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5NT3B_DROME
ID   5NT3B_DROME             Reviewed;         319 AA.
AC   Q9W197;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=7-methylguanosine phosphate-specific 5'-nucleotidase;
DE            Short=7-methylguanosine nucleotidase;
DE            EC=3.1.3.91 {ECO:0000269|PubMed:23223233, ECO:0000269|PubMed:24603684};
DE   AltName: Full=Cytosolic 5'-nucleotidase IIIB {ECO:0000312|FlyBase:FBgn0034988};
DE            EC=3.1.3.5 {ECO:0000269|PubMed:23223233, ECO:0000269|PubMed:24603684};
DE   AltName: Full=N(7)-methylguanylate 5'-phosphatase;
GN   Name=cN-IIIB {ECO:0000312|FlyBase:FBgn0034988};
GN   ORFNames=CG3362 {ECO:0000312|FlyBase:FBgn0034988};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, AND SUBUNIT.
RX   PubMed=23223233; DOI=10.1074/jbc.m112.426700;
RA   Buschmann J., Moritz B., Jeske M., Lilie H., Schierhorn A., Wahle E.;
RT   "Identification of Drosophila and Human 7-Methyl GMP-specific
RT   Nucleotidases.";
RL   J. Biol. Chem. 288:2441-2451(2013).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH REACTION PRODUCTS,
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP   ACTIVE SITE, METAL BINDING, AND MUTAGENESIS OF PHE-75; GLY-76; TRP-121 AND
RP   75-PHE--GLY-76.
RX   PubMed=24603684; DOI=10.1371/journal.pone.0090915;
RA   Monecke T., Buschmann J., Neumann P., Wahle E., Ficner R.;
RT   "Crystal structures of the novel cytosolic 5'-nucleotidase IIIB explain its
RT   preference for m7GMP.";
RL   PLoS ONE 9:90915-90915(2014).
CC   -!- FUNCTION: Specifically hydrolyzes 7-methylguanosine monophosphate
CC       (m(7)GMP) to 7-methylguanosine and inorganic phosphate
CC       (PubMed:23223233, PubMed:24603684). Also able to mediate hydrolysis of
CC       diphosphate (m(7)GDP) to 7-methylguanosine and 2 inorganic phosphate
CC       with lower activity (PubMed:23223233). The specific activity for
CC       m(7)GMP may protect cells against undesired salvage of m(7)GMP and its
CC       incorporation into nucleic acids (PubMed:23223233). Also has weak
CC       activity for CMP (PubMed:23223233, PubMed:24603684). UMP and purine
CC       nucleotides are poor substrates (PubMed:23223233, PubMed:24603684).
CC       {ECO:0000269|PubMed:23223233, ECO:0000269|PubMed:24603684}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(7)-methyl-GMP = N(7)-methylguanosine + phosphate;
CC         Xref=Rhea:RHEA:37107, ChEBI:CHEBI:15377, ChEBI:CHEBI:20794,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58285; EC=3.1.3.91;
CC         Evidence={ECO:0000269|PubMed:23223233, ECO:0000269|PubMed:24603684};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CMP + H2O = cytidine + phosphate; Xref=Rhea:RHEA:29367,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17562, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:60377; EC=3.1.3.91;
CC         Evidence={ECO:0000269|PubMed:23223233, ECO:0000269|PubMed:24603684};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC         phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC         Evidence={ECO:0000269|PubMed:23223233, ECO:0000269|PubMed:24603684};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:24603684};
CC   -!- ACTIVITY REGULATION: Inhibited by high levels of AMP.
CC       {ECO:0000269|PubMed:23223233}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=13 uM for m(7)GMP (at 25 degrees Celsius)
CC         {ECO:0000269|PubMed:23223233};
CC         KM=12 uM for m(7)GMP (at 25 degrees Celsius)
CC         {ECO:0000269|PubMed:24603684};
CC         KM=48 uM for CMP (at 25 degrees Celsius)
CC         {ECO:0000269|PubMed:23223233, ECO:0000269|PubMed:24603684};
CC         KM=102 uM for GMP (at 25 degrees Celsius)
CC         {ECO:0000269|PubMed:23223233};
CC         KM=32 uM for AMP (at 25 degrees Celsius)
CC         {ECO:0000269|PubMed:23223233};
CC         KM=91 uM for UMP (at 25 degrees Celsius)
CC         {ECO:0000269|PubMed:23223233};
CC         Vmax=11 umol/min/mg enzyme with m(7)GMP as substrate
CC         {ECO:0000269|PubMed:23223233};
CC         Vmax=21 umol/min/mg enzyme with CMP as substrate
CC         {ECO:0000269|PubMed:23223233};
CC         Vmax=1.5 umol/min/mg enzyme with GMP as substrate
CC         {ECO:0000269|PubMed:23223233};
CC         Vmax=0.49 umol/min/mg enzyme with AMP as substrate
CC         {ECO:0000269|PubMed:23223233};
CC         Vmax=4.0 umol/min/mg enzyme with UMP as substrate
CC         {ECO:0000269|PubMed:23223233};
CC         Note=kcat is 6.3 sec(-1) with m(7)GMP. kcat is 12 sec(-1) with CMP.
CC         kcat is 0.88 sec(-1) with GMP. kcat is 0.28 sec(-1) with AMP. kcat is
CC         2.3 sec(-1) with UMP.;
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:23223233};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23223233}.
CC   -!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family.
CC       {ECO:0000305}.
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DR   EMBL; AE013599; AAF47180.1; -; Genomic_DNA.
DR   EMBL; AY061358; AAL28906.1; -; mRNA.
DR   RefSeq; NP_611895.1; NM_138051.4.
DR   PDB; 4NV0; X-ray; 1.65 A; A/B=1-319.
DR   PDB; 4NWI; X-ray; 2.05 A; A/B=1-319.
DR   PDBsum; 4NV0; -.
DR   PDBsum; 4NWI; -.
DR   AlphaFoldDB; Q9W197; -.
DR   SMR; Q9W197; -.
DR   IntAct; Q9W197; 1.
DR   STRING; 7227.FBpp0072168; -.
DR   PaxDb; Q9W197; -.
DR   PRIDE; Q9W197; -.
DR   DNASU; 37875; -.
DR   EnsemblMetazoa; FBtr0072261; FBpp0072168; FBgn0034988.
DR   GeneID; 37875; -.
DR   KEGG; dme:Dmel_CG3362; -.
DR   UCSC; CG3362-RA; d. melanogaster.
DR   CTD; 37875; -.
DR   FlyBase; FBgn0034988; cN-IIIB.
DR   VEuPathDB; VectorBase:FBgn0034988; -.
DR   eggNOG; KOG3128; Eukaryota.
DR   GeneTree; ENSGT00390000012959; -.
DR   HOGENOM; CLU_048584_0_2_1; -.
DR   InParanoid; Q9W197; -.
DR   OMA; GPERMQI; -.
DR   OrthoDB; 1171042at2759; -.
DR   PhylomeDB; Q9W197; -.
DR   BRENDA; 3.1.3.91; 1994.
DR   Reactome; R-DME-429958; mRNA decay by 3' to 5' exoribonuclease.
DR   Reactome; R-DME-73621; Pyrimidine catabolism.
DR   SABIO-RK; Q9W197; -.
DR   BioGRID-ORCS; 37875; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 37875; -.
DR   PRO; PR:Q9W197; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0034988; Expressed in adult midgut (Drosophila) and 25 other tissues.
DR   Genevisible; Q9W197; DM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR   GO; GO:0008253; F:5'-nucleotidase activity; IDA:FlyBase.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008252; F:nucleotidase activity; IDA:FlyBase.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IDA:FlyBase.
DR   GO; GO:1901069; P:guanosine-containing compound catabolic process; IDA:FlyBase.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009158; P:ribonucleoside monophosphate catabolic process; IDA:FlyBase.
DR   CDD; cd07504; HAD_5NT; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006434; Pyrimidine_nucleotidase_eu.
DR   Pfam; PF05822; UMPH-1; 1.
DR   SFLD; SFLDG01128; C1.4:_5'-Nucleotidase_Like; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01544; HAD-SF-IE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..319
FT                   /note="7-methylguanosine phosphate-specific 5'-
FT                   nucleotidase"
FT                   /id="PRO_0000421994"
FT   ACT_SITE        55
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:24603684"
FT   ACT_SITE        57
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000269|PubMed:24603684"
FT   BINDING         55
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:24603684"
FT   BINDING         57
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:24603684"
FT   BINDING         103
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000269|PubMed:24603684"
FT   BINDING         103
FT                   /ligand="N(7)-methyl-GMP"
FT                   /ligand_id="ChEBI:CHEBI:58285"
FT                   /evidence="ECO:0000269|PubMed:24603684"
FT   BINDING         124
FT                   /ligand="N(7)-methyl-GMP"
FT                   /ligand_id="ChEBI:CHEBI:58285"
FT                   /evidence="ECO:0000269|PubMed:24603684"
FT   BINDING         171..172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0P0"
FT   BINDING         245
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:24603684"
FT   MUTAGEN         75..76
FT                   /note="FG->HN: Increases KM 7-fold for CMP; when associated
FT                   with TRP-121."
FT                   /evidence="ECO:0000269|PubMed:24603684"
FT   MUTAGEN         75
FT                   /note="F->H: Increases KM 3-fold for m(7)GMP and increases
FT                   KM 10-fold for CMP. Decreases KM 6-fold for m(7)GMP and
FT                   increases KM 2-fold for CMP; when associated with TRP-121."
FT                   /evidence="ECO:0000269|PubMed:24603684"
FT   MUTAGEN         76
FT                   /note="G->N: Decreases KM 6-fold for m(7)GMP. Decreases KM
FT                   1.5-fold for m(7)GMP and increases KM 1.5-fold for CMP;
FT                   when associated with TRP-121."
FT                   /evidence="ECO:0000269|PubMed:24603684"
FT   MUTAGEN         121
FT                   /note="W->Y: Considerable increase (12-fold) in KM for
FT                   m(7)GMP and decreases KM 3-fold for CMP. Decreases KM 6-
FT                   fold for m(7)GMP and increases KM 2-fold for CMP; when
FT                   associated with HIS-75. Decreases KM 1.5-fold for m(7)GMP
FT                   and increases KM 1.5-fold for CMP; when associated with
FT                   ASN-76. Increases KM 7-fold for CMP; when associated with
FT                   75-HIS--ASN-76."
FT   HELIX           16..18
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   HELIX           20..23
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   HELIX           32..45
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   HELIX           47..49
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   STRAND          50..54
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   TURN            57..59
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:4NWI"
FT   HELIX           74..79
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   STRAND          82..84
FT                   /evidence="ECO:0007829|PDB:4NWI"
FT   HELIX           88..103
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   STRAND          106..108
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   HELIX           110..127
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   STRAND          128..131
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   HELIX           135..142
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   HELIX           143..148
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   HELIX           153..163
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   STRAND          167..174
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   HELIX           175..184
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   STRAND          192..197
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   STRAND          199..202
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   STRAND          205..209
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   TURN            221..223
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   HELIX           231..234
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   STRAND          239..246
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   HELIX           247..249
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   TURN            250..255
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   STRAND          261..268
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   HELIX           272..282
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   STRAND          284..289
FT                   /evidence="ECO:0007829|PDB:4NV0"
FT   HELIX           294..310
FT                   /evidence="ECO:0007829|PDB:4NV0"
SQ   SEQUENCE   319 AA;  36294 MW;  71919CE1CBF34EB5 CRC64;
     MGFDEKREPT GGRLRLQDIP ALTQDHCRMR DPAEVERIIN EFVIGGPERM QIVSDFDYTI
     TKQRTEDGGA VPSSFGIFNA CQSLPENFKA ETDKLYHKYR PIEIDPHMPI AEKVQYMIEW
     WTKSGELTSG FPFDQSEIDQ IASKYTHALR DRTHEFFADL QRLGIPTLVF SAGLGNSVVS
     VLRQANVLHP NVKVVSNFLQ FRDGLLDGFQ QPMIHTFNKN ETVLNETSEY YDLVHTRDHI
     IVMGDSIGDA DMASGVPASS HIMKIGFLFD HVEANMKKYM DTFDIVLVDD QTMDVPRTLL
     SLIEKQHKLN LEAPKQSSL
 
 
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