GLPX_CORGL
ID GLPX_CORGL Reviewed; 335 AA.
AC Q6M6E7; Q8NRM9;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Fructose-1,6-bisphosphatase class 2;
DE Short=FBPase class 2;
DE EC=3.1.3.11;
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 2;
GN Name=glpX; Synonyms=fbp; OrderedLocusNames=Cgl1019, cg1157;
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 [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 [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=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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, DETERMINATION OF TRANSLATIONAL START
RP SITE, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12904832; DOI=10.1007/s00203-003-0588-6;
RA Rittmann D., Schaffer S., Wendisch V.F., Sahm H.;
RT "Fructose-1,6-bisphosphatase from Corynebacterium glutamicum: expression
RT and deletion of the fbp gene and biochemical characterization of the
RT enzyme.";
RL Arch. Microbiol. 180:285-292(2003).
CC -!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to
CC fructose 6-phosphate. Is essential for growth on gluconeogenic carbon
CC sources. Also displays a low activity toward glucose 6-phosphate, and
CC fructose 6-phosphate, glycerol 3-phosphate, ribulose 1,5-bisphosphate
CC and myo-inositol-monophosphate are not significant substrates.
CC {ECO:0000269|PubMed:12904832}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC Evidence={ECO:0000269|PubMed:12904832};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12904832};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12904832};
CC Note=Manganese. Mn(2+) can be replaced by Mg(2+).
CC {ECO:0000269|PubMed:12904832};
CC -!- ACTIVITY REGULATION: Inhibited by the monovalent cation Li(+) with an
CC inhibition constant of 140 uM. Also inhibited by AMP and
CC phosphoenolpyruvate and to a lesser extent by phosphate, fructose 6-
CC phosphate, fructose 2,6-bisphosphate, and UDP. ATP and ADP have no
CC significant effects on FBPase activity. {ECO:0000269|PubMed:12904832}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:12904832};
CC Vmax=5.4 umol/min/mg enzyme {ECO:0000269|PubMed:12904832};
CC pH dependence:
CC Optimum pH is 7.7. {ECO:0000269|PubMed:12904832};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12904832}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: The FBPase protein levels during growth on glucose,
CC gluconate, ribose, pyruvate, lacatate, or citrate do not vary much
CC (inferior or equal to two-fold) with respect to the carbon source.
CC {ECO:0000269|PubMed:12904832}.
CC -!- DISRUPTION PHENOTYPE: Strains lacking this gene are unable to grow on
CC the carbon sources acetate, citrate, glutamate, and lactate and display
CC no detectable fructose-1,6-bisphosphatase activity.
CC {ECO:0000269|PubMed:12904832}.
CC -!- SIMILARITY: Belongs to the FBPase class 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB98412.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000036; BAB98412.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX927151; CAF19721.1; -; Genomic_DNA.
DR RefSeq; NP_600242.1; NC_003450.3.
DR RefSeq; WP_003856830.1; NC_006958.1.
DR AlphaFoldDB; Q6M6E7; -.
DR SMR; Q6M6E7; -.
DR STRING; 196627.cg1157; -.
DR World-2DPAGE; 0001:Q6M6E7; -.
DR PRIDE; Q6M6E7; -.
DR GeneID; 58310132; -.
DR KEGG; cgb:cg1157; -.
DR KEGG; cgl:Cgl1019; -.
DR PATRIC; fig|196627.13.peg.997; -.
DR eggNOG; COG1494; Bacteria.
DR HOGENOM; CLU_054938_0_0_11; -.
DR SABIO-RK; Q6M6E7; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; IMP:UniProtKB.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR CDD; cd01516; FBPase_glpX; 1.
DR InterPro; IPR004464; FBPase_class-2/SBPase.
DR PANTHER; PTHR30447; PTHR30447; 1.
DR Pfam; PF03320; FBPase_glpX; 1.
DR PIRSF; PIRSF004532; GlpX; 1.
DR TIGRFAMs; TIGR00330; glpX; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Reference proteome.
FT CHAIN 1..335
FT /note="Fructose-1,6-bisphosphatase class 2"
FT /id="PRO_0000403985"
FT BINDING 41
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 96..98
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 173..175
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 195..197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 335 AA; 35369 MW; 005CC5B67F3D54AB CRC64;
MNLKNPETPD RNLAMELVRV TEAAALASGR WVGRGMKNEG DGAAVDAMRQ LINSVTMKGV
VVIGEGEKDE APMLYNGEEV GTGFGPEVDI AVDPVDGTTL MAEGRPNAIS ILAAAERGTM
YDPSSVFYMK KIAVGPEAAG KIDIEAPVAH NINAVAKSKG INPSDVTVVV LDRPRHIELI
ADIRRAGAKV RLISDGDVAG AVAAAQDSNS VDIMMGTGGT PEGIITACAM KCMGGEIQGI
LAPMNDFERQ KAHDAGLVLD QVLHTNDLVS SDNCYFVATG VTNGDMLRGV SYRANGATTR
SLVMRAKSGT IRHIESVHQL SKLQEYSVVD YTTAT
