PCKG_FRAAA
ID PCKG_FRAAA Reviewed; 607 AA.
AC Q0RCJ7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=FRAAL6204;
OS Frankia alni (strain ACN14a).
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACN14a;
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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; CT573213; CAJ64827.1; -; Genomic_DNA.
DR RefSeq; WP_011607254.1; NC_008278.1.
DR AlphaFoldDB; Q0RCJ7; -.
DR SMR; Q0RCJ7; -.
DR STRING; 326424.FRAAL6204; -.
DR KEGG; fal:FRAAL6204; -.
DR eggNOG; COG1274; Bacteria.
DR HOGENOM; CLU_028872_1_1_11; -.
DR OMA; GPTNNWV; -.
DR OrthoDB; 267285at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000657; 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_1000060289"
FT ACT_SITE 274
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 82
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 387..389
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 389
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 420
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 515..518
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
SQ SEQUENCE 607 AA; 66582 MW; 01D266786EDFF796 CRC64;
MTTAAQIPGL EAAPTKHARL VAWVREIAEL TQPERVEWCD GSEAEFDRLT SLLIEKGTLV
RLNDEKRPNS FYAASDPSDV ARVEDRTYIC SEKAEDAGPT NNWMDPAEMR VKLQGLFEGS
MRGRTMYVVP FCMGPLGSHI SALGVEITDS PYVVISMRTM TRMGAPALEQ LGEDGFFVPA
VHSLGAPLES GAADVPWPCN TTKYITHFPE TREIWSYGSG YGGNALLGKK CYALRIASVM
ARDEGWLAEH MLILKLTSPA GKVHYIAAAF PSACGKTNLA MLIPTLPGWK AETVGDDIAW
MRFGEDGRLY AVNPEAGFFG VAPGTGEQTN PNAIKTLWGN TVFTNVARTD DGDVWWEGLT
KQAPGHLTDW KGRDWTPEST EPAAHPNARF TVPAGQCPTI ASEWQDPKGV PISAILFGGR
RATAVPLVTE APDWRRGVFF GSIVASETTA AQAGAIGKLR RDPFAMLPFC GYNMADYFAH
WLEVGQKADQ AKLPRIYYVN WFRKSPEGKF LWPGFGENSR VLAWIVGRLE GHADGVETPL
GVLPTRDALP TDGLQIDEAD LDALLTVDID VWKQEAELIP EHYQTFGDRL PAALWAEHEA
LVSRLDG
