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Database: UniProt/TrEMBL
Entry: K9P7Y8_CYAGP
LinkDB: K9P7Y8_CYAGP
Original site: K9P7Y8_CYAGP 
ID   K9P7Y8_CYAGP            Unreviewed;      1001 AA.
AC   K9P7Y8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-SEP-2017, entry version 35.
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   OrderedLocusNames=Cyagr_1666 {ECO:0000313|EMBL:AFY28816.1};
OS   Cyanobium gracile (strain ATCC 27147 / PCC 6307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Cyanobium.
OX   NCBI_TaxID=292564 {ECO:0000313|EMBL:AFY28816.1, ECO:0000313|Proteomes:UP000010388};
RN   [1] {ECO:0000313|Proteomes:UP000010388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27147 / PCC 6307 {ECO:0000313|Proteomes:UP000010388};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E.,
RA   Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M.,
RA   Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M.,
RA   Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M.,
RA   Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-
RT   driven genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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; CP003495; AFY28816.1; -; Genomic_DNA.
DR   EnsemblBacteria; AFY28816; AFY28816; Cyagr_1666.
DR   KEGG; cgc:Cyagr_1666; -.
DR   PATRIC; fig|292564.3.peg.1580; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000010388; 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; 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:UP000010388};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AFY28816.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010388}.
FT   ACT_SITE    177    177       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    639    639       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1001 AA;  112547 MW;  E8EA6400AC286886 CRC64;
     MRLHLTEPSV VPAEASPGVI RLLTERLELV EDLWQTVLRS ECPPEQVDRL LRLKELSGPV
     APGLDPEAPS AVDTDGIVAL IKAMDLAEGI AAARAFSLYF QLVNILEQHI EEDSYLESIK
     RAPAPASNDP FLPPLASQSD PATFRQLFER LRALNVPPGQ LEGLLRELDI RLVFTAHPTE
     IVRHTVRHKQ RRVAALIQKL QVNGQGNPDD NDRLRQQLEE EIRLWWRTDE LHQFKPSVID
     EVDYALHYFQ QVLFDALPQL RQRIRAALAA SYPDVQPPRD AFCTFGSWVG SDRDGNPSVT
     PDVTWRTACF QRQLMLARYI QSVSVLRDQL SISMQWSQVS AALLESLEMD RLRFPEIYEE
     RAARYRLEPY RLKLSYTLER LRLTQQRNQQ LAEAGWESPC DGSSGYEAGL SSLMEPAPPQ
     ELHYASVEEF RTDLELIKES LDATGLSCEA LQDLLSQVHI FAFSLASLDI RQESTRHSDA
     IDELSRYLLL PVPYGEMDEE QRVEWLLSEL KTRRPLLPPA ARWSAPTAET FAVFRMLQRL
     QQEFGRRICR TYVISMSHTV SDLLEVVLLA KEAGLVDPMA QKSALLVIPL FETVEDLQGA
     PAVMGRLFAD PFYRQLLISN SDGEQPLQEV MLGYSDSNKD SGFLSSNWEI HRAQIALQSL
     ADAHDVALRI FHGRGGSVGR GGGPAYQAIL AQPSGTLKGR IKITEQGEVL ASKYSLPELA
     LYNLETVTTA VLQNSMVSTP VDDTPTWNVL MERLAARSRD HYRALVHDNP DLVAFFQQVT
     PIEEISKLQI SSRPARRKSG AKDLSSLRAI PWVFGWTQSR FLLPSWYGVG TALQAELDAD
     GEQMELLQLL YQRWPFFRML ISKVEMTLSK VDLELAGHYV TSLGRPQNRE VFAQIFEAIA
     SEFALTHSLV LRISNHSRLL DGDPALQLSV DLRNRTIIPL GYLQVALLRR LREQKRQPPM
     SEGPGDGPGG GGDGRTYSRS ELLRGALLTI NGIAAGMRNT G
//
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