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Database: UniProt/TrEMBL
Entry: A5GVT4_SYNR3
LinkDB: A5GVT4_SYNR3
Original site: A5GVT4_SYNR3 
ID   A5GVT4_SYNR3            Unreviewed;       992 AA.
AC   A5GVT4;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   07-JUN-2017, entry version 70.
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=pepC {ECO:0000313|EMBL:CAK28993.1};
GN   Synonyms=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN   ECO:0000313|EMBL:CAK28993.1};
GN   OrderedLocusNames=SynRCC307_2090 {ECO:0000313|EMBL:CAK28993.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK28993.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK28993.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RA   Genoscope;
RL   Submitted (MAY-2006) 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; CT978603; CAK28993.1; -; Genomic_DNA.
DR   RefSeq; WP_011936504.1; NC_009482.1.
DR   ProteinModelPortal; A5GVT4; -.
DR   STRING; 316278.SynRCC307_2090; -.
DR   EnsemblBacteria; CAK28993; CAK28993; SynRCC307_2090.
DR   KEGG; syr:SynRCC307_2090; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000001115; 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; 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:UP000001115};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:CAK28993.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:CAK28993.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115}.
FT   ACT_SITE    177    177       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    636    636       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   992 AA;  113354 MW;  B0FE90B77305615C CRC64;
     MIETSSTAST SRMPASQTET VQPVGRRTLR QLNERLELVE ELWGNVLRSE CPPEQAARVL
     QLKQLCREDE TSDQIIDLIV AMDLSEAIAA ARAFSLYFQL VNILEQHIEE DRYLATMSQD
     NIAEAAISDT LNGHLANHDQ PATFQRLFQR LRALNVPPGL LEPLLRELDV RLVFTAHPTE
     IVRHTVRHKH RRVAHLIQRL EGLNDENDSF DDRQGLRQQL LEEIRVWWRT DELHQFKPSV
     LDEVDYALHF FQQVLFQAMP LLHERIRKAL KDSYPDVTPP EDGFCTFGSW VGSDRDGNPS
     VTPEITWRTA CYQRQLMLER YLSSVRNLRN QLSISMQWSQ VSPALLESLE MDRLRFPEIY
     EKLAARYRLE PYRLKLCYVL QRLELTHERN AQLSELGWES PLSATEPEEQ TLSSSLTPQQ
     ELHYSTYQDF RSDLELVRTS LEATGLSCEP LNRLLSQVQI FGFCLASLDI RQESTRHSEA
     LAELTRYLQL PQDYEAMEEP QRVEWLLEQL QTRRPLIPTG PLWSDATAET FAVFQMLRRL
     QEEFGQRICR TYVISMSHTE SDLLEVLLLA KEAGLVDPVE GTTRLQVIPL FETVEDLRCA
     PEVMGAVMAR PFYKRLLANE EVPLQEVMLG YSDSNKDSGF LSSNWEIHRA QIALQSLCSE
     HNISLRIFHG RGGSVSRGGG PAYQAILAQP SGTLKGRIKI TEQGEVLASK YALPELALYN
     LETVTTAVLQ NSLLSSGVDD TPSWNELMER LASRSRQHYR ALVHEHPDLV AFFEQVTPIE
     EISKLQISSR PARRRTGARD LSSLRAIPWV FGWTQSRFLL PSWFGVGAAI REELGDDGEQ
     LDTLRTLYQR WPFFRMLISK VEMTLAKVDL SLAKYYVDSL GSADRADAFQ EIFATIAAEY
     SLTKELVLKI TGHERLLDGD PPLQLSVELR NRTIVPLGFL QVALLRRLRN QNRQPPMNES
     DLSDTRTYSR GELLRGALLT INGIAAGLRN TG
//
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