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P07764

- ALF_DROME

UniProt

P07764 - ALF_DROME

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Protein

Fructose-bisphosphate aldolase

Gene

Ald

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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.
ExpressionAtlasiP07764. differential.

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.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view]
PANTHERiPTHR11627. PTHR11627. 1 hit.
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

        10         20         30         40         50
MTTYFNYPSK ELQDELREIA QKIVAPGKGI LAADESGPTM GKRLQDIGVE
60 70 80 90 100
NTEDNRRAYR QLLFSTDPKL AENISGVILF HETLYQKADD GTPFAEILKK
110 120 130 140 150
KGIILGIKVD KGVVPLFGSE DEVTTQGLDD LAARCAQYKK DGCDFAKWRC
160 170 180 190 200
VLKIGKNTPS YQSILENANV LARYASICQS QRIVPIVEPE VLPDGDHDLD
210 220 230 240 250
RAQKVTETVL AAVYKALSDH HVYLEGTLLK PNMVTAGQSA KKNTPEEIAL
260 270 280 290 300
ATVQALRRTV PAAVTGVTFL SGGQSEEEAT VNLSAINNVP LIRPWALTFS
310 320 330 340 350
YGRALQASVL RAWAGKKENI AAGQNELLKR AKANGDAAQG KYVAGSAGAG
360
SGSLFVANHA Y
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_079791.5. [P07764-2]
NP_733140.2. NM_170261.3. [P07764-3]
NP_733141.1. NM_170262.2. [P07764-1]
NP_733142.1. NM_170263.4. [P07764-1]
NP_733143.1. NM_170264.3. [P07764-1]
NP_733144.3. NM_170265.4. [P07764-1]
NP_733145.3. NM_170266.4. [P07764-2]
NP_996300.1. NM_206577.3. [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_079791.5. [P07764-2 ]
NP_733140.2. NM_170261.3. [P07764-3 ]
NP_733141.1. NM_170262.2. [P07764-1 ]
NP_733142.1. NM_170263.4. [P07764-1 ]
NP_733143.1. NM_170264.3. [P07764-1 ]
NP_733144.3. NM_170265.4. [P07764-1 ]
NP_733145.3. NM_170266.4. [P07764-2 ]
NP_996300.1. NM_206577.3. [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.
ExpressionAtlasi P07764. differential.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view ]
PANTHERi PTHR11627. PTHR11627. 1 hit.
Pfami PF00274. Glycolytic. 1 hit.
[Graphical view ]
PROSITEi PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 29, 2014
This is version 154 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