MESH1_DROME
ID MESH1_DROME Reviewed; 179 AA.
AC Q9VAM9;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1;
DE EC=3.1.7.2;
DE AltName: Full=Metazoan SpoT homolog 1;
DE Short=Mesh1;
DE AltName: Full=Penta-phosphate guanosine-3'-pyrophosphohydrolase;
DE Short=(ppGpp)ase;
GN Name=Mesh1; ORFNames=CG11900;
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].
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Celniker S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), DISRUPTION PHENOTYPE, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVE SITE, COFACTOR, AND MANGANESE-BINDING SITES.
RX PubMed=20818390; DOI=10.1038/nsmb.1906;
RA Sun D., Lee G., Lee J.H., Kim H.-Y., Rhee H.W., Park S.-Y., Kim K.J.,
RA Kim Y., Kim B.Y., Hong J.-I., Park C., Choy H.E., Kim J.H., Jeon Y.H.,
RA Chung J.;
RT "A metazoan ortholog of SpoT hydrolyzes ppGpp and functions in starvation
RT responses.";
RL Nat. Struct. Mol. Biol. 17:1188-1194(2010).
CC -!- FUNCTION: ppGpp hydrolyzing enzyme involved in starvation response.
CC {ECO:0000269|PubMed:20818390}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine 3',5'-bis(diphosphate) + H2O = diphosphate + GDP +
CC H(+); Xref=Rhea:RHEA:14253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58189, ChEBI:CHEBI:77828; EC=3.1.7.2;
CC Evidence={ECO:0000269|PubMed:20818390};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:20818390};
CC -!- DISRUPTION PHENOTYPE: Induces retarded body growth and impaired
CC starvation resistance. Mutants have highly down-regulated DNA and
CC protein synthesis-related genes and up-regulated stress-responsible
CC genes. {ECO:0000269|PubMed:20818390}.
CC -!- SIMILARITY: Belongs to the MESH1 family. {ECO:0000305}.
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DR EMBL; AE014297; AAF56875.1; -; Genomic_DNA.
DR EMBL; BT024375; ABC86437.1; -; mRNA.
DR RefSeq; NP_651682.1; NM_143425.2.
DR PDB; 3NQW; X-ray; 2.90 A; A/B=1-179.
DR PDBsum; 3NQW; -.
DR AlphaFoldDB; Q9VAM9; -.
DR SMR; Q9VAM9; -.
DR STRING; 7227.FBpp0084776; -.
DR PaxDb; Q9VAM9; -.
DR DNASU; 43456; -.
DR EnsemblMetazoa; FBtr0085407; FBpp0084776; FBgn0039650.
DR GeneID; 43456; -.
DR KEGG; dme:Dmel_CG11900; -.
DR UCSC; CG11900-RA; d. melanogaster.
DR CTD; 43456; -.
DR FlyBase; FBgn0039650; Mesh1.
DR VEuPathDB; VectorBase:FBgn0039650; -.
DR eggNOG; KOG1157; Eukaryota.
DR GeneTree; ENSGT00390000011608; -.
DR HOGENOM; CLU_084517_1_0_1; -.
DR InParanoid; Q9VAM9; -.
DR OMA; FVWASEV; -.
DR OrthoDB; 1372331at2759; -.
DR PhylomeDB; Q9VAM9; -.
DR BioGRID-ORCS; 43456; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43456; -.
DR PRO; PR:Q9VAM9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039650; Expressed in Malpighian tubule and 23 other tissues.
DR Genevisible; Q9VAM9; DM.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015971; P:guanosine tetraphosphate catabolic process; IDA:FlyBase.
DR GO; GO:0042594; P:response to starvation; IMP:FlyBase.
DR CDD; cd00077; HDc; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR SMART; SM00471; HDc; 1.
DR PROSITE; PS51831; HD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..179
FT /note="Guanosine-3',5'-bis(diphosphate) 3'-
FT pyrophosphohydrolase MESH1"
FT /id="PRO_0000402127"
FT DOMAIN 33..128
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT ACT_SITE 66
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:20818390"
FT ACT_SITE 67
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:20818390"
FT BINDING 36
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 62
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 123
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT HELIX 7..19
FT /evidence="ECO:0007829|PDB:3NQW"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:3NQW"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:3NQW"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3NQW"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:3NQW"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:3NQW"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:3NQW"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:3NQW"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:3NQW"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:3NQW"
FT HELIX 114..133
FT /evidence="ECO:0007829|PDB:3NQW"
FT HELIX 141..158
FT /evidence="ECO:0007829|PDB:3NQW"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:3NQW"
SQ SEQUENCE 179 AA; 20569 MW; 9227D3DA9AD4E983 CRC64;
MATYPSAKFM ECLQYAAFKH RQQRRKDPQE TPYVNHVINV STILSVEACI TDEGVLMAAL
LHDVVEDTDA SFEDVEKLFG PDVCGLVREV TDDKSLEKQE RKRLQIENAA KSSCRAKLIK
LADKLDNLRD LQVNTPTGWT QERRDQYFVW AKKVVDNLRG TNANLELKLD EIFRQRGLL
