSVLTPDL QEVMLGYSDS
     NKDSGFLSSN WEIHKAQKSL QKIAEDYGVN LRIFHGRGGS VGRGGGPAYE AILAQPGHSI
     NGRIKITEQG EVLASKYSLV DLALYNLETV TTAVIQASLL RTGFDDIEPW NEIMEELAAR
     SRQHYRALIY EQPDFIDFFN QVTPIEEISQ LQISSRPARR PSGKKDLSSL RAIPWVFSWT
     QTRVLLPSWY GMGTALQEFL NEEPEEHLKL LRYFYMKWPF FKMVISKAEM TLAKVDMQMA
     RHYVQELSNP EDKERFDKVF EQIASEYYLT RDFVLKITGH NRLLDGDPVL QRSVQLRNGT
     IVPLGFIQVS LLKRLRQAKN TTATSGVIHS RYSKGELLRG ALLTINGIAA GMRNTG
//
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