ID   GLPX_MYCTF              Reviewed;         362 AA.
AC   A5WLC4;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   03-AUG-2022, entry version 68.
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; OrderedLocusNames=TBFG_11120;
OS   Mycobacterium tuberculosis (strain F11).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=336982;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F11;
RA   Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA   Grabherr M., Mauceli E., Brockman W., Young S., LaButti K., Pushparaj V.,
RA   Sykes S., Baldwin J., Fitzgerald M., Bloom T., Zimmer A., Settipalli S.,
RA   Shea T., Arachchi H., Macdonald P., Abouelleil A., Lui A., Priest M.,
RA   Berlin A., Gearin G., Brown A., Aftuck L., Bessette D., Allen N.,
RA   Lubonja R., Lokyitsang T., Matthews C., Dunbar C., Benamara M., Nguyen T.,
RA   Negash T., DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P.,
RA   Pearson M., Howarth C., Kodira C., Zeng Q., Yandava C., O'Leary S.,
RA   Alvarado L., Victor T., Murray M.;
RT   "The complete genome sequence of Mycobacterium tuberculosis F11.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to
CC       fructose 6-phosphate. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FBPase class 2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABR05463.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000717; ABR05463.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_003898726.1; NZ_KK339377.1.
DR   AlphaFoldDB; A5WLC4; -.
DR   SMR; A5WLC4; -.
DR   GeneID; 45425073; -.
DR   KEGG; mtf:TBFG_11120; -.
DR   PATRIC; fig|336982.11.peg.1232; -.
DR   HOGENOM; CLU_054938_0_0_11; -.
DR   OMA; AVFYMDK; -.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Hydrolase; Manganese; Metal-binding.
FT   CHAIN           1..362
FT                   /note="Fructose-1,6-bisphosphatase class 2"
FT                   /id="PRO_0000403680"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         61
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="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         116..118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         193..195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         215..217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   362 AA;  38084 MW;  113D5BA2742F06E9 CRC64;
     MTAEGSGSST AAVASHDPSH TRPSRREAPD RNLAMELVRV TEAGAMAAGR WVGRGDKEGG
     DGAAVDAMRE LVNSVSMRGV VVIGEGEKDH APMLYNGEEV GNGDGPECDF AVDPIDGTTL
     MSKGMTNAIS VLAVADRGTM FDPSAVFYMN KIAVGPDAAH VLDITAPISE NIRAVAKVKD
     LSVRDMTVCI LDRPRHAQLI HDVRATGARI RLITDGDVAG AISACRPHSG TDLLAGIGGT
     PEGIIAAAAI RCMGGAIQAQ LAPRDDAERR KALEAGYDLN QVLTTEDLVS GENVFFCATG
     VTDGDLLKGV RYYPGGCTTH SIVMRSKSGT VRMIEAYHRL SKLNEYSAID FTGDSSAVYP
     LP