(data stored in ACNUC1104 zone)

SWISSPROT: PCKG_STRCO

ID   PCKG_STRCO              Reviewed;         609 AA.
AC   Q93JL5;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAY-2019, entry version 103.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase [GTP] {ECO:0000255|HAMAP-Rule:MF_00452};
DE            Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00452};
DE            Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00452};
DE            EC=4.1.1.32 {ECO:0000255|HAMAP-Rule:MF_00452};
GN   Name=pckG {ECO:0000255|HAMAP-Rule:MF_00452};
GN   OrderedLocusNames=SCO4979; ORFNames=2SCK36.02;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to
CC       phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic
CC       pathway that produces glucose from lactate and other precursors
CC       derived from the citric acid cycle. {ECO:0000255|HAMAP-
CC       Rule:MF_00452}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate;
CC         Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702;
CC         EC=4.1.1.32; Evidence={ECO:0000255|HAMAP-Rule:MF_00452};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00452};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00452};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00452}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00452}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00452}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC       family. {ECO:0000255|HAMAP-Rule:MF_00452}.
DR   EMBL; AL939122; CAC40592.1; -; Genomic_DNA.
DR   RefSeq; NP_629131.1; NC_003888.3.
DR   RefSeq; WP_003973998.1; NC_003888.3.
DR   SMR; Q93JL5; -.
DR   STRING; 100226.SCO4979; -.
DR   PRIDE; Q93JL5; -.
DR   EnsemblBacteria; CAC40592; CAC40592; CAC40592.
DR   GeneID; 1100420; -.
DR   KEGG; sco:SCO4979; -.
DR   PATRIC; fig|100226.15.peg.5060; -.
DR   eggNOG; ENOG4105C0M; Bacteria.
DR   eggNOG; COG1274; LUCA.
DR   HOGENOM; HOG000191700; -.
DR   InParanoid; Q93JL5; -.
DR   KO; K01596; -.
DR   OMA; GPTNNWV; -.
DR   PhylomeDB; Q93JL5; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR   GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IBA:GO_Central.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IBA:GO_Central.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0046327; P:glycerol biosynthetic process from pyruvate; IBA:GO_Central.
DR   GO; GO:0019543; P:propionate catabolic process; IBA:GO_Central.
DR   GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR   GO; GO:0033993; P:response to lipid; IBA:GO_Central.
DR   GO; GO:0042594; P:response to starvation; IBA:GO_Central.
DR   CDD; cd00819; PEPCK_GTP; 1.
DR   Gene3D; 3.40.449.10; -; 1.
DR   Gene3D; 3.90.228.20; -; 1.
DR   HAMAP; MF_00452; PEPCK_GTP; 1.
DR   InterPro; IPR018091; PEP_carboxykin_GTP_CS.
DR   InterPro; IPR013035; PEP_carboxykinase_C.
DR   InterPro; IPR008209; PEP_carboxykinase_GTP.
DR   InterPro; IPR035077; PEP_carboxykinase_GTP_C.
DR   InterPro; IPR035078; PEP_carboxykinase_GTP_N.
DR   InterPro; IPR008210; PEP_carboxykinase_N.
DR   PANTHER; PTHR11561; PTHR11561; 1.
DR   Pfam; PF00821; PEPCK_GTP; 1.
DR   Pfam; PF17297; PEPCK_N; 1.
DR   PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR   SUPFAM; SSF68923; SSF68923; 1.
DR   PROSITE; PS00505; PEPCK_GTP; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q93JL5.
DR   SWISS-2DPAGE; Q93JL5.
KW   Complete proteome; Cytoplasm; Decarboxylase; Gluconeogenesis;
KW   GTP-binding; Lyase; Manganese; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    609       Phosphoenolpyruvate carboxykinase [GTP].
FT                                /FTId=PRO_0000103615.
FT   NP_BIND     276    281       GTP. {ECO:0000255|HAMAP-Rule:MF_00452}.
FT   NP_BIND     518    521       GTP. {ECO:0000255|HAMAP-Rule:MF_00452}.
FT   REGION      224    226       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00452}.
FT   REGION      390    392       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00452}.
FT   ACT_SITE    277    277       {ECO:0000255|HAMAP-Rule:MF_00452}.
FT   METAL       233    233       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00452}.
FT   METAL       253    253       Manganese; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00452}.
FT   METAL       300    300       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00452}.
FT   BINDING      79     79       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00452}.
FT   BINDING     275    275       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00452}.
FT   BINDING     392    392       GTP. {ECO:0000255|HAMAP-Rule:MF_00452}.
FT   BINDING     423    423       GTP. {ECO:0000255|HAMAP-Rule:MF_00452}.
SQ   SEQUENCE   609 AA;  66917 MW;  80FF6E00B817875A CRC64;
     MARDIAAPPV PTNHQELISW VNEIAELTQP DAVVWCDGSE AEYERLCGEL VEKGTFRKLD
     PIKRPNSYYA ASDPTDVARV EDRTFICSAK EEDAGPTNHW KDPAEMRAIF TGDKGEGGLF
     RGSMRGRTMY VVPFCMGPLG SPLSALGVEI TDSAYVAASM RTMTRMGQPV LDELGDEGFF
     VKAVHSVGAP LEPGQADVPW PCNSTKYISH FPEDREIWSY GSGYGGNALL GKKCYALRIA
     SVMARDEGWL AEHMLVLKLT PPTGAPKYVA AAFPSACGKT NLAMLEPTIS GWTVETIGDD
     IAWMRFGEDG RLYAINPEAG FFGVAPGTGE HTNANAMKTL WGNSVFTNVA LTDDGDVWWE
     GMTEETPAHL TDWKGNDWTP ESGTPAAHPN ARFTTPAAQC PIIAPEWEDP RGVPISAILF
     GGRRATAVPL VTESFDWNHG VFLGANVASE KTAAAEGKVG ELRRDPFAML PFCGYNMGDY
     MGHWVDVAKD KDQSKLPKIY YVNWFRKDDA GRFVWPGFGE NGRVLKWIVE RLEGRADGVE
     TPIGVLPTKE SLDTDGLDLA DADLEFLLSV DKEVWREEAA LVPEHLNTFG DHTPAELWDQ
     YRALVRRLG
//

If you have problems or comments...

PBIL Back to PBIL home page