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Database: UniProt/TrEMBL
Entry: A0A191TIS9_9BACT
LinkDB: A0A191TIS9_9BACT
Original site: A0A191TIS9_9BACT 
ID   A0A191TIS9_9BACT        Unreviewed;       856 AA.
AC   A0A191TIS9;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   22-NOV-2017, entry version 7.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00946768};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00946768};
GN   ORFNames=A9P82_04435 {ECO:0000313|EMBL:ANI88601.1};
OS   Arachidicoccus sp. BS20.
OC   Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales;
OC   Chitinophagaceae; Arachidicoccus.
OX   NCBI_TaxID=1850526 {ECO:0000313|EMBL:ANI88601.1, ECO:0000313|Proteomes:UP000078308};
RN   [1] {ECO:0000313|EMBL:ANI88601.1, ECO:0000313|Proteomes:UP000078308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS20 {ECO:0000313|EMBL:ANI88601.1,
RC   ECO:0000313|Proteomes:UP000078308};
RA   Im W.T., Siddiqi M.Z.;
RT   "Arachidicoccus sp. BS20 whole genome sequincing.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle.
CC       {ECO:0000256|SAAS:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00946766};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|SAAS:SAAS00946753}.
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DR   EMBL; CP015971; ANI88601.1; -; Genomic_DNA.
DR   RefSeq; WP_066204555.1; NZ_CP015971.1.
DR   EnsemblBacteria; ANI88601; ANI88601; A9P82_04435.
DR   KEGG; arb:A9P82_04435; -.
DR   KO; K01595; -.
DR   Proteomes; UP000078308; Chromosome.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PTHR30523; 2.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|SAAS:SAAS00946757};
KW   Complete proteome {ECO:0000313|Proteomes:UP000078308};
KW   Lyase {ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ANI88601.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078308}.
SQ   SEQUENCE   856 AA;  98335 MW;  5AFC9E202720FBE3 CRC64;
     MQNSSLLQFR NKVGLRFQLY NSLFTSLPFH RIEKTGVWLS LFLIHCEEGY KKSQSPVELI
     ETFLQQYSTY EDEREQLDML FRFIQYIERQ VVLFDALEDA SFADIQDVSG QGTMKQLRAQ
     TELQDKQAAL AEKVKDFSVR LVLTAHPTQF YPGEVLGIIN DLASALNSNN TQNINDYLVQ
     LAKTPFLKKK KPTPYDEALS LIWYLENVFY QAAGKIVADL QMQFPEMLFE KNSIIRMGFW
     PGGDRDGNPY VNSNTTVQVA EQLHQSILFC YYRDIRKLKR RLTFKGVGED VEAMEKAFHA
     VLLEQNKDIK ITEEWLLDSL RKLRTKIIEQ HNGLFVRLID DLIGKINIFG IYFATIDIRQ
     DSGVHQRLMQ HLSETENGLP KNYTSLSEEE KVDVIIKIKK PANEKLLKEP VFIDTFESMK
     AMKAIQKMNG EFGCNRYIIS HCTSLLDVME VYGLLKLSGW EKKEHSVDIL PLFETIEDLQ
     TAGEVMEKLY NNKTYRNHLQ HRNNTQSIML GFSDGTKDGG YLMANWCIYK AKEELTRISR
     KYDINVVFFD GRGGPPARGG GKTHKFYASM GSNIENKEIQ VTVQGQTVSS NFGTVQSAQY
     NIEQLLNAGI SNDVLFSKKE TLTKEEETLL SQLSEEGFAS YSELKEHPYF MEYLSYASPL
     KFYGATNIGS RPTKRNASAK LTLNDLRAIP YVGAWSQLKQ NVTGYYGVGT ALQKLEKAGK
     FKALKDLYKN SLFFRALIDN SEMSMKKCFF PLTQFHAKHP KYGEIWKKIY EEYLLTEKMV
     LRLSGQTELM ANYPVESLSI QMRERIVLPL VTIQQFGLHK YTELEQSGAK SNLKEVYEKL
     IMRCSFGIIN AGRNSA
//
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