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BSUHB_METJA
ID   BSUHB_METJA             Reviewed;         252 AA.
AC   Q57573;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Fructose-1,6-bisphosphatase/inositol-1-monophosphatase;
DE            Short=FBPase/IMPase;
DE            EC=3.1.3.11 {ECO:0000269|PubMed:9647837};
DE            EC=3.1.3.25 {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:9647837};
DE   AltName: Full=Inositol-1-phosphatase;
DE            Short=I-1-Pase;
GN   Name=suhB; OrderedLocusNames=MJ0109;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   FUNCTION AS IMPASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND ACTIVITY REGULATION.
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=9647837; DOI=10.1128/aem.64.7.2609-2615.1998;
RA   Chen L., Roberts M.F.;
RT   "Cloning and expression of the inositol monophosphatase gene from
RT   Methanococcus jannaschii and characterization of the enzyme.";
RL   Appl. Environ. Microbiol. 64:2609-2615(1998).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PHOSPHATE AND METAL
RP   IONS, FUNCTION AS BOTH FBPASE AND IMPASE, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, AND KINETIC PARAMETERS.
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=11062561; DOI=10.1038/80968;
RA   Stec B., Yang H., Johnson K.A., Chen L., Roberts M.F.;
RT   "MJ0109 is an enzyme that is both an inositol monophosphatase and the
RT   'missing' archaeal fructose-1,6-bisphosphatase.";
RL   Nat. Struct. Biol. 7:1046-1050(2000).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH MYO-INOSITOL
RP   PHOSPHATE; MYO-INOSITOL AND METAL IONS.
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=11170378; DOI=10.1021/bi0016422;
RA   Johnson K.A., Chen L., Yang H., Roberts M.F., Stec B.;
RT   "Crystal structure and catalytic mechanism of the MJ0109 gene product: a
RT   bifunctional enzyme with inositol monophosphatase and fructose 1,6-
RT   bisphosphatase activities.";
RL   Biochemistry 40:618-630(2001).
CC   -!- FUNCTION: Phosphatase with broad specificity; it can dephosphorylate
CC       fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate
CC       (I-1-P), 2'-AMP, pNPP, beta-glycerol phosphate, and alpha-D-glucose-1-
CC       phosphate. Cannot hydrolyze glucose-6-phosphate, fructose-6-phosphate,
CC       NAD(+) or 5'-AMP. May be involved in the biosynthesis of a unique
CC       osmolyte, di-myo-inositol 1,1-phosphate. {ECO:0000269|PubMed:11062561,
CC       ECO:0000269|PubMed:9647837}.
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:11062561};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC         Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC         Evidence={ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:9647837};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:9647837};
CC   -!- ACTIVITY REGULATION: IMPase activity is inhibited by Ca(2+) and Zn(2+).
CC       In contrast to mammalian I-1-P phosphatases, is not inhibited by Li(+)
CC       up to 100 mM. {ECO:0000269|PubMed:9647837}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.091 mM for inositol-1-phosphate (at 85 degrees Celsius)
CC         {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:9647837};
CC         KM=0.038 mM for D-fructose 1,6-bisphosphate (at 85 degrees Celsius)
CC         {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:9647837};
CC         Vmax=9.3 umol/min/mg enzyme for IMPase activity (at 85 degrees
CC         Celsius) {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:9647837};
CC         Note=kcat is 4.2 sec(-1) for IMPase activity (at 85 degrees Celsius)
CC         and 7.0 sec(-1) for FBPase activity (at 85 degrees Celsius).;
CC       Temperature dependence:
CC         Is thermostable. After incubation at 85 degrees Celsius for 30
CC         minutes, more than 95% of I-1-Pase activity remains.
CC         {ECO:0000269|PubMed:9647837};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11062561,
CC       ECO:0000269|PubMed:9647837}.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily. FBPase
CC       class 4 family. {ECO:0000305}.
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DR   EMBL; L77117; AAB98091.1; -; Genomic_DNA.
DR   PIR; E64313; E64313.
DR   RefSeq; WP_010869601.1; NC_000909.1.
DR   PDB; 1DK4; X-ray; 2.60 A; A/B=1-252.
DR   PDB; 1G0H; X-ray; 2.30 A; A/B=1-252.
DR   PDB; 1G0I; X-ray; 2.40 A; A/B=1-252.
DR   PDBsum; 1DK4; -.
DR   PDBsum; 1G0H; -.
DR   PDBsum; 1G0I; -.
DR   AlphaFoldDB; Q57573; -.
DR   SMR; Q57573; -.
DR   STRING; 243232.MJ_0109; -.
DR   EnsemblBacteria; AAB98091; AAB98091; MJ_0109.
DR   GeneID; 1450950; -.
DR   KEGG; mja:MJ_0109; -.
DR   eggNOG; arCOG01349; Archaea.
DR   HOGENOM; CLU_044118_5_0_2; -.
DR   InParanoid; Q57573; -.
DR   OMA; RWGDERY; -.
DR   OrthoDB; 99063at2157; -.
DR   PhylomeDB; Q57573; -.
DR   BioCyc; MetaCyc:MON-5062; -.
DR   BRENDA; 3.1.3.108; 3260.
DR   BRENDA; 3.1.3.11; 3260.
DR   BRENDA; 3.1.3.25; 3260.
DR   SABIO-RK; Q57573; -.
DR   EvolutionaryTrace; Q57573; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR   GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   PROSITE; PS00629; IMP_1; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..252
FT                   /note="Fructose-1,6-bisphosphatase/inositol-1-
FT                   monophosphatase"
FT                   /id="PRO_0000142580"
FT   BINDING         65
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305|PubMed:11062561,
FT                   ECO:0000305|PubMed:11170378"
FT   BINDING         81
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305|PubMed:11062561,
FT                   ECO:0000305|PubMed:11170378"
FT   BINDING         81
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305|PubMed:11062561,
FT                   ECO:0000305|PubMed:11170378"
FT   BINDING         83
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305|PubMed:11062561,
FT                   ECO:0000305|PubMed:11170378"
FT   BINDING         84..86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11170378"
FT   BINDING         84
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305|PubMed:11062561,
FT                   ECO:0000305|PubMed:11170378"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11170378"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11170378"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11170378"
FT   BINDING         201
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305|PubMed:11062561,
FT                   ECO:0000305|PubMed:11170378"
FT   HELIX           3..18
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   HELIX           19..21
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   TURN            25..27
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   STRAND          30..34
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   TURN            35..37
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   STRAND          38..41
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   HELIX           42..55
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   HELIX           56..58
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   STRAND          60..64
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   HELIX           65..67
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   STRAND          75..84
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   HELIX           86..90
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   STRAND          97..115
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   HELIX           116..118
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   STRAND          120..125
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   TURN            126..128
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   STRAND          129..132
FT                   /evidence="ECO:0007829|PDB:1G0I"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:1G0I"
FT   STRAND          148..152
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:1DK4"
FT   HELIX           159..165
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   STRAND          167..169
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   HELIX           175..183
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   STRAND          188..192
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   HELIX           199..210
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   TURN            211..213
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   STRAND          215..217
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   STRAND          219..223
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   STRAND          237..241
FT                   /evidence="ECO:0007829|PDB:1G0H"
FT   HELIX           242..249
FT                   /evidence="ECO:0007829|PDB:1G0H"
SQ   SEQUENCE   252 AA;  28578 MW;  3ED5B4401075EE6E CRC64;
     MKWDEIGKNI AKEIEKEILP YFGRKDKSYV VGTSPSGDET EIFDKISEDI ALKYLKSLNV
     NIVSEELGVI DNSSEWTVVI DPIDGSFNFI NGIPFFAFCF GVFKNNEPYY GLTYEFLTKS
     FYEAYKGKGA YLNGRKIKVK DFNPNNIVIS YYPSKKIDLE KLRNKVKRVR IFGAFGLEMC
     YVAKGTLDAV FDVRPKVRAV DIASSYIICK EAGALITDEN GDELKFDLNA TDRLNIIVAN
     SKEMLDIILD LL
 
 
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