PCKG_CHLAB
ID PCKG_CHLAB Reviewed; 603 AA.
AC Q5L4X1;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=CAB884;
OS Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=218497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27085 / S26/3;
RX PubMed=15837807; DOI=10.1101/gr.3684805;
RA Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT "The Chlamydophila abortus genome sequence reveals an array of variable
RT proteins that contribute to interspecies variation.";
RL Genome Res. 15:629-640(2005).
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; CR848038; CAH64324.1; -; Genomic_DNA.
DR RefSeq; WP_011097399.1; NC_004552.2.
DR AlphaFoldDB; Q5L4X1; -.
DR SMR; Q5L4X1; -.
DR EnsemblBacteria; CAH64324; CAH64324; CAB884.
DR KEGG; cab:CAB884; -.
DR eggNOG; COG1274; Bacteria.
DR HOGENOM; CLU_028872_1_1_0; -.
DR OMA; GPTNNWV; -.
DR OrthoDB; 267285at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001012; 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.
FT CHAIN 1..603
FT /note="Phosphoenolpyruvate carboxykinase [GTP]"
FT /id="PRO_0000103594"
FT ACT_SITE 269
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 76
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 292
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 381..383
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 383
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 414
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 508..511
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
SQ SEQUENCE 603 AA; 66780 MW; BF614C7F35CDC83F CRC64;
MTSVWSEAIQ HKDLKQWIQE VAELVTPKDI RICNGSDSEY VEIYGLMQQS GVAIPLNRDV
HPNCFLVRSS PEDVARVEQF TFICTKEQKD AGPTNNWRDP EEMRQELHGL FRGCMRGRTL
YVVPFCMGPL NSPFSLIGVE ITDSPYVVCS MKIMTRMGEE VLKALGTSGS FHKCLHSVGV
PLAPGEKDLA WPCNPQHMRI VHFQDDSSVM SFGSGYGGNA LLGKKCVALR LASYIARSQG
WLAEHMLIIG VTNPEGQKKY FAASFPSACG KTNLAMLKPK IPGWKVECVG DDIAWIRPGP
DGRLYAVNPE FGFFGVAPGT SATTNPNALA TCTSNSIFTN VALTPDGDVW WEGLTSQPPE
GLIDWQGKPW KPGGAPAAHP NSRFTTPVQQ CPVLDPQWNS PEGVPIEAMI FGGRRSETIP
LVYEALSWQH GVTIGASMSS ATTAASVGEQ GKLRHDPFAM LPFCGYNMAH YFDHWLSFAS
NTSLKLPKIY GVNWFRKDKN GNFIWPGFSD NLRVLEWIFR RTNGEESIAK KTPIGYLPEE
SALNLEGLNL STQALQDLLS VDVPGWLKEV ANVREYCKIF GSDLPQAITD ELFRIENELK
IIK
