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Database: UniProt/TrEMBL
Entry: A2TXN6_9FLAO
LinkDB: A2TXN6_9FLAO
Original site: A2TXN6_9FLAO 
ID   A2TXN6_9FLAO            Unreviewed;       859 AA.
AC   A2TXN6;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   07-JUN-2017, entry version 63.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00635171};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00635171};
GN   Name=ppc {ECO:0000313|EMBL:EAQ43038.1};
GN   ORFNames=MED152_09950 {ECO:0000313|EMBL:EAQ43038.1};
OS   Polaribacter sp. MED152.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Polaribacter.
OX   NCBI_TaxID=313598 {ECO:0000313|EMBL:EAQ43038.1, ECO:0000313|Proteomes:UP000006470};
RN   [1] {ECO:0000313|EMBL:EAQ43038.1, ECO:0000313|Proteomes:UP000006470}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED152 {ECO:0000313|EMBL:EAQ43038.1};
RX   PubMed=17215843; DOI=10.1038/nature05381;
RA   Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P.,
RA   Pascher T., Neutze R., Pedros-Alio C., Pinhassi J.;
RT   "Light stimulates growth of proteorhodopsin-containing marine
RT   Flavobacteria.";
RL   Nature 445:210-213(2007).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle.
CC       {ECO:0000256|SAAS:SAAS00730191}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|SAAS:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00635164};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|SAAS:SAAS00635168}.
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DR   EMBL; CP004349; EAQ43038.1; -; Genomic_DNA.
DR   RefSeq; WP_015481732.1; NC_020830.1.
DR   ProteinModelPortal; A2TXN6; -.
DR   STRING; 313598.MED152_09950; -.
DR   EnsemblBacteria; EAQ43038; EAQ43038; MED152_09950.
DR   KEGG; pom:MED152_09950; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   KO; K01595; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000006470; 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   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:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006470};
KW   Lyase {ECO:0000256|SAAS:SAAS00635169, ECO:0000313|EMBL:EAQ43038.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:EAQ43038.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006470}.
SQ   SEQUENCE   859 AA;  98407 MW;  99BD54D201A37376 CRC64;
     MSTLPKLTKF NDNVLSKYQI YNSIFITLPF DTINNTGVLL PLFHKVCEKG FKNGKNPTEL
     VEKFFKKYQD TPSEKDKKDL LFQFIQYIER QVVLFDAIED AAFPVVNNMD GFGTLRNSKE
     SATLSGKDEA LKKYLEDFKV RVVLTAHPTQ FYPGSVLGII TDLDKAIQND DLLLIKKLLA
     QLGKTPFYKK SKPTPFDEAV SLIWYLENVF YHSVSKIHNY IQEHVYDGQP TENEIIDLGF
     WPGGDRDGNP FVTTQITLDV AERLRQSILR NYYRDVRRLK RRFTFDGVQE ILSRVEKRLY
     KHVVRSYAKV NFSKEILLEE LENAREIVIK NHDSLFIDEL NDVINKVRIF GFHFATLDIR
     QDSRVHHKAF TQIVDDLLAS GDTTFPKNYQ RLSPEEQVEV LALVKGNIDP SIFSDEMSVK
     TIESIYALKT IQQRNGESGA NRYIISNNQT ALNVMQTFAM LNLCGFENEL PVDVIPLFET
     VDDLENASDV MRTLYSNKAY RYHLSKRKDK QTIMLGFSDG TKDGGYLMAN WGIFKAKEAL
     TKVSREFDIE VIFFDGRGGP PARGGGKTHQ FYASLGPTIE DKEIQLTIQG QTISSNFGTL
     DSSQFNLEQL ISSGIKNEVF TKDQINDTNR EIINDLANTS YKTYVDFKNH PQFLSYLEKM
     STLKYYAKTN IGSRPSKRSN SDTLDFSALR AIPFVGSWSQ LKQNVPGFFG VGTALKKYED
     ADRFDEIVAF YNASDFFKTL LENSMMSLTK SFFGLTAYMA DDPVYGEFWK LIYEEYKTTK
     RLLLKLTGHK ELMENYPEGK ASIAMRESIV LPLLTIQQFA LKKIQDLQQS EGNEAEIEVY
     EKMVMRSLFG NINASRNSA
//
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