(data stored in ACNUC7421 zone)

SWISSPROT: E6S7H0_INTC7

ID   E6S7H0_INTC7            Unreviewed;       612 AA.
AC   E6S7H0;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 50.
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=Intca_0310 {ECO:0000313|EMBL:ADU46865.1};
OS   Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 /
OS   NBRC 12989 / 7 KIP).
OC   Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU46865.1, ECO:0000313|Proteomes:UP000008914};
RN   [1] {ECO:0000313|EMBL:ADU46865.1, ECO:0000313|Proteomes:UP000008914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC   {ECO:0000313|Proteomes:UP000008914};
RX   PubMed=21304734; DOI=10.4056/sigs.1263355;
RA   Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S.,
RA   Cheng J.F., Detter C., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Pukall R., Sikorski J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Intrasporangium calvum type strain (7
RT   KIP).";
RL   Stand. Genomic Sci. 3:294-303(2010).
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; CP002343; ADU46865.1; -; Genomic_DNA.
DR   STRING; 710696.Intca_0310; -.
DR   EnsemblBacteria; ADU46865; ADU46865; Intca_0310.
DR   KEGG; ica:Intca_0310; -.
DR   eggNOG; ENOG4105C0M; Bacteria.
DR   eggNOG; COG1274; LUCA.
DR   HOGENOM; HOG000191700; -.
DR   KO; K01596; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000008914; 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; E6S7H0.
DR   SWISS-2DPAGE; E6S7H0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008914};
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:ADU46865.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00452, ECO:0000256|SAAS:SAAS00442795,
KW   ECO:0000313|EMBL:ADU46865.1};
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:ADU46865.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008914};
KW   Transferase {ECO:0000313|EMBL:ADU46865.1}.
FT   DOMAIN       24    244       PEPCK_N. {ECO:0000259|Pfam:PF17297}.
FT   DOMAIN      248    608       PEPCK_GTP. {ECO:0000259|Pfam:PF00821}.
FT   NP_BIND     275    280       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   NP_BIND     518    521       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   REGION      223    225       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00452}.
FT   REGION      390    392       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00452}.
FT   ACT_SITE    276    276       {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   METAL       232    232       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   METAL       252    252       Manganese; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   METAL       299    299       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   BINDING      83     83       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   BINDING     274    274       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   BINDING     392    392       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   BINDING     423    423       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
SQ   SEQUENCE   612 AA;  67345 MW;  DB50B1D1EC92EF2E CRC64;
     MKGLAKLTTT PKTEQTTHAG LQAWVDEVAE LTQPRDIRWI TGTPEEWTEL TDQLVEAGTL
     VRLNEEKKPN SFWCASDPSD VARVEDRTFI CSVEERDAGP TNNWMAPDEM KAIMTDLYRG
     SMQGRTMYVI PFVMGHLDAK VPMFGVEITD SAYVAVSMLV MARCGEKVLR KIEETNASFV
     PALHSVGAPL AEGEQDVTWP CSDTKYIVHF PEERTIWSYG SGYGGNALLG KKCYSLRIAS
     AMARDEGWMA EHMLILKLTN PQGKVHYIAA AFPSACGKTN LAMIDPTIPG WKAEMVGDDI
     AWMRFGEDGR LYAVNPEAGL FGVAPGTGES TNPNAMATVN QGNSVFTNVA LTDDGDIWWE
     GMTDEKPAHL TSWLGEDWTP ESDKPAAHPN SRFCTPIAQC PIAAPEYDNP DGVPISAILF
     GGRRKTTIPL VYESRDWTHG TFVGATLSSE TTAAATGAVG VVRRDPMAML PFLGYNATDY
     FGHWLQIGKQ ADASKLPRIF GVNWFRRDED GSFLWPGYGE NSRVLKWIVD RLEGDAEAVE
     TPIGLVPAPG ALDIDGLDVT EEHLAKAGAV RPEEWAEELP LIEEWFTKFG DELPAELWAE
     FDGLKARINA AQ
//

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