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Database: UniProt/TrEMBL
Entry: E1WIS7_SALTS
LinkDB: E1WIS7_SALTS
Original site: E1WIS7_SALTS 
ID   E1WIS7_SALTS            Unreviewed;       539 AA.
AC   E1WIS7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   11-JUN-2014, entry version 25.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase [ATP];
DE            Short=PCK;
DE            Short=PEP carboxykinase;
DE            Short=PEPCK;
DE            EC=4.1.1.49;
DE   AltName: Full=Phosphoenolpyruvate carboxylase;
GN   Name=pckA; OrderedLocusNames=SL1344_3467;
OS   Salmonella typhimurium (strain SL1344).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=216597;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL1344;
RA   Dougan G., Barrow P., Achtman M., Parkhill J., Thomson N.R.;
RT   "The genome sequence of Salmonella enterica subsp. enterica serovar
RT   Typhimurium SL1344.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL1344;
RX   PubMed=22538806; DOI=10.1073/pnas.1201061109;
RA   Kroger C., Dillon S.C., Cameron A.D., Papenfort K., Sivasankaran S.K.,
RA   Hokamp K., Chao Y., Sittka A., Hebrard M., Handler K., Colgan A.,
RA   Leekitcharoenphon P., Langridge G.C., Lohan A.J., Loftus B.,
RA   Lucchini S., Ussery D.W., Dorman C.J., Thomson N.R., Vogel J.,
RA   Hinton J.C.;
RT   "The transcriptional landscape and small RNAs of Salmonella enterica
RT   serovar Typhimurium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:E1277-E1286(2012).
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes the
CC       conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP)
CC       through direct phosphoryl transfer between the nucleoside
CC       triphosphate and OAA (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + oxaloacetate = ADP + phosphoenolpyruvate
CC       + CO(2).
CC   -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [ATP]
CC       family.
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DR   EMBL; FQ312003; CBW19562.1; -; Genomic_DNA.
DR   RefSeq; YP_005183352.1; NC_016810.1.
DR   ProteinModelPortal; E1WIS7; -.
DR   SMR; E1WIS7; 6-539.
DR   EnsemblBacteria; CBW19562; CBW19562; SL1344_3467.
DR   PATRIC; 43193108; VBISalEnt88447_3860.
DR   OMA; GADPEHY; -.
DR   BioCyc; SENT216597:GJB7-3529-MONOMER; -.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.449.10; -; 1.
DR   Gene3D; 3.90.228.20; -; 2.
DR   HAMAP; MF_00453; PEPCK_ATP; 1.
DR   InterPro; IPR001272; PEP_carboxykinase_ATP.
DR   InterPro; IPR013035; PEP_carboxykinase_C.
DR   InterPro; IPR008210; PEP_carboxykinase_N.
DR   InterPro; IPR015994; PEPCK_ATP_CS.
DR   Pfam; PF01293; PEPCK_ATP; 1.
DR   PIRSF; PIRSF006294; PEP_crbxkin; 1.
DR   SUPFAM; SSF68923; SSF68923; 1.
DR   TIGRFAMs; TIGR00224; pckA; 1.
DR   PROSITE; PS00532; PEPCK_ATP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Decarboxylase;
KW   Gluconeogenesis; Kinase; Lyase; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyruvate; Transferase.
FT   NP_BIND     247    255       ATP (By similarity){EA2}.
FT   NP_BIND     448    449       ATP (By similarity){EA2}.
FT   METAL       212    212       Manganese (By similarity){EA2}.
FT   METAL       231    231       Manganese; via tele nitrogen (By
FT                                similarity){EA2}.
FT   METAL       268    268       Manganese (By similarity){EA2}.
FT   BINDING      64     64       Substrate (By similarity){EA2}.
FT   BINDING     206    206       Substrate (By similarity){EA2}.
FT   BINDING     212    212       ATP (By similarity){EA2}.
FT   BINDING     212    212       Substrate (By similarity){EA2}.
FT   BINDING     231    231       ATP (By similarity){EA2}.
FT   BINDING     296    296       ATP (By similarity){EA2}.
FT   BINDING     332    332       ATP (By similarity){EA2}.
FT   BINDING     332    332       Substrate (By similarity){EA2}.
FT   BINDING     454    454       ATP (By similarity){EA2}.
SQ   SEQUENCE   539 AA;  59647 MW;  3879067543BB8780 CRC64;
     MRVNNLTPQD LKAYGINDVQ DIVYNPSYDT LYQEELNPGL EGYERGVLTN LGAVAVDTGI
     FTGRSPKDKY IVRDDTTRDT LWWSDKGKGK NDNKPLSQET WQHLKGLVTH QLSGKRLFIV
     DAFCGANADT RLSVRFITEV AWQAHFVKNM FIRPTDEELV GFKPDFIVMN GAKCTNPQWK
     EQGLNSENFV AFNLTERIQL IGGTWYGGEM KKGMFSVMNY LLPLKGIASM HCSANVGEKG
     DVAVFFGLSG TGKTTLSTDP KRRLIGDDEH GWDDDGVFNF EGGCYAKTIK LSKEAEPEIY
     HAIRRDALLE NVTVREDGTV DFDDGSKTEN TRVSYPIYHI DNIVKPVSKA GHATKVIFLT
     ADAFGVLPPV SRLTANQTQY HFLSGFTAKL AGTERGVTEP TPTFSACFGA AFLTLHPTQY
     AEVLVKRMQA AGAQAYLVNT GWNGTGKRIS IKDTRAIIDA ILNGSLDNAE TFRLPLFDLA
     IPTELPGVDT HILDPRNTYA SPEQWQEKAT ALAKLFIENF EKYTDTPAGE ALVSAGPKL
//
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