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GLPX_MYCLE
ID   GLPX_MYCLE              Reviewed;         355 AA.
AC   Q9CBH9;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   03-AUG-2022, entry version 91.
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=ML1946;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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=CAC30901.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL583923; CAC30901.1; ALT_INIT; Genomic_DNA.
DR   PIR; E87152; E87152.
DR   AlphaFoldDB; Q9CBH9; -.
DR   SMR; Q9CBH9; -.
DR   STRING; 272631.ML1946; -.
DR   EnsemblBacteria; CAC30901; CAC30901; CAC30901.
DR   KEGG; mle:ML1946; -.
DR   Leproma; ML1946; -.
DR   eggNOG; COG1494; Bacteria.
DR   HOGENOM; CLU_054938_0_0_11; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000806; 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   Carbohydrate metabolism; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..355
FT                   /note="Fructose-1,6-bisphosphatase class 2"
FT                   /id="PRO_0000403678"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         54
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         109..111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         186..188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         208..210
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         235
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   355 AA;  37431 MW;  4A0AA01C2C6F4A82 CRC64;
     MTAEGDGSFK PGPPTERRGE APDRNLAMEL VRVTEAGAMA AGRWVGRGNK EGGDGAAVDT
     IRELVNTVSM RGVVVIGEGE KDHAPMLYNG EEVGNGDGPD CDFAVDPIDG TTLMSKGMPN
     AISVLAVADR GAMFDPSAVF YMNKITVGPD AAHVLDITAP IGENIRAVAK VKDLSVRDMT
     VCILDRPRHA QLIDDVRATG ARIRLITDGD VAGAISACRP QSGTDMLAGI GGTPEGIIAA
     AAIRCMGGAI QAQLAPRDDV ERRKALDAGY NLDRILTTED LVSGENVFFC ATGVTDGDLL
     KGVRYYAGGC TTQSIVMRSK SGTVRMIEAY HRLSKLNEYS AIDFTGDNNA AYPLP
 
 
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