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Database: UniProt/TrEMBL
Entry: K9YQH2_CYASC
LinkDB: K9YQH2_CYASC
Original site: K9YQH2_CYASC 
ID   K9YQH2_CYASC            Unreviewed;      1020 AA.
AC   K9YQH2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   07-JUN-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   OrderedLocusNames=Cyast_2422 {ECO:0000313|EMBL:AFZ48368.1};
OS   Cyanobacterium stanieri (strain ATCC 29140 / PCC 7202).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Cyanobacteriaceae; Cyanobacterium.
OX   NCBI_TaxID=292563 {ECO:0000313|EMBL:AFZ48368.1, ECO:0000313|Proteomes:UP000010483};
RN   [1] {ECO:0000313|Proteomes:UP000010483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29140 / PCC 7202 {ECO:0000313|Proteomes:UP000010483};
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; CP003940; AFZ48368.1; -; Genomic_DNA.
DR   EnsemblBacteria; AFZ48368; AFZ48368; Cyast_2422.
DR   KEGG; csn:Cyast_2422; -.
DR   PATRIC; fig|292563.3.peg.2527; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000010483; 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:UP000010483};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:AFZ48368.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AFZ48368.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010483}.
FT   ACT_SITE    197    197       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    667    667       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1020 AA;  117301 MW;  1F929481884F1AE2 CRC64;
     MTFTKTSHKE ELSIYSNSEL LLRHRLKLVE NLWELVLRNE CGQHLVDLLE QLKSACSPEG
     QTSETPKQSV SKWIEQLELD DAIKAVRALA LYFQLINIVE QHYEQRNQKI IRSTTTEDQV
     NGSQVDSIID KLIEGETQKV VVDSGDKDYS YFEQKPNPAS GGTFHWLFPH LQQLNMPPQK
     IQDLLDELDI RLVFTAHPTE IVRHTIRKKQ RRISQILERL DVAEESCRAM GLTNSYEAEH
     FRNRLMDEIQ LWWRTDELHQ FKPTVLDEVD YALHYFQEVL FDSLPHLSKR LQQALHNTFP
     KLKPPSHKFC YFGSWVGGDR DGNPFVTPEV TWSTACYQRN LVIEKYLESV AKLNDVLSLS
     LHWCNVLPEL LDSLEKDRIK MPEVYDKLYV RYRQEPYRLK LAFIEKKLEN TKARNEALSN
     PETRKSIKLA TKDDNLYPSA SDFLEDLNLL KLNLEQTGLN CQELDHLIFQ VDIYGFHLAE
     LDFRQDSSRH SDALNEIAEY LGVLDKPYNE LSEEEKTAWL VRELKTRRPL VPNPIPFSET
     TAETIETFKV LRALQVEFGI EICNTYIISM TNYVSDVLEV LLLAKEAGLY DPVIGASSIR
     IVPLFETVED LKRSHSVMKE LFDLPLYRAC LAGGYDSSGD SQSNVTMPKL TPHNLQEIML
     GYSDSNKDSG FMSSNWEIHK AQKVLAKLGN AYGVKIKIFH GRGGSVGRGG GPAYAAILAQ
     PTSTINGRIK ITEQGEVLAS KYSLPELALY NLETISTAVI QASLLGSGFD DIEPWNEIME
     EIAIASRKAY RSLIYEEPDF IDFFLSVTPI EEISKLQISS RPARRKKGKK DISSLRAIPW
     VFSWTQSRFL LPAWYGVGTA LQEFLAKEPE ENLKLLRYFY LKWPFFKMVI SKVEMTLSKV
     DLQMASHYVE ELAEDEDKER FHKLFSQIAK EYYLSREMVL KINQQERLLD TDPELQRSVQ
     LRNGSIVPLG FLQVSLLKRL REYANQDKAG LIHFRYSKDE LLRGALLTIN GIAAGMRNTG
//
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