PCKG_ACIAD
ID PCKG_ACIAD Reviewed; 609 AA.
AC Q6F8P2;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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}; OrderedLocusNames=ACIAD2842;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG69573.1; -; Genomic_DNA.
DR RefSeq; WP_004929305.1; NC_005966.1.
DR AlphaFoldDB; Q6F8P2; -.
DR SMR; Q6F8P2; -.
DR STRING; 62977.ACIAD2842; -.
DR EnsemblBacteria; CAG69573; CAG69573; ACIAD2842.
DR GeneID; 45235078; -.
DR KEGG; aci:ACIAD2842; -.
DR eggNOG; COG1274; Bacteria.
DR HOGENOM; CLU_028872_1_1_6; -.
DR OMA; GPTNNWV; -.
DR OrthoDB; 267285at2; -.
DR BioCyc; ASP62977:ACIAD_RS12815-MON; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000430; 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..609
FT /note="Phosphoenolpyruvate carboxykinase [GTP]"
FT /id="PRO_0000103588"
FT ACT_SITE 269
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 216..218
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 225
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 245
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 268..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 294
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 382..384
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 384
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 415
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 609 AA; 67306 MW; 5301EBFB66E3231E CRC64;
MTQVNAPEFV RHPKLIAWVE EIAKLTKPAK IEWCDGSDEE YQRLIDLMIA NGTMQALNQE
KHPGSYLANS DPSDVARVED RTFICSEKQE DAGATNNWEA PEVMRAKLNG LFDGCMQGRT
MYVVPFSMGP LGSHIAQIGI ELTDSPYVAV SMRKMARMGK AVYDVLGTDG EFVPCVHTVA
APLAEGQKDV AWPCNPEKYI VHYPETREIW SYGSGYGGNA LLGKKCLALR IASAMGREQG
WLAEHMLILG VTNPKGEKHY IAAAFPSACG KTNFAMLIPP AGYEGWKIET VGDDIAWIKP
GEDGRLYAIN PEAGFFGVAP GTNTKTNPNC MATLHKDVIY TNVAVTEDGQ VWWEGLSKEV
PANLTNWKGQ PHVAGEKAAH PNARFTVAAG QCPSIDADWE NPAGVPISAF IFGGRRADTV
PLVSEAFDWV DGVYKAATMG SETTAAAVGQ QGIVRRDPFA MLPFAGYNMA DYFDHWLQLG
QQVGEKAEAA GNKLPKIFNV NWFRRDAEGN FVWPGFGQNM RVLEWMIDRV EGRANAVETP
IGYVPTYEDL NWTGTDFSKE EFDLITSQSK DQWITEIESH TELFNKLGER LPKALKERQD
QLLQAVQKI
