GLPX_BACSU
ID GLPX_BACSU Reviewed; 321 AA.
AC Q03224;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=ywjI; OrderedLocusNames=BSU37090;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BD99 / MS119;
RX PubMed=8423140; DOI=10.1128/jb.175.3.647-654.1993;
RA Quirk P.G., Dunkley E.A. Jr., Lee P., Krulwich T.A.;
RT "Identification of a putative Bacillus subtilis rho gene.";
RL J. Bacteriol. 175:647-654(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, ACTIVITY REGULATION,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=19270101; DOI=10.1128/jb.01783-08;
RA Jules M., Le Chat L., Aymerich S., Le Coq D.;
RT "The Bacillus subtilis ywjI (glpX) gene encodes a class II fructose-1,6-
RT bisphosphatase, functionally equivalent to the class III Fbp enzyme.";
RL J. Bacteriol. 191:3168-3171(2009).
CC -!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to
CC fructose 6-phosphate. Can functionally substitute for the FBPase class
CC 3 (Fbp) of B.subtilis. {ECO:0000269|PubMed:19270101}.
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:19270101};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by phosphoenolpyruvate (PEP).
CC {ECO:0000269|PubMed:19270101}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:19270101};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Expressed at the same level under glycolytic or
CC gluconeogenic conditions. {ECO:0000269|PubMed:19270101}.
CC -!- DISRUPTION PHENOTYPE: Disruption of ywjI alone (or fbp alone) does not
CC affect growth on various carbon sources. But the ywjI fbp double mutant
CC is unable to grow with carbon sources demanding FBPase activity, i.e.
CC glycerol, malate, and a mixture of succinate and glutamate.
CC {ECO:0000269|PubMed:19270101}.
CC -!- SIMILARITY: Belongs to the FBPase class 2 family. {ECO:0000305}.
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DR EMBL; M97678; AAA02899.1; -; Unassigned_DNA.
DR EMBL; Z49782; CAA89876.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15726.1; -; Genomic_DNA.
DR PIR; S55429; S55429.
DR RefSeq; NP_391590.1; NC_000964.3.
DR RefSeq; WP_003242962.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; Q03224; -.
DR SMR; Q03224; -.
DR STRING; 224308.BSU37090; -.
DR jPOST; Q03224; -.
DR PaxDb; Q03224; -.
DR PRIDE; Q03224; -.
DR EnsemblBacteria; CAB15726; CAB15726; BSU_37090.
DR GeneID; 937035; -.
DR KEGG; bsu:BSU37090; -.
DR PATRIC; fig|224308.179.peg.4018; -.
DR eggNOG; COG1494; Bacteria.
DR InParanoid; Q03224; -.
DR OMA; AVFYMDK; -.
DR PhylomeDB; Q03224; -.
DR BioCyc; BSUB:BSU37090-MON; -.
DR SABIO-RK; Q03224; -.
DR UniPathway; UPA00138; -.
DR PRO; PR:Q03224; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IMP: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; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..321
FT /note="Fructose-1,6-bisphosphatase class 2"
FT /id="PRO_0000201105"
FT BINDING 33
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 88..90
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164..166
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 186..188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 321 AA; 33951 MW; 418442320FCE7C09 CRC64;
MERSLSMELV RVTEAAALAS ARWMGRGKKD EADEAATSAM RDVFDTVPMK GTVVIGEGEM
DEAPMLYIGE KLGNGYGPRV DVAVDPLEGT NILASGGWNA LTVIAVADHG TLLNAPDMYM
QKIAVGPEAV GCIDIEAPVI DNLKAVAKAK NKDVEDVVAT ILNRERHAKI ISELREAGAR
IKLINDGDVA GAINTAFDHT GVDILFGSGG APEGVLSAVA LKALGGEIIG KLLPQSEEEI
TRCHKMGLDL SKVLRMEDLV KGDDAIFAAT GVTDGELLKG VQFKGSVGTT ESLVIRAKSG
TVRFVDGRHS LKKKPNLVIR P
