(data stored in ACNUC1104 zone)

SWISSPROT: D5URG2_TSUPD

ID   D5URG2_TSUPD            Unreviewed;       614 AA.
AC   D5URG2;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   08-MAY-2019, entry version 57.
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=Tpau_0372 {ECO:0000313|EMBL:ADG77015.1};
OS   Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / JCM 10117 /
OS   NBRC 16120 / NCTC 13040) (Corynebacterium paurometabolum).
OC   Bacteria; Actinobacteria; Corynebacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG77015.1, ECO:0000313|Proteomes:UP000001213};
RN   [1] {ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C.,
RA   Tapia R., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG77015.1, ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RX   PubMed=21886861;
RA   Munk A.C., Lapidus A., Lucas S., Nolan M., Tice H., Cheng J.F.,
RA   Del Rio T.G., Goodwin L., Pitluck S., Liolios K., Huntemann M.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Tapia R., Han C., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Yasawong M., Brambilla E.M., Rohde M.,
RA   Sikorski J., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Tsukamurella paurometabola type strain
RT   (no. 33).";
RL   Stand. Genomic Sci. 4:342-351(2011).
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; CP001966; ADG77015.1; -; Genomic_DNA.
DR   RefSeq; WP_013125061.1; NC_014158.1.
DR   STRING; 521096.Tpau_0372; -.
DR   EnsemblBacteria; ADG77015; ADG77015; Tpau_0372.
DR   KEGG; tpr:Tpau_0372; -.
DR   eggNOG; ENOG4105C0M; Bacteria.
DR   eggNOG; COG1274; LUCA.
DR   HOGENOM; HOG000191700; -.
DR   KO; K01596; -.
DR   OMA; GPTNNWV; -.
DR   OrthoDB; 267285at2; -.
DR   BioCyc; TPAU521096:G1GKO-355-MONOMER; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001213; 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; D5URG2.
DR   SWISS-2DPAGE; D5URG2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001213};
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:ADG77015.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00452, ECO:0000256|SAAS:SAAS00442795,
KW   ECO:0000313|EMBL:ADG77015.1};
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:ADG77015.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001213};
KW   Transferase {ECO:0000313|EMBL:ADG77015.1}.
FT   DOMAIN       23    242       PEPCK_N. {ECO:0000259|Pfam:PF17297}.
FT   DOMAIN      247    613       PEPCK_GTP. {ECO:0000259|Pfam:PF00821}.
FT   NP_BIND     274    279       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   NP_BIND     523    526       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   REGION      222    224       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00452}.
FT   REGION      395    397       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00452}.
FT   ACT_SITE    275    275       {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   METAL       231    231       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   METAL       251    251       Manganese; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   METAL       298    298       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   BINDING      83     83       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   BINDING     273    273       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   BINDING     397    397       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   BINDING     428    428       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
SQ   SEQUENCE   614 AA;  67612 MW;  BA30A4F79E68504A CRC64;
     MTSATIDGLD GDSIPTKHAK LIEWVREVAE LTQPERVVWA DGSEEEWDRL TAEMVAAGTF
     TKLNENKKPN SFLALSDPAD VARVESRTYI CSETKEAAGP TNNWVRPAEM RATMTDLYRG
     SMQGRTMYVI PFCMGPLGAE DPKLGVEISD SPYVVVSMKI MTRMGTAVLD KLGEDGFFVK
     GLHSVGKPLA PGEADVPWPC SETKYITHFP ETREIWSYGS GYGGNALLGK KCYALRIASA
     MAHDEGWLAE HMLILKLISP EDKVYYIAAA FPSACGKTNL AMIQPTLPGW RAETVGDDIA
     WMRFGKDGRL YAVNPEFGFF GVAPGTSMDS NPNAMKTIDA GNTLFTNVAK TDDGDVWWEG
     MSAAPQHLTD WRGNDWESSS AENEDGLVTV AAHPNSRYTT PMSQCPSIAP EWDDPQGVPI
     SAILFGGRRK TTVPLVTQAR DWKHGVFMGA TVGSEQTAAA EGKVGTVRRD PMAMLPFLGY
     NVGDYFDHWL NIGKQADESK LPEVFYVNWF RRGEDKRFLW PGFGENTRVL KWIIDRIEGN
     AAGKETPVGI VATPEELDLT GLDTPVEDVA EALAVNVDEW RGEIPSIEEW FSFVGDKLPT
     GLQDELDALK QRLG
//

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