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Database: UniProt/TrEMBL
Entry: A0A1D7QDB6_9SPHI
LinkDB: A0A1D7QDB6_9SPHI
Original site: A0A1D7QDB6_9SPHI 
ID   A0A1D7QDB6_9SPHI        Unreviewed;       862 AA.
AC   A0A1D7QDB6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, 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=BFS30_05445 {ECO:0000313|EMBL:AOM76650.1};
OS   Pedobacter steynii.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=430522 {ECO:0000313|EMBL:AOM76650.1, ECO:0000313|Proteomes:UP000094313};
RN   [1] {ECO:0000313|EMBL:AOM76650.1, ECO:0000313|Proteomes:UP000094313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DX4 {ECO:0000313|EMBL:AOM76650.1,
RC   ECO:0000313|Proteomes:UP000094313};
RA   Seilhamer J.J.;
RL   Submitted (AUG-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; CP017141; AOM76650.1; -; Genomic_DNA.
DR   RefSeq; WP_069378344.1; NZ_CP017141.1.
DR   EnsemblBacteria; AOM76650; AOM76650; BFS30_05445.
DR   KEGG; psty:BFS30_05445; -.
DR   KO; K01595; -.
DR   Proteomes; UP000094313; 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:UP000094313};
KW   Lyase {ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AOM76650.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094313}.
SQ   SEQUENCE   862 AA;  98490 MW;  357FBB30A5573794 CRC64;
     MMQKQRAKGQ RESVFNNEVI SRFELYNSLF LTLPFYKVKD TGTLLPLFIK YCEDGVKNHE
     TPAGIINAFF EKYTQNNSKK DIIDLLFRFI QYIERQVVLF DAVEDASFNK LNADEEHSAL
     LVYLKKGVDN KPLNEKIEKL IDEFSLRLVL TAHPTQFYPG SVLSIITDLT SAIKTNDIST
     INQLLQQLGK TPFFNKKSPT PVDEALSLAW YLENVFYFAA ANIQSEIDQS LNDYNLESKK
     IIELGFWPGG DRDGNPNVHT DSTIQVSKML RQILFRCYYR DFRNLKRRIT FRGVEDNIAL
     VHDVLYKNAF DPNIETENIS DFLIENLNKI KTTLIEDHDG LFSDLVSDLI RKVELYGSHF
     ASLDIRQDSR VLRDVHAYCR NNKPINALYP ENYDSLNEEE KIKALVFKSA KINYTEQPDS
     LTQDTLETIA EIKQIQQSNG EMACHRFIIS NCQQASDILQ LMELFLWNGW TEDELSIDFV
     PLFETVHDLA GAAEIMETLY SHSFYKKHLA NRGGKQHIML GFSDSTKDGG YLMANWSIFN
     AKVALTATAD QHQIQLAFFD GRGGPPSRGG GKTHRFYASM GKEIANKNIQ LTIQGQTISS
     QYGSIDSAEF NMEQMINAGI SAGMKEKHNI LLDPLHKNLL DEMATESYDS YVSLRKHPLF
     LSYLEKFSPL TLLSKITISS RPVKRNSGGS LKLEDLRAIG FVTAWSQLKQ NIPGFYGIGT
     ALKNQEKQGN WDKVVKTYQE SGYFKTIIDN CMMSMSKADF SITAHFANDK EYGAFWKMLY
     EEFELSKTLL LKLSGHETLM ENYPVEKRSI SVREKIVLPL VLIQHYALEQ LQNEVTDEEQ
     QSLEKLSIRT VYGIVNAGRN LA
//
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