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Database: UniProt
Entry: R7KRJ4_9FIRM
LinkDB: R7KRJ4_9FIRM
Original site: R7KRJ4_9FIRM 
ID   R7KRJ4_9FIRM            Unreviewed;       611 AA.
AC   R7KRJ4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
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   ORFNames=BN622_01109 {ECO:0000313|EMBL:CDE78970.1};
OS   Ruminococcus sp. CAG:353.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1262955 {ECO:0000313|EMBL:CDE78970.1, ECO:0000313|Proteomes:UP000017936};
RN   [1] {ECO:0000313|EMBL:CDE78970.1, ECO:0000313|Proteomes:UP000017936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:353 {ECO:0000313|Proteomes:UP000017936};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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 derived
CC       from the citric acid cycle. {ECO:0000256|HAMAP-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; EC=4.1.1.32;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00452};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00452};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|HAMAP-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|ARBA:ARBA00005796, ECO:0000256|HAMAP-
CC       Rule:MF_00452}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDE78970.1}.
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DR   EMBL; CBJQ010000042; CDE78970.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7KRJ4; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000017936; Unassembled WGS sequence.
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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00819; PEPCK_GTP; 1.
DR   Gene3D; 3.90.228.20; -; 1.
DR   Gene3D; 3.40.449.10; Phosphoenolpyruvate Carboxykinase, domain 1; 1.
DR   Gene3D; 2.170.8.10; Phosphoenolpyruvate Carboxykinase, domain 2; 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; PHOSPHOENOLPYRUVATE CARBOXYKINASE; 1.
DR   PANTHER; PTHR11561:SF0; PHOSPHOENOLPYRUVATE CARBOXYKINASE, CYTOSOLIC [GTP]; 1.
DR   Pfam; PF00821; PEPCK_GTP; 1.
DR   Pfam; PF17297; PEPCK_N; 1.
DR   PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR   SUPFAM; SSF68923; PEP carboxykinase N-terminal domain; 1.
DR   SUPFAM; SSF53795; PEP carboxykinase-like; 1.
DR   PROSITE; PS00505; PEPCK_GTP; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00452};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_00452}; Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00452};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00452}; Kinase {ECO:0000313|EMBL:CDE78970.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00452};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00452};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00452};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00452}; Pyruvate {ECO:0000313|EMBL:CDE78970.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017936};
KW   Transferase {ECO:0000313|EMBL:CDE78970.1}.
FT   DOMAIN          11..226
FT                   /note="Phosphoenolpyruvate carboxykinase GTP-utilising N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17297"
FT   DOMAIN          230..608
FT                   /note="Phosphoenolpyruvate carboxykinase C-terminal P-loop"
FT                   /evidence="ECO:0000259|Pfam:PF00821"
FT   ACT_SITE        258
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         205..207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         214
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         234
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         257..262
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         285
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         386..388
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         388
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         419
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         513..516
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
SQ   SEQUENCE   611 AA;  68020 MW;  C1B37AF99D619E62 CRC64;
     MSLTNNPNVL KWVDEMVALT KPDKVVWIDG SKEQLDALTD EVCSLPEGNR DKMYRLNQEK
     LPGCLYHRTL PNDVARVEDR TFICTPTKEE AGPTNNWMDP KEMYAKLTPL YDGVMKGRTM
     YVIPYSMGPI GSPLAKVGVE LTDSIYVVLN MNIMTRMGKQ AFENLGDTSN DFVRGLHSKA
     DVDPENRYIV QFPQDNTIWS INSAYGGNVL LGKKCFALRI ASYQGKNEGW MAEHMLILGV
     KKPDGKVVYI TAAFPSACGK TNLAMLIPPK TYKDKGYEVF TVGDDIAWMK PGADGRLYAI
     NPENGFFGVA PGTNAKSNYN ALASTMKNTI FTNVALNNAD NTVWWEGLDK NPPEDATEWK
     GAKVNGKEYT SVIGADGKPQ KLAHPNSRFT APAVNCPCVS PEFNNPNGVP VSAIIFGGRR
     ASTTPLVYQS FDWTHGTYIG SAVSSETTAA AVGAVGVLRH DPMAMKPFIG YNVGDYWAHW
     LEMGEKLGDK APKIFNVNWF KQDEEGHFMW PGFGDNMRVL DWIIKRCEGT IDAEETAIGY
     LPKKGDINLE GIEDEVTPEI LDKLLYVDKD LWKKEIAEMR RYYKEDISDK GGHIPAALIA
     QLDKLEERLN K
//
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