P07764 (ALF_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fructose-bisphosphate aldolase
EC=4.1.2.13

Gene names

Name:	Ald
ORF Names:	CG6058

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Glycolysis
Coding sequence diversity	Alternative splicing
Ligand	Schiff base
Molecular function	Lyase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from direct assay PubMed 2128175. Source: FlyBase mesoderm development Non-traceable author statement PubMed 11486054. Source: FlyBase mitotic G2 DNA damage checkpoint Inferred from genetic interaction PubMed 21205937. Source: FlyBase
Cellular_component	M band Inferred from direct assay PubMed 12756285. Source: FlyBase Z disc Inferred from direct assay PubMed 12756285. Source: FlyBase
Molecular_function	fructose-bisphosphate aldolase activity Inferred from direct assay PubMed 2128175. Source: FlyBase
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9 Ref.10

Chain

2 – 361

360

Fructose-bisphosphate aldolase

PRO_0000216927

Sites

Active site

188

1

Proton acceptor By similarity

Active site

230

1

Schiff-base intermediate with dihydroxyacetone-P

Binding site

56

1

Substrate

Binding site

147

1

Substrate

Site

361

1

Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Amino acid modifications

Modified residue

2

1

N-acetylthreonine Ref.9 Ref.13

Natural variations

Alternative sequence

335 – 361

27

GDAAQ…ANHAY → SQACQGIYVPGSIPSFAGNA NLFVAQHKY in isoform Beta.

VSP_000221

Alternative sequence

336 – 361

26

DAAQG…ANHAY → EAACGNYTAGSVKGFAGKDT LHVDDHRY in isoform Alpha.

VSP_000223

Experimental info

Sequence conflict

40

1

M → H in BAA01236. Ref.1

Sequence conflict

40

1

M → H in BAA01237. Ref.1

Sequence conflict

40

1

M → H in BAA01238. Ref.1

Sequence conflict

40

1

M → H in BAA01592. Ref.4

Sequence conflict

111

1

K → E in CAA42666. Ref.3

Sequence conflict

111

1

K → E in CAA42667. Ref.3

Sequence conflict

181

1

Q → E in BAA01236. Ref.1

Sequence conflict

181

1

Q → E in BAA01237. Ref.1

Sequence conflict

181

1

Q → E in BAA01238. Ref.1

Sequence conflict

181

1

Q → E in BAA01592. Ref.4

Sequence conflict

201

1

R → G in CAA42666. Ref.3

Sequence conflict

201

1

R → G in CAA42667. Ref.3

Sequence conflict

251

1

A → T in CAA42666. Ref.3

Sequence conflict

251

1

A → T in CAA42667. Ref.3

Secondary structure

1

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361

Helix Strand Turn

Details...

Helix

10 – 23

14

Beta strand

29 – 33

5

Helix

37 – 46

10

Helix

53 – 64

12

Helix

68 – 72

5

Beta strand

74 – 79

6

Helix

81 – 84

4

Helix

94 – 100

7

Beta strand

104 – 108

5

Beta strand

113 – 115

3

Beta strand

119 – 121

3

Beta strand

123 – 125

3

Helix

131 – 140

10

Beta strand

143 – 152

10

Beta strand

155 – 157

3

Helix

161 – 180

20

Beta strand

184 – 191

8

Helix

199 – 219

21

Helix

224 – 226

3

Helix

245 – 259

15

Beta strand

266 – 269

4

Helix

276 – 286

11

Beta strand

295 – 302

8

Helix

303 – 305

3

Helix

307 – 313

7

Helix

320 – 337

18

Turn

338 – 340

3

Turn

344 – 347

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform Gamma (4C) (B) (C) (D) [UniParc]. Last modified January 23, 2007. Version 5. Checksum: D8DA46E273668CE9	FASTA	361	39,047
	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
	Isoform Alpha (4A) (E) [UniParc]. Checksum: E48CC61438C85B64	FASTA	363	39,561
	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 AKANGEAACG NYTAGSVKGF AGKDTLHVDD HRY
	Isoform Beta (4B) (H) [UniParc]. Checksum: 7B326172746BF31D	FASTA	363	39,589
	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 AKANSQACQG IYVPGSIPSF AGNANLFVAQ HKY

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

PIR

ADFFR. A42027.
A42263.
ADFF. B42027.
B42263.
C42263.
JX0233.
S68360.

RefSeq

NP_001262985.1. NM_001276056.1.
NP_524515.2. NM_079791.4.
NP_733140.2. NM_170261.2.
NP_733141.1. NM_170262.2.
NP_733142.1. NM_170263.3.
NP_733143.1. NM_170264.2.
NP_733144.3. NM_170265.3.
NP_733145.3. NM_170266.3.
NP_996300.1. NM_206577.2.

UniGene

Dm.2349.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FBA	X-ray	1.90	A/B/C/D	2-361	[»]

ProteinModelPortal

P07764.

SMR

P07764. Positions 2-361.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-782439.

Proteomic databases

PaxDb

P07764.

PRIDE

P07764.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0084994; FBpp0084367; FBgn0000064.
FBtr0084995; FBpp0084368; FBgn0000064.
FBtr0084999; FBpp0084372; FBgn0000064.
FBtr0310660; FBpp0302780; FBgn0000064.

GeneID

43183.

KEGG

dme:Dmel_CG6058.

Organism-specific databases

CTD

42126.

FlyBase

FBgn0000064. Ald.

Phylogenomic databases

eggNOG

COG3588.

GeneTree

ENSGT00390000010235.

InParanoid

P07764.

KO

K01623.

OMA

NIGTHTP.

OrthoDB

EOG4WPZJ4.

Enzyme and pathway databases

SABIO-RK

P07764.

UniPathway

UPA00109; UER00183.

Gene expression databases

Bgee

P07764.

GermOnline

CG6058. Drosophila melanogaster.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]

PANTHER

PTHR11627. PTHR11627. 1 hit.

Pfam

PF00274. Glycolytic. 1 hit.
[Graphical view]

PROSITE

PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ALD. drosophila.

EvolutionaryTrace

P07764.

GenomeRNAi

43183.

NextBio

832589.

Entry information

Entry name

ALF_DROME

Accession

Primary (citable) accession number: P07764
Secondary accession number(s): A4V3F9 , 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:	May 1, 2013
This is version 143 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project