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P00967

- PUR2_DROME

UniProt

P00967 - PUR2_DROME

Protein

Trifunctional purine biosynthetic protein adenosine-3

Gene

ade3

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide.
    ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole.
    10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi291 – 2911ManganeseBy similarity
    Metal bindingi293 – 2931ManganeseBy similarity
    Binding sitei1219 – 1219110-formyltetrahydrofolateBy similarity
    Binding sitei1261 – 1261110-formyltetrahydrofolateBy similarity
    Active sitei1263 – 12631Proton donorBy similarity
    Sitei1299 – 12991Raises pKa of active site HisBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi140 – 20263ATPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. methyltransferase activity Source: InterPro
    4. phosphoribosylamine-glycine ligase activity Source: FlyBase
    5. phosphoribosylformylglycinamidine cyclo-ligase activity Source: FlyBase
    6. phosphoribosylglycinamide formyltransferase activity Source: FlyBase

    GO - Biological processi

    1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
    2. purine nucleobase biosynthetic process Source: FlyBase

    Keywords - Molecular functioni

    Ligase, Transferase

    Keywords - Biological processi

    Purine biosynthesis

    Keywords - Ligandi

    ATP-binding, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_208157. Purine ribonucleoside monophosphate biosynthesis.
    UniPathwayiUPA00074; UER00125.
    UPA00074; UER00126.
    UPA00074; UER00129.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trifunctional purine biosynthetic protein adenosine-3
    Including the following 3 domains:
    Phosphoribosylamine--glycine ligase (EC:6.3.4.13)
    Alternative name(s):
    Glycinamide ribonucleotide synthetase
    Short name:
    GARS
    Phosphoribosylglycinamide synthetase
    Phosphoribosylformylglycinamidine cyclo-ligase (EC:6.3.3.1)
    Alternative name(s):
    AIR synthase
    Short name:
    AIRS
    Phosphoribosyl-aminoimidazole synthetase
    Phosphoribosylglycinamide formyltransferase (EC:2.1.2.2)
    Alternative name(s):
    5'-phosphoribosylglycinamide transformylase
    GAR transformylase
    Short name:
    GART
    Gene namesi
    Name:ade3
    Synonyms:Gart
    ORF Names:CG31628
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0000053. ade3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13531353Trifunctional purine biosynthetic protein adenosine-3PRO_0000074934Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei814 – 8141Phosphoserine1 Publication
    Modified residuei816 – 8161Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP00967.

    Expressioni

    Gene expression databases

    BgeeiP00967.

    Interactioni

    Protein-protein interaction databases

    BioGridi60135. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP00967.
    SMRiP00967. Positions 1-431, 442-791, 841-1134, 1155-1343.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini114 – 321208ATP-graspAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni434 – 1152719AIRSAdd
    BLAST
    Regioni1153 – 1353201GARTAdd
    BLAST
    Regioni1164 – 116635'-phosphoribosylglycinamide bindingBy similarity
    Regioni1244 – 1247410-formyltetrahydrofolate bindingBy similarity
    Regioni1295 – 1299510-formyltetrahydrofolate bindingBy similarity
    Regioni1325 – 132845'-phosphoribosylglycinamide bindingBy similarity

    Sequence similaritiesi

    In the N-terminal section; belongs to the GARS family.Curated
    In the central section; belongs to the AIR synthase family.Curated
    In the C-terminal section; belongs to the GART family.Curated
    Contains 1 ATP-grasp domain.Curated

    Phylogenomic databases

    eggNOGiCOG0151.
    InParanoidiP00967.
    KOiK11787.
    OrthoDBiEOG7RBZ7H.
    PhylomeDBiP00967.

    Family and domain databases

    Gene3Di3.30.1330.10. 2 hits.
    3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.170. 1 hit.
    3.40.50.20. 1 hit.
    3.90.600.10. 1 hit.
    3.90.650.10. 2 hits.
    HAMAPiMF_00138. GARS.
    InterProiIPR010918. AIR_synth_C_dom.
    IPR000728. AIR_synth_N_dom.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR002376. Formyl_transf_N.
    IPR001555. GART_AS.
    IPR016185. PreATP-grasp_dom.
    IPR020561. PRibGlycinamid_synth_ATP-grasp.
    IPR000115. PRibGlycinamide_synth.
    IPR020560. PRibGlycinamide_synth_C-dom.
    IPR020559. PRibGlycinamide_synth_CS.
    IPR020562. PRibGlycinamide_synth_N.
    IPR004733. PurM_cligase.
    IPR016188. PurM_N-like.
    IPR004607. PurN_trans.
    IPR011054. Rudment_hybrid_motif.
    [Graphical view]
    PfamiPF00586. AIRS. 2 hits.
    PF02769. AIRS_C. 2 hits.
    PF00551. Formyl_trans_N. 1 hit.
    PF01071. GARS_A. 1 hit.
    PF02843. GARS_C. 1 hit.
    PF02844. GARS_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51246. SSF51246. 1 hit.
    SSF52440. SSF52440. 1 hit.
    SSF53328. SSF53328. 1 hit.
    SSF55326. SSF55326. 2 hits.
    SSF56042. SSF56042. 2 hits.
    TIGRFAMsiTIGR00877. purD. 1 hit.
    TIGR00878. purM. 2 hits.
    TIGR00639. PurN. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    PS00184. GARS. 1 hit.
    PS00373. GART. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P00967-1) [UniParc]FASTAAdd to Basket

    Also known as: A, 4.7 kb

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSHRVLVIGS GGREHAICWK LSQSPKVAQI YALPGSHGIQ LVEKCRNLDA     50
    KTLDPKDFEA IAKWSKENQI ALVVVGPEDP LALGLGDVLQ SAGIPCFGPG 100
    KQGAQIEADK KWAKDFMLRH GIPTARYESF TDTEKAKAFI RSAPYPALVV 150
    KAAGLAAGKG VVVAANAKEA CQAVDEILGD LKYGQAGATL VVEELLEGEE 200
    VSVLAFTDGK SVRAMLPAQD HKRLGNGDTG PNTGGMGAYC PCPLISQPAL 250
    ELVQKAVLER AVQGLIKERI NYQGVLYAGL MLTRDGPRVL EFNCRFGDPE 300
    TQVILPLLES DLFDVMEACC SGKLDKIPLQ WRNGVSAVGV ILASAGYPET 350
    STKGCIISGL PAANTPTQLV FHSGLAVNAQ KEALTNGGRV LIAIALDGSL 400
    KEAAAKATKL AGSISFSGSG AQYRTDIAQK AFKIASASTP GLSYKDSGVD 450
    IDAGDALVQR IKPLSRGTQR PGVIGGLGGF GGLFRLKELT YKEPVIAEAT 500
    QGVGAKIHLA LTHEFYENVG YDLFALAAND VLEVGAEPVA FLDYIACGKL 550
    QVPLAAQLVK GMADGCRDAR CALVGGETAE MPSLYAPGQH DMAGYCVGIV 600
    EHSRILPRFD LYQPGDLLIG LPSSGLHCAG FNEILTQLAA SKVNLRERSP 650
    VDGGDDGLTL AHVLATPTQL YVQQLLPHLQ KGDEIKSVAH VTHGLLNDIL 700
    RLLPDGFETT LDFGAVPVPK IFGWLAGKLK LSAQTILERH NCGIGMVLIL 750
    PQSSQLWRTS LPGAKVLGVL QRRSKVSGSP VQVRNFVEQL EKVASPFGGL 800
    GDRELPEELK KLPSNSDLSA PREECFENAA GRRLTRIPTH YKDPILILGT 850
    DGVGTKLKIA QQTNRNTSVG IDLVAMCVND ILCNGAEPIS FSSYYACGHW 900
    QEQLAKGVHS GVQEGARQAN SSFIDSHSAA LPLLYEPQVY DLAGFALGIA 950
    EHTGILPLLA EIQPGDVLIG LPSSGVHSNG FSLVHAVLKR VGLGLHDKAP 1000
    FSDKTLGEEL LVPTKIYVKA LSTLLSRGKH GIKALAHITG GGLSENIPRV 1050
    LRKDLAVRLD ANKFQLPPVF AWLAAAGNIS STELQRTYNC GLGMVLVVAP 1100
    TEVEDVLKEL RYPQRAAVVG EVVARKDPKK SQVVVQNFEA SLARTQKMLS 1150
    QRRKRVAVLI SGTGSNLQAL IDATRDSAQG IHADVVLVIS NKPGVLGLQR 1200
    ATQAGIPSLV ISHKDFASRE VYDAELTRNL KAARVDLICL AGFMRVLSAP 1250
    FVREWRGRLV NIHPSLLPKY PGLHVQKQAL EAGEKESGCT VHFVDEGVDT 1300
    GAIIVQAAVP ILPDDDEDSL TQRIHKAEHW AFPRALAMLV NGTALISPEV 1350
    SSQ 1353
    Length:1,353
    Mass (Da):144,448
    Last modified:April 1, 1990 - v2
    Checksum:iA68DAB61A02DFD4F
    GO
    Isoform Short (identifier: P00967-2) [UniParc]FASTAAdd to Basket

    Also known as: 1.7 kb

    The sequence of this isoform differs from the canonical sequence as follows:
         434-434: I → M
         435-1353: Missing.

    Show »
    Length:434
    Mass (Da):45,864
    Checksum:i0EF3BD499D8B8495
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti515 – 5151F → L in AAF52474. (PubMed:10731132)Curated
    Sequence conflicti602 – 6021H → Q in AAF52474. (PubMed:10731132)Curated
    Sequence conflicti907 – 9071G → E in AAF52474. (PubMed:10731132)Curated
    Sequence conflicti960 – 9601A → D in AAF52474. (PubMed:10731132)Curated
    Sequence conflicti1193 – 11931P → T in AAF52474. (PubMed:10731132)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei434 – 4341I → M in isoform Short. CuratedVSP_005512
    Alternative sequencei435 – 1353919Missing in isoform Short. CuratedVSP_005513Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02527 Genomic DNA. Translation: AAA28562.1.
    J02527 Genomic DNA. Translation: AAA28563.1.
    AE014134 Genomic DNA. Translation: AAF52474.2.
    X00041 Genomic DNA. Translation: CAA24923.1.
    PIRiS01206. AJFFPM.
    RefSeqiNP_001014477.1. NM_001014477.1. [P00967-2]
    NP_523497.2. NM_078773.2.
    UniGeneiDm.21459.

    Genome annotation databases

    GeneIDi33986.
    KEGGidme:Dmel_CG31628.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02527 Genomic DNA. Translation: AAA28562.1 .
    J02527 Genomic DNA. Translation: AAA28563.1 .
    AE014134 Genomic DNA. Translation: AAF52474.2 .
    X00041 Genomic DNA. Translation: CAA24923.1 .
    PIRi S01206. AJFFPM.
    RefSeqi NP_001014477.1. NM_001014477.1. [P00967-2 ]
    NP_523497.2. NM_078773.2.
    UniGenei Dm.21459.

    3D structure databases

    ProteinModelPortali P00967.
    SMRi P00967. Positions 1-431, 442-791, 841-1134, 1155-1343.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 60135. 1 interaction.

    Proteomic databases

    PaxDbi P00967.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 33986.
    KEGGi dme:Dmel_CG31628.

    Organism-specific databases

    CTDi 33986.
    FlyBasei FBgn0000053. ade3.

    Phylogenomic databases

    eggNOGi COG0151.
    InParanoidi P00967.
    KOi K11787.
    OrthoDBi EOG7RBZ7H.
    PhylomeDBi P00967.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00125 .
    UPA00074 ; UER00126 .
    UPA00074 ; UER00129 .
    Reactomei REACT_208157. Purine ribonucleoside monophosphate biosynthesis.

    Miscellaneous databases

    GenomeRNAii 33986.
    NextBioi 786281.
    PROi P00967.

    Gene expression databases

    Bgeei P00967.

    Family and domain databases

    Gene3Di 3.30.1330.10. 2 hits.
    3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.170. 1 hit.
    3.40.50.20. 1 hit.
    3.90.600.10. 1 hit.
    3.90.650.10. 2 hits.
    HAMAPi MF_00138. GARS.
    InterProi IPR010918. AIR_synth_C_dom.
    IPR000728. AIR_synth_N_dom.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR002376. Formyl_transf_N.
    IPR001555. GART_AS.
    IPR016185. PreATP-grasp_dom.
    IPR020561. PRibGlycinamid_synth_ATP-grasp.
    IPR000115. PRibGlycinamide_synth.
    IPR020560. PRibGlycinamide_synth_C-dom.
    IPR020559. PRibGlycinamide_synth_CS.
    IPR020562. PRibGlycinamide_synth_N.
    IPR004733. PurM_cligase.
    IPR016188. PurM_N-like.
    IPR004607. PurN_trans.
    IPR011054. Rudment_hybrid_motif.
    [Graphical view ]
    Pfami PF00586. AIRS. 2 hits.
    PF02769. AIRS_C. 2 hits.
    PF00551. Formyl_trans_N. 1 hit.
    PF01071. GARS_A. 1 hit.
    PF02843. GARS_C. 1 hit.
    PF02844. GARS_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51246. SSF51246. 1 hit.
    SSF52440. SSF52440. 1 hit.
    SSF53328. SSF53328. 1 hit.
    SSF55326. SSF55326. 2 hits.
    SSF56042. SSF56042. 2 hits.
    TIGRFAMsi TIGR00877. purD. 1 hit.
    TIGR00878. purM. 2 hits.
    TIGR00639. PurN. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    PS00184. GARS. 1 hit.
    PS00373. GART. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Conserved arrangement of nested genes at the Drosophila Gart locus."
      Henikoff S., Eghtedarzadeh M.K.
      Genetics 117:711-725(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
      Strain: Canton-S.
      Tissue: Embryo.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. "A Drosophila metabolic gene transcript is alternatively processed."
      Henikoff S., Sloan J.S., Kelly J.D.
      Cell 34:405-414(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-1353, ALTERNATIVE SPLICING.
      Strain: Canton-S and Oregon-R.
      Tissue: Embryo.
    5. "Sequence of a Drosophila DNA segment that functions in Saccharomyces cerevisiae and its regulation by a yeast promoter."
      Henikoff S., Furlong C.E.
      Nucleic Acids Res. 11:789-800(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1147-1353 (ISOFORM LONG).
      Strain: Oregon-R.
      Tissue: Embryo.
    6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-814 AND SER-816, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiPUR2_DROME
    AccessioniPrimary (citable) accession number: P00967
    Secondary accession number(s): Q9VM53
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3