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Database: UniProt/TrEMBL
Entry: A0A076HEW2_9SYNE
LinkDB: A0A076HEW2_9SYNE
Original site: A0A076HEW2_9SYNE 
ID   A0A076HEW2_9SYNE        Unreviewed;       997 AA.
AC   A0A076HEW2;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   07-JUN-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=KR52_00445 {ECO:0000313|EMBL:AII47663.1};
OS   Synechococcus sp. KORDI-52.
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=585425 {ECO:0000313|EMBL:AII47663.1, ECO:0000313|Proteomes:UP000028593};
RN   [1] {ECO:0000313|EMBL:AII47663.1, ECO:0000313|Proteomes:UP000028593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KORDI-52 {ECO:0000313|EMBL:AII47663.1,
RC   ECO:0000313|Proteomes:UP000028593};
RA   Choi D.H., Kwon K.-K., Lee J.-H., Noh J.H.;
RT   "Genome sequence of Synechococcus sp. KORDI-52.";
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; CP006271; AII47663.1; -; Genomic_DNA.
DR   RefSeq; WP_038551120.1; NZ_CP006271.1.
DR   EnsemblBacteria; AII47663; AII47663; KR52_00445.
DR   KEGG; synd:KR52_00445; -.
DR   KO; K01595; -.
DR   Proteomes; UP000028593; 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:UP000028593};
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:AII47663.1}.
FT   ACT_SITE    183    183       {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   997 AA;  113255 MW;  343194E00B519C22 CRC64;
     MPESTTPVSD HETARLSGGG SGAGQLLQHR LDLIEDLWKS VLRSECPPEQ SERLLRLKQL
     SDPVSLEGRD GDSTSEAIVE LIKAMDLSEA ISAARAFSLY FQLINILEQR IEEDSYLDSL
     RPNHSADAAQ RDAFDPFAPP LANQTDPATF GEVFERLRRM NVPPAQVEHL LRELDIRLVF
     TAHPTEIVRH TVRHKQRRVA NLLQQLQSDT PLAHQVREDC RDQLEEEIRL WWRTDELHQF
     KPTVIDEVDS TLHYFQQVLF DAMPQLRRRL IAALHRHYPD VQVPQASFCT FGSWVGSDRD
     GNPSVTPEIT WRTACYQRQL MLELYISSVQ TLRQQLSISM QWSQVAPALL ESLEMDRLRF
     PEIYERRAAR YRLEPYRLKL CYVLEKLERT LARNNQLSEA GWQMPCEALA DSQVGLSGAE
     VLHYTSVDQF RSDLELVRNS LVSTDLSCEQ LDTLLHQVHI FGFSLASLDI RQESTRHSDA
     IDELTRSLDL PQAYGDMDET QRMAWLLQEL QTRRPLIPPA ANWSAPTAET LAVFRMLQRL
     QEEFGPRICN SYVISMSHTA SDLLEVLLLA KETGLVDPPN KRASLLVVPL FETVEDLQRA
     PEVMEGLFKT PLYRALLPVV GQQKQPLQEL MLGYSDSNKD SGFLSSNWEI HQAQIALQEL
     ASRQDVALRL FHGRGGSVSR GGGPAYQAIL AQPSGTLQGR IKITEQGEVL ASKYSLPELA
     LYNLETVTTA VVQNSLVTNQ LDATPSWNQL MSRLATRSRE HYRALVHDNP DLVAFFQQVT
     PIEEISKLQI SSRPARRKTG AKDLSSLRAI PWVFGWTQSR FLLPSWFGFG TALSEEVGSD
     TEQLDLLRRL HQRWPFFRML ISKVEMTLSK VDLDLAHHYM NSLGHPEQRE AFEAIFQVIA
     KEYELTRKLV LEITGQNRLL GADQGLQLSV DLRNRTIVPL GFLQVALLKR LRDQNRQPPM
     SETPGAPEDT RTYSRSELLR GALLTLNGIA AGMRNTG
//
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