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Database: UniProt/TrEMBL
Entry: Q31KY7_SYNE7
LinkDB: Q31KY7_SYNE7
Original site: Q31KY7_SYNE7 
ID   Q31KY7_SYNE7            Unreviewed;      1017 AA.
AC   Q31KY7;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   22-NOV-2017, entry version 86.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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:SAAS00946768};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=Synpcc7942_2252 {ECO:0000313|EMBL:ABB58282.1};
OS   Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1140 {ECO:0000313|EMBL:ABB58282.1, ECO:0000313|Proteomes:UP000002717};
RN   [1] {ECO:0000313|Proteomes:UP000002717}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 {ECO:0000313|Proteomes:UP000002717};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC
RT   7942.";
RL   Submitted (AUG-2005) 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:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
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:SAAS00946753}.
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DR   EMBL; CP000100; ABB58282.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q31KY7; -.
DR   STRING; 1140.Synpcc7942_2252; -.
DR   PRIDE; Q31KY7; -.
DR   EnsemblBacteria; ABB58282; ABB58282; Synpcc7942_2252.
DR   KEGG; syf:Synpcc7942_2252; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OrthoDB; POG091H040O; -.
DR   BioCyc; SYNEL:SYNPCC7942_2252-MONOMER; -.
DR   Proteomes; UP000002717; 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   PANTHER; PTHR30523; PTHR30523; 1.
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:SAAS00946757};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002717};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:ABB58282.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ABB58282.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002717}.
FT   ACT_SITE    210    210       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    663    663       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1017 AA;  117292 MW;  856E209D3FA5D469 CRC64;
     MNYCQNARTA MSAALQSSDD AFRTVSSPLA TDLDLSSPLE FFLRHRLTVV EELWEVVLRQ
     ECGQELVDIL TQLRDLTSPE GQAPEVGGEA LVQVIETLEL SDAIRAARAF ALYFQLINIV
     EQHYEQTQYQ LAYERSRLEP LPGPDESPEG LHTIEIPQHQ LDPFAAVIPL NQDPATFQTL
     FPRLRQLNVP PQMIQELTDR LDIRLVFTAH PTEIVRHTIR DKQRRIAYLL RQLDELETGK
     NRGFRELEAQ NIRQQLTEEI RLWWRTDELH QFKPTVLDEV DYALHYFQEV LFEAIPLLYQ
     RFRLALQGTF PDLQPPRYNF CQFGSWVGSD RDGNPSVTSA VTWQTACYQR SLVLDRYITA
     VEHLRNVLSL SMHWSEVLPE LLSSLEQESM LFPETYEQLA VRYRQEPYRL KLSYILERLH
     NTRDRNTRLQ QQQEKDPTTP LPEYRDGTLY QAGTAFLEDL KLIQHNLKQT GLSCYELEKL
     ICQVEIFGFN LVHLDIRQES SRHSDAINEI CEYLQILPQP YNELSEAERT AWLVQELKTR
     RPLVPARMPF SESTREIIET LRMVKQLQEE FGEAACQTYI ISMSRELSDL LEVLLLAKEV
     GLYDPVTGKS SLQVIPLFET VEDLQNAPRV MTALFELPFY TQLNPTQSEP LQEVMLGYSD
     SNKDSGFLSS NWEIHKAQKA LGTVARDHRV KLRIFHGRGG SVGRGGGPAY EAILAQPGRT
     TDGRIKITEQ GEVLASKYAL PELALYNLET ITTAVIQSSL LGSGFDDIEP WNQIMEELAA
     RSRRHYRALV YEQPDLVDFF NQVTPIEEIS KLQISSRPAR RKTGKRDLGS LRAIPWVFSW
     TQSRFLLPSW YGVGTALQEF LQERPEQNLN LLRYFYEKWP FFRMVISKVE MTLAKVDLQI
     AHHYVHELAN PEDQERFERV FSQIAAEFQL TCHLVLTITN HGRLLDGDPE LQRSVQLRNG
     TIVPLGFLQV ALLKRLRQYR QQTETTGLMR SRYSKGELLR GALLTINGIA AGMRNTG
//
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