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P07764 (ALF_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase

EC=4.1.2.13
Gene names
Name:Ald
ORF Names:CG6058
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.12

Catalytic activity

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Ref.12

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

Subunit structure

Homotetramer. Ref.12

Tissue specificity

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. Ref.1 Ref.12

Developmental stage

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. Ref.12

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.2-7.8 for isozyme alpha, and 7.2-7.5 for isozymes beta and gamma. Ref.12

Temperature dependence:

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.

Sequence caution

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.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

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)

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.
Isoform Alpha (identifier: P07764-2)

Also known as: 4A; E;

The sequence of this isoform differs from the canonical sequence as follows:
     336-361: DAAQGKYVAGSAGAGSGSLFVANHAY → EAACGNYTAGSVKGFAGKDTLHVDDHRY
Isoform Beta (identifier: P07764-3)

Also known as: 4B; H;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9 Ref.10
Chain2 – 361360Fructose-bisphosphate aldolase
PRO_0000216927

Sites

Active site1881Proton acceptor By similarity
Active site2301Schiff-base intermediate with dihydroxyacetone-P
Binding site561Substrate
Binding site1471Substrate
Site3611Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Amino acid modifications

Modified residue21N-acetylthreonine Ref.9 Ref.13

Natural variations

Alternative sequence335 – 36127GDAAQ…ANHAY → SQACQGIYVPGSIPSFAGNA NLFVAQHKY in isoform Beta.
VSP_000221
Alternative sequence336 – 36126DAAQG…ANHAY → EAACGNYTAGSVKGFAGKDT LHVDDHRY in isoform Alpha.
VSP_000223

Experimental info

Sequence conflict401M → H in BAA01236. Ref.1
Sequence conflict401M → H in BAA01237. Ref.1
Sequence conflict401M → H in BAA01238. Ref.1
Sequence conflict401M → H in BAA01592. Ref.4
Sequence conflict1111K → E in CAA42666. Ref.3
Sequence conflict1111K → E in CAA42667. Ref.3
Sequence conflict1811Q → E in BAA01236. Ref.1
Sequence conflict1811Q → E in BAA01237. Ref.1
Sequence conflict1811Q → E in BAA01238. Ref.1
Sequence conflict1811Q → E in BAA01592. Ref.4
Sequence conflict2011R → G in CAA42666. Ref.3
Sequence conflict2011R → G in CAA42667. Ref.3
Sequence conflict2511A → T in CAA42666. Ref.3
Sequence conflict2511A → T in CAA42667. Ref.3

Secondary structure

....................................................... 361
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Gamma (4C) (B) (C) (D) [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: D8DA46E273668CE9

FASTA36139,047
        10         20         30         40         50         60 
MTTYFNYPSK ELQDELREIA QKIVAPGKGI LAADESGPTM GKRLQDIGVE NTEDNRRAYR 

        70         80         90        100        110        120 
QLLFSTDPKL AENISGVILF HETLYQKADD GTPFAEILKK KGIILGIKVD KGVVPLFGSE 

       130        140        150        160        170        180 
DEVTTQGLDD LAARCAQYKK DGCDFAKWRC VLKIGKNTPS YQSILENANV LARYASICQS 

       190        200        210        220        230        240 
QRIVPIVEPE VLPDGDHDLD RAQKVTETVL AAVYKALSDH HVYLEGTLLK PNMVTAGQSA 

       250        260        270        280        290        300 
KKNTPEEIAL ATVQALRRTV PAAVTGVTFL SGGQSEEEAT VNLSAINNVP LIRPWALTFS 

       310        320        330        340        350        360 
YGRALQASVL RAWAGKKENI AAGQNELLKR AKANGDAAQG KYVAGSAGAG SGSLFVANHA 


Y 

« Hide

Isoform Alpha (4A) (E) [UniParc].

Checksum: E48CC61438C85B64
Show »

FASTA36339,561
Isoform Beta (4B) (H) [UniParc].

Checksum: 7B326172746BF31D
Show »

FASTA36339,589

References

« Hide 'large scale' references
[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]"Adaptive evolution of metabolic pathways in Drosophila."
Flowers J., Sezgin E., Kumagai S., Duvernell D., Matzkin L., Schmidt P., Eanes W.
Mol. Biol. Evol. 24:1347-1354(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[8]"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] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRADFFR. A42027.
A42263.
ADFF. B42027.
B42263.
C42263.
JX0233.
S68360.
RefSeqNP_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]
UniGeneDm.2349.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FBAX-ray1.90A/B/C/D2-361[»]
ProteinModelPortalP07764.
SMRP07764. Positions 2-361.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid68080. 88 interactions.
MINTMINT-782439.

Proteomic databases

PaxDbP07764.
PRIDEP07764.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0084994; FBpp0084367; FBgn0000064. [P07764-1]
FBtr0084995; FBpp0084368; FBgn0000064. [P07764-1]
FBtr0084999; FBpp0084372; FBgn0000064. [P07764-1]
FBtr0310660; FBpp0302780; FBgn0000064. [P07764-1]
GeneID43183.
KEGGdme:Dmel_CG6058.

Organism-specific databases

CTD42126.
FlyBaseFBgn0000064. Ald.

Phylogenomic databases

eggNOGCOG3588.
GeneTreeENSGT00390000010235.
InParanoidP07764.
KOK01623.
OMAMLFRSDD.
OrthoDBEOG744T94.
PhylomeDBP07764.

Enzyme and pathway databases

SABIO-RKP07764.
UniPathwayUPA00109; UER00183.

Gene expression databases

BgeeP07764.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERPTHR11627. PTHR11627. 1 hit.
PfamPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALD. drosophila.
EvolutionaryTraceP07764.
GenomeRNAi43183.
NextBio832589.

Entry information

Entry nameALF_DROME
AccessionPrimary (citable) accession number: P07764
Secondary accession number(s): A4V3F9 expand/collapse secondary AC list , A5XCY2, P29841, Q24236, Q24237, Q7KRY9, Q8IMS1, Q8MQQ4, Q9VBG2, Q9VBG3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 151 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase