PCKG_CORGL
ID PCKG_CORGL Reviewed; 610 AA.
AC Q9AEM1;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Phosphoenolpyruvate carboxykinase [GTP] {ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000303|PubMed:11565516};
DE Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000303|PubMed:11565516};
DE Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000303|PubMed:11565516};
DE EC=4.1.1.32 {ECO:0000255|HAMAP-Rule:MF_00452};
DE AltName: Full=GTP-dependent phosphoenolpyruvate carboxykinase {ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000303|PubMed:18234538};
DE Short=GTP-PEPCK {ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000303|PubMed:18234538};
GN Name=pckG {ECO:0000255|HAMAP-Rule:MF_00452}; Synonyms=pck;
GN OrderedLocusNames=Cgl2863, cg3169;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=11565516;
RA Riedel C., Rittmann D., Dangel P., Mockel B., Petersen S., Sahm H.,
RA Eikmanns B.J.;
RT "Characterization of the phosphoenolpyruvate carboxykinase gene from
RT Corynebacterium glutamicum and significance of the enzyme for growth and
RT amino acid production.";
RL J. Mol. Microbiol. Biotechnol. 3:573-583(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SUBUNIT.
RX PubMed=18234538; DOI=10.1016/j.biocel.2007.12.002;
RA Aich S., Prasad L., Delbaere L.T.J.;
RT "Structure of a GTP-dependent bacterial PEP-carboxykinase from
RT Corynebacterium glutamicum.";
RL Int. J. Biochem. Cell Biol. 40:1597-1603(2008).
CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes the conversion of
CC oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step
CC in the metabolic pathway that produces glucose from lactate and other
CC precursors derived from the citric acid cycle.
CC {ECO:0000269|PubMed:11565516}.
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 ECO:0000269|PubMed:18234538}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00452}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene lead to the absence of
CC PEP carboxykinase activity and the inability to grow on acetate or
CC lactate. {ECO:0000269|PubMed:11565516}.
CC -!- MISCELLANEOUS: The presence and the level of PEP carboxykinase activity
CC has a strong influence on the biosynthesis of glutamate and a weak
CC influence on the biosynthesis of lysine. {ECO:0000269|PubMed:11565516}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC family. {ECO:0000255|HAMAP-Rule:MF_00452}.
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DR EMBL; AJ269506; CAC36295.1; -; Genomic_DNA.
DR EMBL; BA000036; BAC00257.1; -; Genomic_DNA.
DR EMBL; BX927156; CAF20888.1; -; Genomic_DNA.
DR RefSeq; NP_602055.1; NC_003450.3.
DR RefSeq; WP_011015446.1; NC_006958.1.
DR PDB; 2ZCI; X-ray; 2.30 A; A/B/C/D=1-610.
DR PDBsum; 2ZCI; -.
DR AlphaFoldDB; Q9AEM1; -.
DR SMR; Q9AEM1; -.
DR STRING; 196627.cg3169; -.
DR KEGG; cgb:cg3169; -.
DR KEGG; cgl:Cgl2863; -.
DR PATRIC; fig|196627.13.peg.2795; -.
DR eggNOG; COG1274; Bacteria.
DR HOGENOM; CLU_028872_1_1_11; -.
DR OMA; GPTNNWV; -.
DR BRENDA; 4.1.1.32; 960.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; Q9AEM1; -.
DR Proteomes; UP000000582; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Decarboxylase; Gluconeogenesis; GTP-binding;
KW Lyase; Manganese; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..610
FT /note="Phosphoenolpyruvate carboxykinase [GTP]"
FT /id="PRO_0000103603"
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"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:2ZCI"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2ZCI"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:2ZCI"
FT TURN 118..123
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 124..134
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:2ZCI"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:2ZCI"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 274..280
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 305..311
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:2ZCI"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 330..336
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 402..405
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 427..430
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 434..442
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:2ZCI"
FT TURN 468..470
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 475..489
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 495..499
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 518..530
FT /evidence="ECO:0007829|PDB:2ZCI"
FT STRAND 539..543
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 546..548
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 561..565
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 569..574
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 576..585
FT /evidence="ECO:0007829|PDB:2ZCI"
FT HELIX 592..605
FT /evidence="ECO:0007829|PDB:2ZCI"
SQ SEQUENCE 610 AA; 66874 MW; 45C97817F49744E0 CRC64;
MTTAAIRGLQ GEAPTKNKEL LNWIADAVEL FQPEAVVFVD GSQAEWDRMA EDLVEAGTLI
KLNEEKRPNS YLARSNPSDV ARVESRTFIC SEKEEDAGPT NNWAPPQAMK DEMSKHYAGS
MKGRTMYVVP FCMGPISDPD PKLGVQLTDS EYVVMSMRIM TRMGIEALDK IGANGSFVRC
LHSVGAPLEP GQEDVAWPCN DTKYITQFPE TKEIWSYGSG YGGNAILAKK CYALRIASVM
AREEGWMAEH MLILKLINPE GKAYHIAAAF PSACGKTNLA MITPTIPGWT AQVVGDDIAW
LKLREDGLYA VNPENGFFGV APGTNYASNP IAMKTMEPGN TLFTNVALTD DGDIWWEGMD
GDAPAHLIDW MGNDWTPESD ENAAHPNSRY CVAIDQSPAA APEFNDWEGV KIDAILFGGR
RADTVPLVTQ TYDWEHGTMV GALLASGQTA ASAEAKVGTL RHDPMAMLPF IGYNAGEYLQ
NWIDMGNKGG DKMPSIFLVN WFRRGEDGRF LWPGFGDNSR VLKWVIDRIE GHVGADETVV
GHTAKAEDLD LDGLDTPIED VKEALTAPAE QWANDVEDNA EYLTFLGPRV PAEVHSQFDA
LKARISAAHA
