(data stored in ACNUC7421 zone)

SWISSPROT: PCKA_RHOPS

ID   PCKA_RHOPS              Reviewed;         537 AA.
AC   Q13E86;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000255|HAMAP-Rule:MF_00453};
DE            Short=PCK {ECO:0000255|HAMAP-Rule:MF_00453};
DE            Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00453};
DE            Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00453};
DE            EC=4.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00453};
GN   Name=pckA {ECO:0000255|HAMAP-Rule:MF_00453};
GN   OrderedLocusNames=RPD_0365;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate;
CC         Xref=Rhea:RHEA:18617, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC         EC=4.1.1.49; Evidence={ECO:0000255|HAMAP-Rule:MF_00453};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00453};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00453};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC       family. {ECO:0000255|HAMAP-Rule:MF_00453}.
DR   EMBL; CP000283; ABE37603.1; -; Genomic_DNA.
DR   RefSeq; WP_011500792.1; NC_007958.1.
DR   SMR; Q13E86; -.
DR   STRING; 316057.RPD_0365; -.
DR   EnsemblBacteria; ABE37603; ABE37603; RPD_0365.
DR   KEGG; rpd:RPD_0365; -.
DR   eggNOG; ENOG4105DJ1; Bacteria.
DR   eggNOG; COG1866; LUCA.
DR   HOGENOM; HOG000271471; -.
DR   KO; K01610; -.
DR   OMA; MRYAGEM; -.
DR   OrthoDB; 146648at2; -.
DR   BioCyc; RPAL316057:RPD_RS01885-MONOMER; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   CDD; cd00484; PEPCK_ATP; 1.
DR   Gene3D; 3.40.449.10; -; 1.
DR   Gene3D; 3.90.228.20; -; 1.
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   PANTHER; PTHR30031; PTHR30031; 1.
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;
DR   PRODOM; Q13E86.
DR   SWISS-2DPAGE; Q13E86.
KW   ATP-binding; Complete proteome; Cytoplasm; Decarboxylase;
KW   Gluconeogenesis; Lyase; Manganese; Metal-binding; Nucleotide-binding.
FT   CHAIN         1    537       Phosphoenolpyruvate carboxykinase (ATP).
FT                                /FTId=PRO_1000026345.
FT   NP_BIND     236    244       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   METAL       201    201       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   METAL       220    220       Manganese; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   METAL       257    257       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING      61     61       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING     195    195       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING     201    201       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   BINDING     201    201       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING     220    220       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   BINDING     285    285       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   BINDING     323    323       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   BINDING     323    323       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING     448    448       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
SQ   SEQUENCE   537 AA;  58485 MW;  0C4601B6382FE06D CRC64;
     MQETGVHNGA HGADKFGLKN LKGIYWNFGA PQLYEHALRN GEAVLSADGA LVADTGVFTG
     RSPKDKFTVR DATTETTMWW GGNQSITAEQ FETLYQDFIK HAEGMTLFAQ DLYGGADPSF
     QIKTRVFTEL AWHSLFIRTL LRRPDRADLA AFVPELTLID LPSFRADPKR HGCRSENVVA
     IDFARKIVLI GGTQYAGEMK KSVFTTLNYY LPERGVLPMH CSANVGPAGD TAIFFGLSGT
     GKTTLSADPN RTLIGDDEHG WGKDGVFNFE GGCYAKCIKL SPEAEPEIFA ASSRFGAVLE
     NVVLDEITRK PDFDNGSKTE NTRSAYPLES IPNASPTGRA GQPKNVVMLA ADAFGVMPPI
     AKLTPAQAMY HFLSGYTAKV AGTERGVTEP TPEFSTCFGS PFLPRDPSVY GNMLRDLIHN
     HNVDCWLVNT GWTGGKYGTG HRMPIKVTRA LLTAALDGSL RNAEFRTDPY FGFAVPTALP
     GVPSDILEPA KTWADKAEFD KTARALVGMF QKNFAKFEAQ VDADVRAAAP DVKIAAE
//

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