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Entry: K9PV97_9CYAN
LinkDB: K9PV97_9CYAN
Original site: K9PV97_9CYAN 
ID   K9PV97_9CYAN            Unreviewed;      1027 AA.
AC   K9PV97;
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=Cal7507_6141 {ECO:0000313|EMBL:AFY36437.1};
OS   Calothrix sp. PCC 7507.
OC   Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Calothrix.
OX   NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY36437.1, ECO:0000313|Proteomes:UP000010390};
RN   [1] {ECO:0000313|EMBL:AFY36437.1, ECO:0000313|Proteomes:UP000010390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY36437.1,
RC   ECO:0000313|Proteomes:UP000010390};
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., Teshima H., Chen A.,
RA   Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished genome of Calothrix sp. PCC 7507.";
RL   Submitted (APR-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; CP003943; AFY36437.1; -; Genomic_DNA.
DR   RefSeq; WP_015132226.1; NC_019682.1.
DR   EnsemblBacteria; AFY36437; AFY36437; Cal7507_6141.
DR   KEGG; calo:Cal7507_6141; -.
DR   PATRIC; fig|99598.3.peg.6900; -.
DR   KO; K01595; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000010390; 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; 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:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010390};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:AFY36437.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AFY36437.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010390}.
FT   ACT_SITE    199    199       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    673    673       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1027 AA;  117897 MW;  563BC7ABEA4B38F4 CRC64;
     MSSLLYSLSQ AANIYPTSEL FLRHRLQIVE ELWESVLRQE CGQKMVDLLR QLRDLCSPEG
     QATDDQASSA VKLIEQLNIN EAIRAARAFA LYFQLINIIE QEYEQRQQLT RYSELEAAAA
     EPESLPNISY SSNKGEDDAP VNGALAADML AKNWISKQKE KQKGTFSALF PHLFKLNVPP
     QQIQRLIAQL DVRLVFTAHP TEIVRHTIRD KQRQVVTLLQ HLDTAENRTG NTIGGYPWEA
     AELREKLLEE IRLWWRTDEL HQFKPTVLDE VDYALHYFQE VLFDGIPQLY QRFKYSLNKT
     FPWLEPPQKN FCSFGSWVGS DRDGNPSVTP ETTWQTACYQ RKMVLERYVQ SVKKLIELLS
     VSMHWSDVLP DLLESLELDQ SQLSEVYDAL ALRYRQEPYR LKLSYVLRRL ENTRDRNLAL
     YKRETPKNEG TPMYRSGADF LTELRLIHRN LTETGLSCRE LENLISQVEI FGFDLTQLDI
     RQESSRHADA LNEILEYLQV LPQPYNELSE AQRVAWLTGE LQTRRPLIPA ELPFSEKTND
     VIQTFRIVRS LQQEFGVNIC QTYIISMCRE VSDVLEVLLL AKEARLFDPA IAVGTIQVVP
     LFETVEDLQR SRSVMRQLFE LPLYRALLAG GYEVIKARKE NIPPSSPLPI SPAFSPLTPD
     LQEIMLGYSD SNKDSGFLSS NWEIHKAQKS LQQTAEDYDL NVRIFHGRGG SVGRGGGPAY
     EAILAQPGHS INGRIKITEQ GEVLASKYSL LDLALYNLET ITTAVIQASL LRTGFDDIQP
     WNEIMEELAA RSRTHYRALI YDQPDFIDFF HQVTPIEEIS QLQISSRPAR RPSGKKDLTS
     LRAIPWVFSW TQTRFLLPSW YGVGTALQEF LNEEPEEHLK LLSYFYIKWP FFKMVISKAE
     MTLAKVDMQM ARHYVQELSN PEDLPRFEKV FEQIASEFYL TRDLVLKITG HNRLLDGDPV
     LQRSVQLRNG TIVPLGFIQV SLLKRLRQSR NTTSTSGVIH SRYSKGELLR GALLTINGIA
     AGMRNTG
//
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