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P07764

- ALF_DROME

UniProt

P07764 - ALF_DROME

Protein

Fructose-bisphosphate aldolase

Gene

Ald

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 153 (01 Oct 2014)
      Sequence version 5 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    May take part in developmental stage-specific or tissue -specific sugar-phosphate metabolisms. Protein acts on two substrates fructose 1,6-bisphosphate and fructose 1-phosphate (like other class I aldolases).1 Publication

    Catalytic activityi

    D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.1 Publication

    pH dependencei

    Optimum pH is 7.2-7.8 for isozyme alpha, and 7.2-7.5 for isozymes beta and gamma.1 Publication

    Temperature dependencei

    Thermostability of the isozymes, calculated as the temperature causing half maximal stability, is 42-43 degrees Celsius for isozymes alpha and beta and 45 degrees Celsius for isozyme gamma.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei56 – 561Substrate
    Binding sitei147 – 1471Substrate
    Active sitei188 – 1881Proton acceptorBy similarity
    Active sitei230 – 2301Schiff-base intermediate with dihydroxyacetone-P
    Sitei361 – 3611Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

    GO - Molecular functioni

    1. fructose-bisphosphate aldolase activity Source: FlyBase

    GO - Biological processi

    1. glycolytic process Source: FlyBase
    2. mesoderm development Source: FlyBase
    3. mitotic G2 DNA damage checkpoint Source: FlyBase

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Schiff base

    Enzyme and pathway databases

    ReactomeiREACT_206319. Glycolysis.
    REACT_213188. Fructose catabolism.
    REACT_220315. Gluconeogenesis.
    SABIO-RKP07764.
    UniPathwayiUPA00109; UER00183.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-bisphosphate aldolase (EC:4.1.2.13)
    Gene namesi
    Name:Ald
    ORF Names:CG6058
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0000064. Ald.

    Subcellular locationi

    GO - Cellular componenti

    1. M band Source: FlyBase
    2. Z disc Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 361360Fructose-bisphosphate aldolasePRO_0000216927Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP07764.
    PRIDEiP07764.

    Expressioni

    Tissue specificityi

    Isozyme gamma is mainly expressed in the heads and partly in the thoraxes of adult flies. Isozyme alpha is expressed in all adult tissues. Isozyme beta is mainly expressed in adult abdominal regions and is also expressed in lesser amounts in other parts of the body and in earlier developmental stages. Isozyme alpha-beta shows strong expression in the abdomens of adults. Isozyme beta-gamma is expressed in adult heads.2 Publications

    Developmental stagei

    Isozyme gamma is first detected during late embryogenesis, is present through larval stages, declines in abundance during pupal stages and is maximum at eclosion. Isozyme beta is abundant during the earliest stages of embryogenesis, declines in amount and increases prior to hatching. Isozyme alpha is found only during the adult stage. Expression correlates to dietary behavior: high dietary activity in the larvae and adults causes active glycolysis and high expression levels. Isozyme alpha-beta is detected in the pupae and adults and isozyme beta-gamma in the adult.1 Publication

    Gene expression databases

    BgeeiP07764.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi68080. 88 interactions.
    MINTiMINT-782439.

    Structurei

    Secondary structure

    1
    361
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 2314
    Beta strandi29 – 335
    Helixi37 – 4610
    Helixi53 – 6412
    Helixi68 – 725
    Beta strandi74 – 796
    Helixi81 – 844
    Helixi94 – 1007
    Beta strandi104 – 1085
    Beta strandi113 – 1153
    Beta strandi119 – 1213
    Beta strandi123 – 1253
    Helixi131 – 14010
    Beta strandi143 – 15210
    Beta strandi155 – 1573
    Helixi161 – 18020
    Beta strandi184 – 1918
    Helixi199 – 21921
    Helixi224 – 2263
    Helixi245 – 25915
    Beta strandi266 – 2694
    Helixi276 – 28611
    Beta strandi295 – 3028
    Helixi303 – 3053
    Helixi307 – 3137
    Helixi320 – 33718
    Turni338 – 3403
    Turni344 – 3474

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FBAX-ray1.90A/B/C/D2-361[»]
    ProteinModelPortaliP07764.
    SMRiP07764. Positions 2-361.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07764.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG3588.
    GeneTreeiENSGT00390000010235.
    InParanoidiP07764.
    KOiK01623.
    OMAiMLFRSDD.
    OrthoDBiEOG744T94.
    PhylomeDBiP07764.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR000741. FBA_I.
    [Graphical view]
    PfamiPF00274. Glycolytic. 1 hit.
    [Graphical view]
    PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Two additional mRNAs also exist (Alpha-beta and Beta-gamma). The translation product of Alpha-beta mRNA is isoform Alpha.

    Isoform Gamma (identifier: P07764-1) [UniParc]FASTAAdd to Basket

    Also known as: 4C, B, C, D

    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

    MTTYFNYPSK ELQDELREIA QKIVAPGKGI LAADESGPTM GKRLQDIGVE    50
    NTEDNRRAYR QLLFSTDPKL AENISGVILF HETLYQKADD GTPFAEILKK 100
    KGIILGIKVD KGVVPLFGSE DEVTTQGLDD LAARCAQYKK DGCDFAKWRC 150
    VLKIGKNTPS YQSILENANV LARYASICQS QRIVPIVEPE VLPDGDHDLD 200
    RAQKVTETVL AAVYKALSDH HVYLEGTLLK PNMVTAGQSA KKNTPEEIAL 250
    ATVQALRRTV PAAVTGVTFL SGGQSEEEAT VNLSAINNVP LIRPWALTFS 300
    YGRALQASVL RAWAGKKENI AAGQNELLKR AKANGDAAQG KYVAGSAGAG 350
    SGSLFVANHA Y 361
    Length:361
    Mass (Da):39,047
    Last modified:January 23, 2007 - v5
    Checksum:iD8DA46E273668CE9
    GO
    Isoform Alpha (identifier: P07764-2) [UniParc]FASTAAdd to Basket

    Also known as: 4A, E

    The sequence of this isoform differs from the canonical sequence as follows:
         336-361: DAAQGKYVAGSAGAGSGSLFVANHAY → EAACGNYTAGSVKGFAGKDTLHVDDHRY

    Show »
    Length:363
    Mass (Da):39,561
    Checksum:iE48CC61438C85B64
    GO
    Isoform Beta (identifier: P07764-3) [UniParc]FASTAAdd to Basket

    Also known as: 4B, H

    The sequence of this isoform differs from the canonical sequence as follows:
         335-361: GDAAQGKYVAGSAGAGSGSLFVANHAY → SQACQGIYVPGSIPSFAGNANLFVAQHKY

    Show »
    Length:363
    Mass (Da):39,589
    Checksum:i7B326172746BF31D
    GO

    Sequence cautioni

    The sequence AAM75045.1 differs from that shown. Reason: Frameshift at positions 267 and 333.
    The sequence ABH06768.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence ABH06769.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence ABH06770.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence ABH06771.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence ABH06772.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence ABH06773.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence ABH06774.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence ABH06775.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence ABH06776.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence ABH06777.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence ABH06778.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence ABH06779.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAA42666.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 401M → H in BAA01236. (PubMed:1339430)Curated
    Sequence conflicti40 – 401M → H in BAA01237. (PubMed:1339430)Curated
    Sequence conflicti40 – 401M → H in BAA01238. (PubMed:1339430)Curated
    Sequence conflicti40 – 401M → H in BAA01592. (PubMed:7487099)Curated
    Sequence conflicti111 – 1111K → E in CAA42666. (PubMed:1732743)Curated
    Sequence conflicti111 – 1111K → E in CAA42667. (PubMed:1732743)Curated
    Sequence conflicti181 – 1811Q → E in BAA01236. (PubMed:1339430)Curated
    Sequence conflicti181 – 1811Q → E in BAA01237. (PubMed:1339430)Curated
    Sequence conflicti181 – 1811Q → E in BAA01238. (PubMed:1339430)Curated
    Sequence conflicti181 – 1811Q → E in BAA01592. (PubMed:7487099)Curated
    Sequence conflicti201 – 2011R → G in CAA42666. (PubMed:1732743)Curated
    Sequence conflicti201 – 2011R → G in CAA42667. (PubMed:1732743)Curated
    Sequence conflicti251 – 2511A → T in CAA42666. (PubMed:1732743)Curated
    Sequence conflicti251 – 2511A → T in CAA42667. (PubMed:1732743)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei335 – 36127GDAAQ…ANHAY → SQACQGIYVPGSIPSFAGNA NLFVAQHKY in isoform Beta. 1 PublicationVSP_000221Add
    BLAST
    Alternative sequencei336 – 36126DAAQG…ANHAY → EAACGNYTAGSVKGFAGKDT LHVDDHRY in isoform Alpha. 1 PublicationVSP_000223Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10446 Genomic DNA. Translation: BAA01236.1.
    D10446 Genomic DNA. Translation: BAA01237.1.
    D10446 Genomic DNA. Translation: BAA01238.1.
    M98351 Genomic DNA. Translation: AAA99426.1.
    M98351 Genomic DNA. Translation: AAA99427.1.
    M98351 Genomic DNA. Translation: AAA99428.1.
    X60064 Genomic DNA. Translation: CAA42666.1. Sequence problems.
    X60064 Genomic DNA. Translation: CAA42667.1.
    X60064 Genomic DNA. Translation: CAA42668.1.
    D10762 mRNA. Translation: BAA01592.1.
    DQ864133 Genomic DNA. Translation: ABH06768.1. Sequence problems.
    DQ864134 Genomic DNA. Translation: ABH06769.1. Sequence problems.
    DQ864135 Genomic DNA. Translation: ABH06770.1. Sequence problems.
    DQ864136 Genomic DNA. Translation: ABH06771.1. Sequence problems.
    DQ864137 Genomic DNA. Translation: ABH06772.1. Sequence problems.
    DQ864138 Genomic DNA. Translation: ABH06773.1. Sequence problems.
    DQ864139 Genomic DNA. Translation: ABH06774.1. Sequence problems.
    DQ864140 Genomic DNA. Translation: ABH06775.1. Sequence problems.
    DQ864141 Genomic DNA. Translation: ABH06776.1. Sequence problems.
    DQ864142 Genomic DNA. Translation: ABH06777.1. Sequence problems.
    DQ864143 Genomic DNA. Translation: ABH06778.1. Sequence problems.
    DQ864144 Genomic DNA. Translation: ABH06779.1. Sequence problems.
    AE014297 Genomic DNA. Translation: AAF56579.1.
    AE014297 Genomic DNA. Translation: AAN14381.1.
    AE014297 Genomic DNA. Translation: AAN14382.1.
    AE014297 Genomic DNA. Translation: AAN14384.1.
    AE014297 Genomic DNA. Translation: AAS65220.1.
    AY058667 mRNA. Translation: AAL13896.1.
    AY128452 mRNA. Translation: AAM75045.1. Frameshift.
    PIRiA42027. ADFFR.
    A42263.
    B42027. ADFF.
    B42263.
    C42263.
    JX0233.
    S68360.
    RefSeqiNP_001262985.1. NM_001276056.1. [P07764-3]
    NP_524515.2. NM_079791.4. [P07764-2]
    NP_733140.2. NM_170261.2. [P07764-3]
    NP_733141.1. NM_170262.2. [P07764-1]
    NP_733142.1. NM_170263.3. [P07764-1]
    NP_733143.1. NM_170264.2. [P07764-1]
    NP_733144.3. NM_170265.3. [P07764-1]
    NP_733145.3. NM_170266.3. [P07764-2]
    NP_996300.1. NM_206577.2. [P07764-3]
    UniGeneiDm.2349.

    Genome annotation databases

    EnsemblMetazoaiFBtr0084994; FBpp0084367; FBgn0000064. [P07764-1]
    FBtr0084995; FBpp0084368; FBgn0000064. [P07764-1]
    FBtr0084999; FBpp0084372; FBgn0000064. [P07764-1]
    FBtr0310660; FBpp0302780; FBgn0000064. [P07764-1]
    GeneIDi43183.
    KEGGidme:Dmel_CG6058.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10446 Genomic DNA. Translation: BAA01236.1 .
    D10446 Genomic DNA. Translation: BAA01237.1 .
    D10446 Genomic DNA. Translation: BAA01238.1 .
    M98351 Genomic DNA. Translation: AAA99426.1 .
    M98351 Genomic DNA. Translation: AAA99427.1 .
    M98351 Genomic DNA. Translation: AAA99428.1 .
    X60064 Genomic DNA. Translation: CAA42666.1 . Sequence problems.
    X60064 Genomic DNA. Translation: CAA42667.1 .
    X60064 Genomic DNA. Translation: CAA42668.1 .
    D10762 mRNA. Translation: BAA01592.1 .
    DQ864133 Genomic DNA. Translation: ABH06768.1 . Sequence problems.
    DQ864134 Genomic DNA. Translation: ABH06769.1 . Sequence problems.
    DQ864135 Genomic DNA. Translation: ABH06770.1 . Sequence problems.
    DQ864136 Genomic DNA. Translation: ABH06771.1 . Sequence problems.
    DQ864137 Genomic DNA. Translation: ABH06772.1 . Sequence problems.
    DQ864138 Genomic DNA. Translation: ABH06773.1 . Sequence problems.
    DQ864139 Genomic DNA. Translation: ABH06774.1 . Sequence problems.
    DQ864140 Genomic DNA. Translation: ABH06775.1 . Sequence problems.
    DQ864141 Genomic DNA. Translation: ABH06776.1 . Sequence problems.
    DQ864142 Genomic DNA. Translation: ABH06777.1 . Sequence problems.
    DQ864143 Genomic DNA. Translation: ABH06778.1 . Sequence problems.
    DQ864144 Genomic DNA. Translation: ABH06779.1 . Sequence problems.
    AE014297 Genomic DNA. Translation: AAF56579.1 .
    AE014297 Genomic DNA. Translation: AAN14381.1 .
    AE014297 Genomic DNA. Translation: AAN14382.1 .
    AE014297 Genomic DNA. Translation: AAN14384.1 .
    AE014297 Genomic DNA. Translation: AAS65220.1 .
    AY058667 mRNA. Translation: AAL13896.1 .
    AY128452 mRNA. Translation: AAM75045.1 . Frameshift.
    PIRi A42027. ADFFR.
    A42263.
    B42027. ADFF.
    B42263.
    C42263.
    JX0233.
    S68360.
    RefSeqi NP_001262985.1. NM_001276056.1. [P07764-3 ]
    NP_524515.2. NM_079791.4. [P07764-2 ]
    NP_733140.2. NM_170261.2. [P07764-3 ]
    NP_733141.1. NM_170262.2. [P07764-1 ]
    NP_733142.1. NM_170263.3. [P07764-1 ]
    NP_733143.1. NM_170264.2. [P07764-1 ]
    NP_733144.3. NM_170265.3. [P07764-1 ]
    NP_733145.3. NM_170266.3. [P07764-2 ]
    NP_996300.1. NM_206577.2. [P07764-3 ]
    UniGenei Dm.2349.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FBA X-ray 1.90 A/B/C/D 2-361 [» ]
    ProteinModelPortali P07764.
    SMRi P07764. Positions 2-361.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 68080. 88 interactions.
    MINTi MINT-782439.

    Proteomic databases

    PaxDbi P07764.
    PRIDEi P07764.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0084994 ; FBpp0084367 ; FBgn0000064 . [P07764-1 ]
    FBtr0084995 ; FBpp0084368 ; FBgn0000064 . [P07764-1 ]
    FBtr0084999 ; FBpp0084372 ; FBgn0000064 . [P07764-1 ]
    FBtr0310660 ; FBpp0302780 ; FBgn0000064 . [P07764-1 ]
    GeneIDi 43183.
    KEGGi dme:Dmel_CG6058.

    Organism-specific databases

    CTDi 42126.
    FlyBasei FBgn0000064. Ald.

    Phylogenomic databases

    eggNOGi COG3588.
    GeneTreei ENSGT00390000010235.
    InParanoidi P07764.
    KOi K01623.
    OMAi MLFRSDD.
    OrthoDBi EOG744T94.
    PhylomeDBi P07764.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00183 .
    Reactomei REACT_206319. Glycolysis.
    REACT_213188. Fructose catabolism.
    REACT_220315. Gluconeogenesis.
    SABIO-RK P07764.

    Miscellaneous databases

    ChiTaRSi ALD. drosophila.
    EvolutionaryTracei P07764.
    GenomeRNAii 43183.
    NextBioi 832589.

    Gene expression databases

    Bgeei P07764.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR000741. FBA_I.
    [Graphical view ]
    Pfami PF00274. Glycolytic. 1 hit.
    [Graphical view ]
    PROSITEi PS00158. ALDOLASE_CLASS_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Gene structure and multiple mRNA species of Drosophila melanogaster aldolase generating three isozymes with different enzymatic properties."
      Kai T., Sugimoto Y., Kusakabe T., Zhang R., Koga K., Hori K.
      J. Biochem. 112:677-688(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS ALPHA; BETA AND GAMMA), TISSUE SPECIFICITY.
      Strain: Oregon-R.
    2. "Alternative splicing of fructose 1,6-bisphosphate aldolase transcripts in Drosophila melanogaster predicts three isozymes."
      Shaw-Lee R., Lissemore J.L., Sullivan D.T., Tolan D.R.
      J. Biol. Chem. 267:3959-3967(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS ALPHA; BETA AND GAMMA).
      Strain: Oregon-R.
    3. "Alternate use of divergent forms of an ancient exon in the fructose-1,6-bisphosphate aldolase gene of Drosophila melanogaster."
      Kim J., Yim J.J., Wang S., Dorsett D.
      Mol. Cell. Biol. 12:773-783(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS BETA AND GAMMA).
      Strain: Oregon-R.
      Tissue: Head.
    4. "Analysis of the in vitro translation product of a novel-type Drosophila melanogaster aldolase mRNA in which two carboxyl-terminal exons remain unspliced."
      Sugimoto Y., Kusakabe T., Kai T., Okamura T., Koga K., Hori K.
      Arch. Biochem. Biophys. 323:361-366(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), PROTEIN SEQUENCE OF 354-361 (ISOFORM ALPHA).
      Strain: Oregon-R.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DPF3, DPF4, HFL12, HFL13, HFL15, HFL16, HFL8, SC12, SC19, VT1, VT39 and VT41.
    6. "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.
    7. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS BETA AND GAMMA).
      Strain: Berkeley.
      Tissue: Embryo, Larva and Pupae.
    9. "Amino acid sequence of an invertebrate FBP aldolase (from Drosophila melanogaster)."
      Malek A.A., Suter F.X., Frank G., Brenner-Holzach O.
      Biochem. Biophys. Res. Commun. 126:199-205(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-361 (ISOFORM GAMMA), ACETYLATION AT THR-2.
    10. "Fructose-1,6-bisphosphate aldolase from Drosophila melanogaster: primary structure analysis, secondary structure prediction, and comparison with vertebrate aldolases."
      Malek A.A., Hy M., Honegger A., Rose K., Brenner-Holzach O.
      Arch. Biochem. Biophys. 266:10-31(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-361 (ISOFORM GAMMA).
    11. "Fructose 1,6-bisphosphate aldolase of Drosophila melanogaster: comparative sequence analyses around the substrate-binding lysyl residue."
      Brenner-Holzach O., Zumsteg C.
      Arch. Biochem. Biophys. 214:89-101(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 170-272.
    12. "Drosophila melanogaster aldolase: characterization of the isozymes alpha, beta, and gamma generated from a single gene."
      Zhang R., Kai T., Sugimoto Y., Kusakabe T., Takasaki Y., Koga K., Hori K.
      J. Biochem. 118:183-188(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    13. "The crystal structure of fructose-1,6-bisphosphate aldolase from Drosophila melanogaster at 2.5-A resolution."
      Hester G., Brenner-Holzach O., Rossi F.A., Struck-Donatz M., Winterhalter K.H., Smit J.D.G., Piontek K.
      FEBS Lett. 292:237-242(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), ACETYLATION AT THR-2.

    Entry informationi

    Entry nameiALF_DROME
    AccessioniPrimary (citable) accession number: P07764
    Secondary accession number(s): A4V3F9
    , A5XCY2, P29841, Q24236, Q24237, Q7KRY9, Q8IMS1, Q8MQQ4, Q9VBG2, Q9VBG3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 153 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3