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Database: UniProt/TrEMBL
Entry: A0A076GZZ1_9SYNE
LinkDB: A0A076GZZ1_9SYNE
Original site: A0A076GZZ1_9SYNE 
ID   A0A076GZZ1_9SYNE        Unreviewed;      1009 AA.
AC   A0A076GZZ1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   10-MAY-2017, entry version 18.
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=KR100_03495 {ECO:0000313|EMBL:AII42438.1};
OS   Synechococcus sp. KORDI-100.
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1280380 {ECO:0000313|EMBL:AII42438.1, ECO:0000313|Proteomes:UP000028591};
RN   [1] {ECO:0000313|EMBL:AII42438.1, ECO:0000313|Proteomes:UP000028591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KORDI-100 {ECO:0000313|EMBL:AII42438.1,
RC   ECO:0000313|Proteomes:UP000028591};
RA   Choi D.H., Kwon K.-K., Lee J.-H., Noh J.H.;
RT   "Genome sequence of Synechococcus sp. KORDI-100.";
RL   Submitted (JUN-2013) 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; CP006269; AII42438.1; -; Genomic_DNA.
DR   EnsemblBacteria; AII42438; AII42438; KR100_03495.
DR   KEGG; synk:KR100_03495; -.
DR   KO; K01595; -.
DR   Proteomes; UP000028591; 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:UP000028591};
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:AII42438.1}.
FT   ACT_SITE    195    195       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    651    651       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1009 AA;  114904 MW;  1EF7B0AABF46255E CRC64;
     MIMTKEENRG ASMQQPTVHA PGGELLRADG VVAGNGGLLQ QRLELIEDLW QTVLRSECPS
     EQSERVLRLK QLSDPVALDG RDGNSTSEAI VDLIKAMDLA EAIAAARAFS LYFQLINIVE
     QRIEEDGYLD SLLPSRNQTQ SHNHPFDPFA PPLASQTDPA TFGELFERLR RLNVPPAQIE
     SLLQELDIRL VFTAHPTEIV RHTVRRKQRR VANLLQRLQS DSLLNSQDEE VLRDQLEEEI
     RLWWRTDELH QFKPTVLDEV DSTLHHFQQV LFDAMPQMRR RLTSALSRHY PDVRFPQASF
     CTFGSWVGSD RDGNPSVTPE ITWQTACYQR QLMLERYVRS VQDLRSQLSI SMQWSQVAPE
     LLESLEMDRL RFPDIYEDRA ARYRLEPYRL KLSYVLERLQ LTLLRNNQLS EAGWQTPQEV
     AAQGIDRLQV GETLHYMAVD EFRSDLELIR NSLVSTALSC EQLDTLLNQV HIFGFSLASL
     DIRQESTRHS DAIDELTRYL ELPKPYGEMD EGERVEWLHR ELQTRRPLIP TGVDWSAATA
     ETMAVFRMLR RLQQEFGQRI CNSYVISMSH TGSDLLEVLL LAKQAGLVDP TARHSSLLVV
     PLFETVEDLQ RAPEVMKELF ESLLYRQLLP LVGGQRQPLQ ELMLGYSDSN KDSGFLSSNW
     EIHQAQMALQ ELASRHGVAL RLFHGRGGSV SRGGGPAYQA ILAQPSGTLQ GRIKITEQGE
     VLASKYSLPE LALYNLETMT TAVVQNSLVT NQLDATPSWN QLMTRLAGHS REHYRALVHD
     NPDLVPFFQQ VTPIEEISKL QISSRPARRK TGAKDLSSLR AIPWVFGWTQ SRFLLPSWFG
     VGTALAAEVK DDPEQLDLLR RLHQRWPFFR MLISKVEMTL SKVDLDLAHH YMTSLGAPDN
     RESFERIFRT IADEYELTRS LVLAITGQSR LLGADQALQL SVDLRNRTIV PLGFLQVALL
     KRLRDQNRQP PMSEAPGVEE DRRTYSRSEL LRGALLTLNG IAAGMRNTG
//
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