(data stored in SCRATCH zone)

SWISSPROT: A1SD50_NOCSJ

ID   A1SD50_NOCSJ            Unreviewed;       614 AA.
AC   A1SD50;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 85.
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=Noca_0190 {ECO:0000313|EMBL:ABL79735.1};
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL79735.1, ECO:0000313|Proteomes:UP000000640};
RN   [1] {ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
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., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Mattes T., Gossett J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABL79735.1, ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX   PubMed=21551312; DOI=10.1128/JB.05109-11;
RA   Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C.,
RA   Copeland A., Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A.,
RA   Hammon N.M., Han S., Hauser L.J., Israni S., Kim E., Kyrpides N.,
RA   Land M.L., Lapidus A., Larimer F.W., Lucas S., Pitluck S.,
RA   Richardson P., Schmutz J., Tapia R., Thompson S., Tice H.N.,
RA   Spain J.C., Gossett J.G., Mattes T.E.;
RT   "Genome Sequence of the ethene- and vinyl chloride-oxidizing
RT   actinomycete Nocardioides sp. strain JS614.";
RL   J. Bacteriol. 193:3399-3400(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; CP000509; ABL79735.1; -; Genomic_DNA.
DR   RefSeq; WP_011753686.1; NC_008699.1.
DR   STRING; 196162.Noca_0190; -.
DR   EnsemblBacteria; ABL79735; ABL79735; Noca_0190.
DR   KEGG; nca:Noca_0190; -.
DR   eggNOG; ENOG4105C0M; Bacteria.
DR   eggNOG; COG1274; LUCA.
DR   HOGENOM; HOG000191700; -.
DR   KO; K01596; -.
DR   OMA; GPTNNWV; -.
DR   OrthoDB; 267285at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000640; 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; A1SD50.
DR   SWISS-2DPAGE; A1SD50.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000640};
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:ABL79735.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00452, ECO:0000256|SAAS:SAAS00442795,
KW   ECO:0000313|EMBL:ABL79735.1};
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:ABL79735.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000640};
KW   Transferase {ECO:0000313|EMBL:ABL79735.1}.
FT   DOMAIN       28    249       PEPCK_N. {ECO:0000259|Pfam:PF17297}.
FT   DOMAIN      253    612       PEPCK_GTP. {ECO:0000259|Pfam:PF00821}.
FT   NP_BIND     280    285       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   NP_BIND     522    525       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   REGION      228    230       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00452}.
FT   REGION      394    396       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00452}.
FT   ACT_SITE    281    281       {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   METAL       237    237       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   METAL       257    257       Manganese; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   METAL       304    304       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   BINDING      88     88       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   BINDING     279    279       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   BINDING     396    396       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   BINDING     427    427       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
SQ   SEQUENCE   614 AA;  67600 MW;  AEDB96B39A3CE2AD CRC64;
     MTADTQAPIS TPTSDLSGRP STHPGILEFV SEVAALTQPD RIHWCTGSDE EWTVLTDALV
     STGTFTPLNP DLKPNSFHAA SDPMDVARVE GRTFICSVDE RDAGPTNNWM DPQEMKAIMR
     DLYAGCMRGR TMYVIPFVMG HLDAEQPMFG IEITDSAYVT ASMRVMARMG SNVLERMEEL
     EAEFVPALHS VGHPLEPGEA DVVWPCNDTK YIVQFPEEHA IWSYGSGYGG NALLGKKCYA
     LRIASVMARD EGWLAEHMLI LKLTSPQGVV KYVAAAFPSA CGKTNLAMLR PTIPGWKVET
     LGDDIAWMRV GEDGRLWAVN PEYGFFGVAP GTNEHTNPNA MTTINKGNSV FTNVALTEDG
     DVWWEGLENP PARATSWTGQ PWTPESEEPS SHPNSRYCTP IKQCDILAAE YDDPRGVPID
     AILFGGRRET TVPLVFEARD WTHGTFLGAT LSSETTAAAV GAVGVVRRDP MAMLPFIGYN
     AGDYFNHWIT VGKDNDEALL PRIFYVNWFR RDADGGFLWP GFGENSRVLK WVVERIDGQA
     AAVETPIGYV PTPESLDTDG LDLSAEDLAA ALAVDPEEWR AEVPQIQEWF EKFGEDLPAV
     LWTELDGLRA RLGS
//

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