NFT1_DROME
ID NFT1_DROME Reviewed; 460 AA.
AC O76464;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Nitrilase and fragile histidine triad fusion protein NitFhit;
DE AltName: Full=NFT-1 protein;
DE Includes:
DE RecName: Full=Bis(5'-adenosyl)-triphosphatase;
DE EC=3.6.1.29;
DE AltName: Full=Diadenosine 5',5'''-P1,P3-triphosphate hydrolase;
DE Short=AP3A hydrolase;
DE Short=AP3Aase;
DE Short=Dinucleosidetriphosphatase;
DE Includes:
DE RecName: Full=Nitrilase homolog;
DE EC=3.5.-.-;
GN Name=NitFhit {ECO:0000312|EMBL:AAF47347.1}; ORFNames=CG7067;
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] {ECO:0000305, ECO:0000312|EMBL:AAC39137.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=9671749; DOI=10.1073/pnas.95.15.8744;
RA Pekarsky Y., Campiglio M., Siprashvili Z., Druck T., Sedkov Y., Tillib S.,
RA Draganescu A., Wermuth P., Rothman J.H., Huebner K., Buchberg A.M.,
RA Mazo A., Brenner C., Croce C.M.;
RT "Nitrilase and Fhit homologs are encoded as fusion proteins in Drosophila
RT melanogaster and Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8744-8749(1998).
RN [2] {ECO:0000312|EMBL:AAF47347.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [3]
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAL89959.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Testis {ECO:0000312|EMBL:AAL89959.1};
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).
CC -!- FUNCTION: Cleaves A-5'-PPP-5'A to yield AMP and ADP.
CC {ECO:0000269|PubMed:9671749}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(3)-bis(5'-adenosyl) triphosphate = ADP + AMP + 2
CC H(+); Xref=Rhea:RHEA:13893, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58529, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=3.6.1.29; Evidence={ECO:0000269|PubMed:9671749};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O76463}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo and adult.
CC {ECO:0000269|PubMed:9671749}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the UPF0012 family.
CC {ECO:0000255}.
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DR EMBL; AF069989; AAC39137.1; -; mRNA.
DR EMBL; AE014296; AAF47347.1; -; Genomic_DNA.
DR EMBL; AY089221; AAL89959.1; -; mRNA.
DR RefSeq; NP_525122.1; NM_080383.4.
DR AlphaFoldDB; O76464; -.
DR SMR; O76464; -.
DR BioGRID; 63593; 2.
DR IntAct; O76464; 1.
DR STRING; 7227.FBpp0072385; -.
DR PaxDb; O76464; -.
DR PRIDE; O76464; -.
DR DNASU; 38029; -.
DR EnsemblMetazoa; FBtr0072483; FBpp0072385; FBgn0024945.
DR GeneID; 38029; -.
DR KEGG; dme:Dmel_CG7067; -.
DR CTD; 38029; -.
DR FlyBase; FBgn0024945; NitFhit.
DR VEuPathDB; VectorBase:FBgn0024945; -.
DR eggNOG; KOG0807; Eukaryota.
DR eggNOG; KOG3379; Eukaryota.
DR GeneTree; ENSGT00550000075099; -.
DR HOGENOM; CLU_030130_12_1_1; -.
DR InParanoid; O76464; -.
DR OMA; GWHNKKR; -.
DR OrthoDB; 1154369at2759; -.
DR PhylomeDB; O76464; -.
DR SignaLink; O76464; -.
DR BioGRID-ORCS; 38029; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38029; -.
DR PRO; PR:O76464; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0024945; Expressed in adult Malpighian tubule (Drosophila) and 24 other tissues.
DR Genevisible; O76464; DM.
DR GO; GO:0047710; F:bis(5'-adenosyl)-triphosphatase activity; IDA:UniProtKB.
DR GO; GO:0110050; F:deaminated glutathione amidase activity; ISS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0043605; P:cellular amide catabolic process; ISS:UniProtKB.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IDA:UniProtKB.
DR CDD; cd01275; FHIT; 1.
DR CDD; cd07572; nit; 1.
DR Gene3D; 3.30.428.10; -; 1.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR039383; FHIT.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF01230; HIT; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
DR PROSITE; PS00892; HIT_1; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Manganese; Multifunctional enzyme; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..460
FT /note="Nitrilase and fragile histidine triad fusion protein
FT NitFhit"
FT /id="PRO_0000109792"
FT DOMAIN 33..279
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT DOMAIN 315..422
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT MOTIF 407..411
FT /note="Histidine triad motif"
FT ACT_SITE 72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 409
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P49789,
FT ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 460 AA; 52232 MW; 81121A00BC337706 CRC64;
MSTLVNTTRR SIVIAIHQQL RRMSVQKRKD QSATIAVGQM RSTSDKAANL SQVIELVDRA
KSQNACMLFL PECCDFVGES RTQTIELSEG LDGELMAQYR ELAKCNKIWI SLGGVHERND
QKIFNAHVLL NEKGELAAVY RKLHMFDVTT KEVRLRESDT VTPGYCLERP VSTPVGQIGL
QICYDLRFAE PAVLLRKLGA NLLTYPSAFT YATGKAHWEI LLRARAIETQ CFVVAAAQIG
WHNQKRQSWG HSMIVSPWGN VLADCSEQEL DIGTAEVDLS VLQSLYQTMP CFEHRRNDIY
ALTAYNLRSK EPTQDRPFAT NIVDKRTIFY ESEHCFAFTN LRCVVKGHVL VSTKRVTPRL
CGLDCAEMAD MFTTVCLVQR LLEKIYQTTS ATVTVQDGAQ AGQTVPHVHF HIMPRRLGDF
GHNDQIYVKL DERAEEKPPR TIEERIEEAQ IYRKFLTDIS
