Reviewed, UniProtKB/Swiss-Prot O76464 (NFT1_DROME)

Names and origin

Protein names

Recommended name:
    Nitrilase and fragile histidine triad fusion protein NitFhit
Alternative name(s):
    NFT-1 protein
Including the following 2 domains:
    1- Recommended name:
            Bis(5'-adenosyl)-triphosphatase
              EC=3.6.1.29
        Alternative name(s):
            Diadenosine 5',5'''-P1,P3-triphosphate hydrolase
              Short name=Dinucleosidetriphosphatase
              Short name=AP3A hydrolase
              Short name=AP3Aase
    2- Recommended name:
            Nitrilase homolog
              EC=3.5.-.-

Gene names

Name:	NitFhit
ORF Names:	CG7067

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	460 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cleaves A-5'-PPP-5'A to yield AMP and ADP. Ref.1
Catalytic activity	P(1)-P(3)-bis(5'-adenosyl) triphosphate + H2O = ADP + AMP. Ref.1
Cofactor	Manganese. Ref.1
Subunit structure	Homotetramer By similarity. UniProtKB O76463
Developmental stage	Expressed in embryo and adult. Ref.1
Sequence similarities	In the N-terminal section; belongs to the UPF0012 family. Contains 1 CN hydrolase domain. Contains 1 HIT domain.

Ontologies

Keywords
Ligand	Manganese
Molecular function	Hydrolase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	nitrogen compound metabolic process Inferred from electronic annotation. Source: InterPro nucleobase, nucleoside, nucleotide and nucleic acid metabolic process Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	bis(5'-adenosyl)-triphosphatase activity Ref.1 Inferred from direct assay. Source: UniProtKB hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Ref.1 Traceable author statement. Source: UniProtKB manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 460	460	Nitrilase and fragile histidine triad fusion protein NitFhit		PRO_0000109792
Regions
	Domain	33 – 301	269	CN hydrolase
	Domain	315 – 422	108	HIT
	Region	395 – 412	18	Binding to substrate; phosphate linker By similarity
	Motif	407 – 411	5	Histidine triad motif By similarity UniProtKB P49789
Sites
	Active site	72	1	By similarity UniProtKB O76463
	Active site	142	1	By similarity UniProtKB O76463
	Active site	183	1	By similarity UniProtKB O76463
	Active site	409	1	Tele-AMP-histidine intermediate By similarity UniProtKB P49789

Sequences

	Sequence		Length	Mass (Da)
	O76464-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 81121A00BC337706	FASTA	460	52,232
	10 20 30 40 50 60 MSTLVNTTRR SIVIAIHQQL RRMSVQKRKD QSATIAVGQM RSTSDKAANL SQVIELVDRA 70 80 90 100 110 120 KSQNACMLFL PECCDFVGES RTQTIELSEG LDGELMAQYR ELAKCNKIWI SLGGVHERND 130 140 150 160 170 180 QKIFNAHVLL NEKGELAAVY RKLHMFDVTT KEVRLRESDT VTPGYCLERP VSTPVGQIGL 190 200 210 220 230 240 QICYDLRFAE PAVLLRKLGA NLLTYPSAFT YATGKAHWEI LLRARAIETQ CFVVAAAQIG 250 260 270 280 290 300 WHNQKRQSWG HSMIVSPWGN VLADCSEQEL DIGTAEVDLS VLQSLYQTMP CFEHRRNDIY 310 320 330 340 350 360 ALTAYNLRSK EPTQDRPFAT NIVDKRTIFY ESEHCFAFTN LRCVVKGHVL VSTKRVTPRL 370 380 390 400 410 420 CGLDCAEMAD MFTTVCLVQR LLEKIYQTTS ATVTVQDGAQ AGQTVPHVHF HIMPRRLGDF 430 440 450 460 GHNDQIYVKL DERAEEKPPR TIEERIEEAQ IYRKFLTDIS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nitrilase and Fhit homologs are encoded as fusion proteins in Drosophila melanogaster and Caenorhabditis elegans." Pekarsky Y., Campiglio M., Siprashvili Z., Druck T., Sedkov Y., Tillib S., Draganescu A., Wermuth P., Rothman J.H., Huebner K., Buchberg A.M., Mazo A., Brenner C., Croce C.M. Proc. Natl. Acad. Sci. U.S.A. 95:8744-8749(1998) [PubMed: 9671749] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Testis.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF069989 mRNA. Translation: AAC39137.1. AE014296 Genomic DNA. Translation: AAF47347.1. AY089221 mRNA. Translation: AAL89959.1.
RefSeq	NP_525122.1.
UniGene	Dm.1660
3D structure databases
HSSP	HSSP built from PDB template 1EMS based on UniProtKB O76463.
ModBase	Search...
Protein-protein interaction databases
IntAct	O76464. 1 interaction.
Proteomic databases
PRIDE	O76464.
Genome annotation databases
Ensembl	FBgn0024945. Drosophila melanogaster. [Contig view]
GeneID	38029.
KEGG	dme:Dmel_CG7067.
NMPDR	fig|7227.3.peg.4184.
Organism-specific databases
FlyBase	FBgn0024945. NitFhit.
Phylogenomic databases
HOGENOM	O76464.
OMA	O76464. ETQCFVV.
Enzyme and pathway databases
BRENDA	3.6.1.29. 48.
Gene expression databases
ArrayExpress	O76464.
GermOnline	CG7067. Drosophila melanogaster.
Family and domain databases
InterPro	IPR011151. His_triad_motif. IPR019808. Histidine_triad_CS. IPR001310. Histidine_triad_HIT. IPR003010. Ntlse/CNhydtse. [Graphical view]
Gene3D	G3DSA:3.30.428.10. His_triad_motif. 1 hit. G3DSA:3.60.110.10. Ntlse/CNhydtse. 1 hit.
Pfam	PF00795. CN_hydrolase. 1 hit. PF01230. HIT. 1 hit. [Graphical view]
PROSITE	PS50263. CN_HYDROLASE. 1 hit. PS00892. HIT_1. 1 hit. PS51084. HIT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	806645.

Entry information

Entry name

NFT1_DROME

Accession

Primary (citable) accession number: O76464

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	November 1, 1998
Last modified:	June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project