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F16A1_PARXL
ID   F16A1_PARXL             Reviewed;         338 AA.
AC   Q13V64;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Fructose-1,6-bisphosphatase class 1 1 {ECO:0000255|HAMAP-Rule:MF_01855};
DE            Short=FBPase class 1 1 {ECO:0000255|HAMAP-Rule:MF_01855};
DE            EC=3.1.3.11 {ECO:0000255|HAMAP-Rule:MF_01855};
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 1 {ECO:0000255|HAMAP-Rule:MF_01855};
GN   Name=fbp1 {ECO:0000255|HAMAP-Rule:MF_01855}; OrderedLocusNames=Bxeno_A3487;
GN   ORFNames=Bxe_A0920;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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:0000255|HAMAP-Rule:MF_01855};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01855};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01855};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01855}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01855}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01855}.
CC   -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01855}.
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DR   EMBL; CP000270; ABE32025.1; -; Genomic_DNA.
DR   RefSeq; WP_007180818.1; NZ_CP008760.1.
DR   AlphaFoldDB; Q13V64; -.
DR   SMR; Q13V64; -.
DR   STRING; 266265.Bxe_A0920; -.
DR   EnsemblBacteria; ABE32025; ABE32025; Bxe_A0920.
DR   KEGG; bxb:DR64_3083; -.
DR   KEGG; bxe:Bxe_A0920; -.
DR   eggNOG; COG0158; Bacteria.
DR   OMA; YIPENCP; -.
DR   OrthoDB; 945770at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   CDD; cd00354; FBPase; 1.
DR   HAMAP; MF_01855; FBPase_class1; 1.
DR   InterPro; IPR044015; FBPase_C_dom.
DR   InterPro; IPR000146; FBPase_class-1.
DR   InterPro; IPR033391; FBPase_N.
DR   InterPro; IPR028343; FBPtase.
DR   PANTHER; PTHR11556; PTHR11556; 1.
DR   Pfam; PF00316; FBPase; 1.
DR   Pfam; PF18913; FBPase_C; 1.
DR   PIRSF; PIRSF500210; FBPtase; 1.
DR   PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR   PRINTS; PR00115; F16BPHPHTASE.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..338
FT                   /note="Fructose-1,6-bisphosphatase class 1 1"
FT                   /id="PRO_0000364506"
FT   BINDING         94
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         119..122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         119
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         210
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         282
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
SQ   SEQUENCE   338 AA;  37622 MW;  60E172A370B1D6FD CRC64;
     MALQRRTTLT KYLIEQQRET NNLPADLRLL IEVVARACKA ISYHVSKGAL GDALGTAGSE
     NVQGEVQKKL DILSNEILLE ANEWGGNLAG MASEEMEQFF PIPANYPKGE YLLVFDPLDG
     SSNIDVNVSI GTIFSVLRCP DGQQPTEQSF LQPGTQQVAA GYAVYGPQTV LVLTTGNGVN
     CFTLDRELGS WVLTQSDMRI PVETREYAIN ASNERHWYPP VQQYIGELKD GKEGSRQSDF
     NMRWIASMVA DVHRILNRGG IFMYPADKRT PDKPGKLRLM YEANPMAFIV EQAGGAATNG
     EKRILDIQPK SLHERVAVFL GSKNEVDRVT RYHLETKK
 
 
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