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Entry: A0A0X8WQJ6_9CYAN
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ID   A0A0X8WQJ6_9CYAN        Unreviewed;      1031 AA.
AC   A0A0X8WQJ6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   22-NOV-2017, entry version 13.
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   ECO:0000313|EMBL:BAU40841.1};
GN   ORFNames=O77CONTIG1_00648 {ECO:0000313|EMBL:BAU40841.1};
OS   Leptolyngbya sp. O-77.
OC   Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae;
OC   Leptolyngbya.
OX   NCBI_TaxID=1080068 {ECO:0000313|EMBL:BAU40841.1, ECO:0000313|Proteomes:UP000057790};
RN   [1] {ECO:0000313|EMBL:BAU40841.1, ECO:0000313|Proteomes:UP000057790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O-77 {ECO:0000313|EMBL:BAU40841.1,
RC   ECO:0000313|Proteomes:UP000057790};
RA   Tran K.T., Nguyen T.N., Yoon K-S., Ogo S.;
RT   "Complete genome sequence of Leptolyngbya sp. O-77.";
RL   Submitted (JAN-2016) 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; AP017367; BAU40841.1; -; Genomic_DNA.
DR   RefSeq; WP_068507961.1; NZ_AP017367.1.
DR   EnsemblBacteria; BAU40841; BAU40841; O77CONTIG1_00648.
DR   KEGG; let:O77CONTIG1_00648; -.
DR   PATRIC; fig|1080068.3.peg.733; -.
DR   KO; K01595; -.
DR   Proteomes; UP000057790; 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; 3.
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:UP000057790};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:BAU40841.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:BAU40841.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000057790}.
FT   ACT_SITE    202    202       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    679    679       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1031 AA;  118397 MW;  805310907209BCBE CRC64;
     MSSILHSSDD AFSTGTATED RDDQPLSATD LFLRHRLKLV EELWESVLQQ ECGQQLVDLL
     QQLRLVCSPE GQAPEEGEAI ALAVIEKLDL NDAIRAARAF ALYFQLINIV EQHYEQRGQQ
     QQYRASYDVA TASDDKQNGS DTQTAGLSAD MLERSLREET ALRREMSTFR GLFPKLANLN
     VPPRQIQNLI DNLDIRLVFT AHPTEIVRHT IRDKQRRIAK ILRQLDTAED SMRMLGLTSS
     WETETLREQL TEEIRLWWRT DELHQFKPTV LDEVDYALHY FQEVLFDVIP HLYYRFRSAL
     KATFPGLHPP RYNFCKFGSW VGSDRDGNPS VTPEITWKTA CYQRNLVLAK YIQSVKHLIN
     LLSLSLHWSD VLPDLLESLE QDQAQMPEVY EQLAIRYRQE PYRLKLSYIQ KRLENTCERS
     RKLYNGDYFN DESPDYNPAT LYRSGDEFLA DLQLIRRNLE ETGLTCRDLE NLICQVEIYG
     FNLAHLDIRQ ESGRHSDAIA EIAEYLQILP KSYHEMTEEE RSHWLATELK TRRPLIPSEL
     PFSEKTCETI QTFRMVRKLH QEFGPAICQT YVISMSHHAS DLLEVLLLAK EAGIYDPATG
     SGAINVVPLF ETVEDLLRAP AVMKELFELP LYRAYLSGGY AERQQEETGQ KVDIAGSRST
     LPQRASLQEI MLGYSDSNKD SGFLSSNWEI HKAQQSLQAM AETYGISLRI FHGRGGSVGR
     GGGPAYEAIL AQPGRSIDGR IKITEQGEVL ASKYNLPELA LYNLETITAA VVQASLLRNG
     FDDIQPWHEI MEELATRSRS HYRSLIYEQP DFVDFFHQVT PIEEISQLQI SSRPARRGGK
     KDLGSLRAIP WVFSWTQTRF LLPSWYGVGT AINEFLQEEP EENLKLLRYF YYKWPFFKMV
     ISKCEMTLSK VDLQIANHYV QQLSQPEDRE RFERLFEQIR DEYHLTKGLV LAIAGHERLL
     DGDPDLQRSV QLRNSTIVPL GFLQVSLLKR LRQHKTSAAS GVIRSRYSRG ELLRGALLTI
     NGIAAGMRNT G
//
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