GLPX_MYCTO
ID GLPX_MYCTO Reviewed; 362 AA.
AC P9WN20; L0T8L8; O53447; Q7D8U9;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
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=MT1131;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to
CC fructose 6-phosphate. Seems to be the major FBPase of M.tuberculosis
CC and to play a key role in gluconeogenesis for conversion of lipid
CC carbon into cell wall glycans. Does not display activity against
CC inositol 1-phosphate (By similarity). {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=AAK45389.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK45389.1; ALT_INIT; Genomic_DNA.
DR PIR; A70897; A70897.
DR RefSeq; WP_003898726.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WN20; -.
DR SMR; P9WN20; -.
DR EnsemblBacteria; AAK45389; AAK45389; MT1131.
DR GeneID; 45425073; -.
DR KEGG; mtc:MT1131; -.
DR PATRIC; fig|83331.31.peg.1221; -.
DR HOGENOM; CLU_054938_0_0_11; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001020; Chromosome.
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 Acetylation; Carbohydrate metabolism; Cytoplasm; Hydrolase; Manganese;
KW Metal-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..362
FT /note="Fructose-1,6-bisphosphatase class 2"
FT /id="PRO_0000427203"
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"
FT MOD_RES 2
FT /note="N-acetylthreonine; partial"
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
