PCKG_RENSM
ID PCKG_RENSM Reviewed; 607 AA.
AC A9WL73;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Phosphoenolpyruvate carboxykinase [GTP] {ECO:0000255|HAMAP-Rule:MF_00452};
DE Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00452};
DE Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00452};
DE EC=4.1.1.32 {ECO:0000255|HAMAP-Rule:MF_00452};
GN Name=pckG {ECO:0000255|HAMAP-Rule:MF_00452};
GN OrderedLocusNames=RSal33209_0029;
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Renibacterium.
OX NCBI_TaxID=288705;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235;
RX PubMed=18723615; DOI=10.1128/jb.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
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:0000255|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:0000255|HAMAP-Rule:MF_00452};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00452};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00452};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_00452}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00452}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00452}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC family. {ECO:0000255|HAMAP-Rule:MF_00452}.
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DR EMBL; CP000910; ABY21787.1; -; Genomic_DNA.
DR RefSeq; WP_012243495.1; NC_010168.1.
DR AlphaFoldDB; A9WL73; -.
DR SMR; A9WL73; -.
DR STRING; 288705.RSal33209_0029; -.
DR PRIDE; A9WL73; -.
DR EnsemblBacteria; ABY21787; ABY21787; RSal33209_0029.
DR KEGG; rsa:RSal33209_0029; -.
DR eggNOG; COG1274; Bacteria.
DR HOGENOM; CLU_028872_1_1_11; -.
DR OMA; GPTNNWV; -.
DR OrthoDB; 267285at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002007; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
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;
KW Cytoplasm; Decarboxylase; Gluconeogenesis; GTP-binding; Lyase; Manganese;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..607
FT /note="Phosphoenolpyruvate carboxykinase [GTP]"
FT /id="PRO_1000080987"
FT ACT_SITE 274
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 221..223
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 230
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 250
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 273..278
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 297
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 388..390
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 390
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 421
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 516..519
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
SQ SEQUENCE 607 AA; 66756 MW; 12E563E9DAE4DBA0 CRC64;
MGLTAQPVLD TAPTTNKRLL DWVAEVAELT QPESIYWVDG SEAENTRLTD ELVAAGTLTR
LNPELFPNSF AGFSDPKDVA RVEEQTFICS EKEHDAGFTN NWMEPAEMRT KLSGLFKGSM
RGRTMYVIPF VMGHLDAKSP KFGVEITDSA YVVASMRIMA RIGTEVLRKI EEPDAFFVPA
IHSLGAPLEP GQADVPWPCN DEKWIVHFPE SREIWSYGSG YGGNALLGKK CYALRIASVM
AHDEGWLAEH MLILKLTSPE QKTYYMAAAF PSACGKTNLA LLDPTIKGWK VETLGDDITW
MNFDDEGALR AVNPEAGLFG VAPGTGWDTN PNAMRAIAKG NSIFTNVALT DDGGVWWEGM
TTETPSHLTD WRGNSWTPDS AEPAAHPNSR FCTPIDQIDM LAPEYNEPDG VPLSAILFGG
RRKTTIPLVT QSRDWTNGIF MGSTLSSETT AAAAGAVGVV RRDPMAMLPF IGYDAGDYLK
HWVELSKQGD QEKLPKIFLV NWFRRTADGG FAWPGFGDNS RVVTWAIERI EGKADAVETP
IGFVPTKESL DLDGLDISDE QLSAALNVDA LEWAAEAESI DEWYRRFGGS LPEELLGELE
GLKERLG
