(data stored in SCRATCH zone)

SWISSPROT: Q47TU3_THEFY

ID   Q47TU3_THEFY            Unreviewed;       604 AA.
AC   Q47TU3;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 100.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase [GTP] {ECO:0000256|HAMAP-Rule:MF_00452};
DE            Short=PEP carboxykinase {ECO:0000256|HAMAP-Rule:MF_00452};
DE            Short=PEPCK {ECO:0000256|HAMAP-Rule:MF_00452};
DE            EC=4.1.1.32 {ECO:0000256|HAMAP-Rule:MF_00452};
DE   AltName: Full=GTP-dependent phosphoenolpyruvate carboxykinase {ECO:0000256|HAMAP-Rule:MF_00452};
DE            Short=GTP-PEPCK {ECO:0000256|HAMAP-Rule:MF_00452};
GN   Name=pckG {ECO:0000256|HAMAP-Rule:MF_00452};
GN   OrderedLocusNames=Tfu_0083 {ECO:0000313|EMBL:AAZ54121.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54121.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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:0000256|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:0000256|HAMAP-Rule:MF_00452};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00452};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00452};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00452}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00452}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00452}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC       family. {ECO:0000256|HAMAP-Rule:MF_00452}.
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DR   EMBL; CP000088; AAZ54121.1; -; Genomic_DNA.
DR   RefSeq; WP_011290530.1; NC_007333.1.
DR   STRING; 269800.Tfu_0083; -.
DR   EnsemblBacteria; AAZ54121; AAZ54121; Tfu_0083.
DR   KEGG; tfu:Tfu_0083; -.
DR   eggNOG; ENOG4105C0M; Bacteria.
DR   eggNOG; COG1274; LUCA.
DR   HOGENOM; HOG000191700; -.
DR   KO; K01596; -.
DR   OMA; GPTNNWV; -.
DR   OrthoDB; 267285at2; -.
DR   BioCyc; TFUS269800:G1G4Q-83-MONOMER; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
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; Q47TU3.
DR   SWISS-2DPAGE; Q47TU3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00452};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00452,
KW   ECO:0000256|SAAS:SAAS00051790};
KW   Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00452};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00452};
KW   Kinase {ECO:0000313|EMBL:AAZ54121.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00452, ECO:0000256|SAAS:SAAS00442795,
KW   ECO:0000313|EMBL:AAZ54121.1};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00452};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00452};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00452,
KW   ECO:0000256|SAAS:SAAS00071028};
KW   Pyruvate {ECO:0000313|EMBL:AAZ54121.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000313|EMBL:AAZ54121.1}.
FT   DOMAIN       20    240       PEPCK_N. {ECO:0000259|Pfam:PF17297}.
FT   DOMAIN      244    603       PEPCK_GTP. {ECO:0000259|Pfam:PF00821}.
FT   NP_BIND     271    276       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   NP_BIND     513    516       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   REGION      219    221       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00452}.
FT   REGION      385    387       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00452}.
FT   ACT_SITE    272    272       {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   METAL       228    228       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   METAL       248    248       Manganese; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   METAL       295    295       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   BINDING      80     80       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   BINDING     270    270       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   BINDING     387    387       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   BINDING     418    418       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
SQ   SEQUENCE   604 AA;  67433 MW;  FE3F2D6AC3626024 CRC64;
     MTTAVHGNNV APTSHQELVD WVREIAELTQ PDEVVWCDGS DAEWERLTSQ LVEQGTLIRL
     NEELRPNSFY CRSDPSDVAR VEDRTFICSE RQEDAGPTNN WVDPAEMRAT LKEIFTGCMR
     GRTMYVVPFC MGPLGGKISQ LGVEITDSPY VVVSMRIMTR MGAPALRLIE ERGTFVKAVH
     SVGAPLEPGQ KDVPWPCNST KYITHFPETR EIWSYGSGYG GNALLGKKCY ALRIASVMAR
     DEGWLAEHML IIKVTPPSGE PRYIAAAFPS ACGKTNLAML QPTIPGWKVE TIGDDIAWMR
     FGEDGRLYAI NPEYGFFGVA PGTGESTNAN AVKALWGNSI FTNVALTDDG DVWWEGLTDE
     PPAHLTDWRG RDWTPDSGEP AAHPNARFTT PASQAPTIAP EWEDPNGVPI SVILFGGRRA
     TAVPLVVEAF NWQHGVYLGA NVASERTAAA EGKVGELRRD PFAMLPFCGY NMGDYFGHWL
     KIGRQTDPDK LPRIYYVNWF RKNDEGKFIW PGFGENSRVI KWIIERLEGK AAAQDTPIGR
     VPTPEALDTE GLDISQEDLE LLLSVDREVW RQEADLVPDF FNSFGDRLPK ELWDEYEALR
     QRLG
//

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