Reviewed, UniProtKB/Swiss-Prot P81641 (AMYB_DROME)

Names and origin

Protein names

Recommended name:
    Alpha-amylase B
    EC=3.2.1.1
Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase

Gene names

Name:	Amy-d
Synonyms:	AmyB
ORF Names:	CG17876

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	494 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides.
Cofactor	Binds 1 calcium ion per subunit By similarity. Binds 1 chloride ion per subunit By similarity.
Subunit structure	Monomer By similarity.
Polymorphism	At least 6 electrophoretic isozymes are known: Amy1, Amy2, Amy3, Amy4, Amy5 and Amy6. Strains KO123 expresses Amy1; J87 expresses Amy3; 1420#1, L16 and TN256 express Amy6.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Calcium Chloride Metal-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Pyrrolidone carboxylic acid
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Ref.3 Traceable author statement. Source: UniProtKB
Molecular function	alpha-amylase activity Ref.3 Traceable author statement. Source: UniProtKB calcium ion binding Ref.3 Traceable author statement. Source: UniProtKB chloride ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18
	Chain	19 – 494	476	Alpha-amylase B		PRO_0000001365
Sites
	Active site	204	1	Nucleophile By similarity
	Active site	241	1	Proton donor By similarity
	Active site	306	1	By similarity
	Metal binding	116	1	Calcium By similarity
	Metal binding	165	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	174	1	Calcium By similarity
	Metal binding	208	1	Calcium; via carbonyl oxygen By similarity
	Binding site	202	1	Chloride By similarity
	Binding site	304	1	Chloride By similarity
	Binding site	343	1	Chloride By similarity
Amino acid modifications
	Modified residue	19	1	Pyrrolidone carboxylic acid By similarity
	Disulfide bond	46 ↔ 102		By similarity
	Disulfide bond	153 ↔ 167		By similarity
	Disulfide bond	376 ↔ 382		By similarity
	Disulfide bond	448 ↔ 460		By similarity
Natural variations
	Natural variant	6	1	Missing in strain: KN-22.
	Natural variant	11	1	A → S in strain: Berkeley, JP-5, JP-35, JP-55, JP-75, KN-12 and Oregon-R.
	Natural variant	71	1	S → R in strain: 1420#1, JP-169, JP-186, JP-190, KO123, KN-3, KN-9, KN-10, TN22 and TN256.
	Natural variant	121	1	D → E in strain: JP-55.
	Natural variant	121	1	D → G in strain: 1420#1, JP-190, JP-169, JP-186, KO123, TN22 and TN256.
	Natural variant	121	1	D → N in strain: KN-10, KN-3 and KN-9.
	Natural variant	138	1	S → T in strain: JP-75, KN-17, KN-21, KN-22 and L16.
	Natural variant	156	1	S → R in strain: 1420#1, JP-169, JP-186, JP-190, KO123, KN-3, KN-9, KN-10, TN22 and TN256.
	Natural variant	278	1	D → N in strain: 1420#1, AO168, J87, JP-60, JP-169, JP-186, JP-190, KO123, KN-3, KN-9, KN-10, TN22 and TN256.
	Natural variant	288	1	T → I in strain: KN-15.
	Natural variant	398	1	T → A in strain: Berkeley, JP-5, JP-35, JP-55, JP-60, JP-65, JP-70, JP-75, JP-169, JP-186, JP-190, KN-3, KN-9, KN-10, KN-12, KN-17, KN-21 and KN-23.
	Natural variant	401	1	S → L in strain: Berkeley, JP-5, JP-35, JP-55, JP-65, JP-70, KN-12 and KN-21.
	Natural variant	403	1	E → A in strain: 1420#1, AO168, J87, JP-60, JP-169, JP-186, JP-190, KO123, KN-3, KN-9, KN-10, TN22 and TN256.
	Natural variant	410	1	N → S in strain: Berkeley, JP-5, JP-35, JP-55, JP-65 and KN-12.
	Natural variant	465	1	V → I in strain: JP-1, JP-15, JP-84, KO140 and KN-27.
	Natural variant	476	1	Y → N in strain: 1420#1, AO168, J87, JP-1, JP-15, JP-55, JP-60, JP-75, JP-84, JP-169, JP-186, JP-190, KO123, KO140, KN-3, KN-9, KN-10, KN-15, KN-17, KN-21, KN-22, KN-23, KN-27, L16, TN22 and TN256.
	Natural variant	478	1	G → A in strain: KN-21.

Sequences

	Sequence		Length	Mass (Da)
	P81641-1 [UniParc]. Last modified December 1, 2000. Version 3. Checksum: B477CB031754C298	FASTA	494	53,795
	10 20 30 40 50 60 MFLAKSIVCL ALLAVANAQF DTNYASGRSG MVHLFEWKWD DIAAECENFL GPNGYAGVQV 70 80 90 100 110 120 SPVNENAVKD SRPWWERYQP ISYKLETRSG NEEQFASMVK RCNAVGVRTY VDVVFNHMAA 130 140 150 160 170 180 DGGTYGTGGS TASPSSKSYP GVPYSSLDFN PTCAISNYND ANEVRNCELV GLRDLNQGNS 190 200 210 220 230 240 YVQDKVVEFL DHLIDLGVAG FRVDAAKHMW PADLAVIYGR LKNLNTDHGF ASGSKAYIVQ 250 260 270 280 290 300 EVIDMGGEAI SKSEYTGLGA ITEFRHSDSI GKVFRGKDQL QYLTNWGTAW GFAASDRSLV 310 320 330 340 350 360 FVDNHDNQRG HGAGGADVLT YKVPKQYKMA SAFMLAHPFG TPRVMSSFSF TDTDQGPPTT 370 380 390 400 410 420 DGHNIASPIF NSDNSCSGGW VCEHRWRQIY NMVAFRNTVG SDEIQNWWDN GSNQISFSRG 430 440 450 460 470 480 SRGFVAFNND NYDLNSSLQT GLPAGTYCDV ISGSKSGSSC TGKTVTVGSD GRASIYIGSS 490 EDDGVLAIHV NAKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequences of the duplicated Amylase structural genes in Drosophila melanogaster." Okuyama E., Yamazaki T. Proc. Jpn. Acad., B, Phys. Biol. Sci. 64:274-277(1988) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: TN329.
[2]	"Evolutionary relationships and sequence variation of alpha-amylase variants encoded by duplicated genes in the Amy locus of Drosophila melanogaster." Inomata N., Shibata H., Okuyama E., Yamazaki T. Genetics 141:237-244(1995) [PubMed: 8536971] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 1420#1, AO168, J87, KO123, KO140, L16, TN22, TN256 and TN329.
[3]	"Molecular evolution of duplicated amylase gene regions in Drosophila melanogaster: evidence of positive selection in the coding regions and selective constraints in the cis-regulatory regions." Araki H., Inomata N., Yamazaki T. Genetics 157:667-677(2001) [PubMed: 11156987] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: JP-1, JP-15, JP-169, JP-186, JP-190, JP-35, JP-5, JP-55, JP-60, JP-65, JP-70, JP-75, JP-84, KN-10, KN-12, KN-15, KN-17, KN-21, KN-22, KN-23, KN-27, KN-3 and KN-9.
[4]	"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: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[5]	"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: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[6]	"The alpha-amylase gene in Drosophila melanogaster: nucleotide sequence, gene structure and expression motifs." Boer P.H., Hickey D.A. Nucleic Acids Res. 14:8399-8411(1986) [PubMed: 3024105] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22. Strain: Oregon-R.
[7]	"Molecular analysis of cis-regulatory sequences at the alpha-amylase locus in Drosophila melanogaster." Hawley S.A., Doane W.W., Norman R.A. Biochem. Genet. 30:257-277(1992) [PubMed: 1616481] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13. Strain: Canton-S.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X84405 Genomic DNA. Translation: CAA59126.1. L22717 Genomic DNA. Translation: AAA92227.1. L22718 Genomic DNA. Translation: AAA92228.1. L22720 Genomic DNA. Translation: AAA92230.1. L22724 Genomic DNA. Translation: AAA92232.1. L22727 Genomic DNA. Translation: AAA92233.1. L22728 Genomic DNA. Translation: AAA92242.1. L22730 Genomic DNA. Translation: AAA92237.1. L22732 Genomic DNA. Translation: AAA92243.1. L22734 Genomic DNA. Translation: AAA92238.1. AB043027 Genomic DNA. Translation: BAB32525.1. AB043028 Genomic DNA. Translation: BAB32526.1. AB043029 Genomic DNA. Translation: BAB32527.1. AB043030 Genomic DNA. Translation: BAB32528.1. AB043031 Genomic DNA. Translation: BAB32529.1. AB043032 Genomic DNA. Translation: BAB32530.1. AB043033 Genomic DNA. Translation: BAB32531.1. AB043034 Genomic DNA. Translation: BAB32532.1. AB043035 Genomic DNA. Translation: BAB32533.1. AB043036 Genomic DNA. Translation: BAB32534.1. AB043037 Genomic DNA. Translation: BAB32535.1. AB043039 Genomic DNA. Translation: BAB32537.1. AB043040 Genomic DNA. Translation: BAB32538.1. AB043041 Genomic DNA. Translation: BAB32539.1. AB043042 Genomic DNA. Translation: BAB32540.1. AB043043 Genomic DNA. Translation: BAB32541.1. AB043044 Genomic DNA. Translation: BAB32542.1. AB043045 Genomic DNA. Translation: BAB32543.1. AB043046 Genomic DNA. Translation: BAB32544.1. AB043047 Genomic DNA. Translation: BAB32545.1. AB043049 Genomic DNA. Translation: BAB72141.1. AB043050 Genomic DNA. Translation: BAB72142.1. AB043051 Genomic DNA. Translation: BAB72143.1. AE013599 Genomic DNA. Translation: AAF57894.1. X04570 Genomic DNA. Translation: CAA28239.1. X84410 Genomic DNA. Translation: CAA59130.1.
PIR	S58951. S58954. S58959. S58960. S58962. S58964.
RefSeq	NP_523768.1.
UniGene	Dm.18520
3D structure databases
HSSP	HSSP built from PDB template 1JAE based on UniProtKB P56634.
ModBase	Search...
Protein-protein interaction databases
IntAct	P81641. 2 interactions.
STRING	P81641.
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
Genome annotation databases
Ensembl	FBtr0086983; FBpp0086136; FBgn0000078; Drosophila melanogaster. [Genome view]
GeneID	36932.
KEGG	dme:Dmel_CG17876.
Organism-specific databases
CTD	36932.
FlyBase	FBgn0000078. Amy-d.
Enzyme and pathway databases
BRENDA	3.2.1.1. 48.
Gene expression databases
GermOnline	CG18730. Drosophila melanogaster.
Family and domain databases
InterPro	IPR006048. A-amylase_b_C. IPR006046. Glyco_hydro_13. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat. IPR006589. Glyco_hydro_13_sub_cat. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF02806. Alpha-amylase_C. 1 hit. [Graphical view]
PRINTS	PR00110. ALPHAAMYLASE.
SMART	SM00642. Aamy. 1 hit. SM00632. Aamy_C. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	801098.

Entry information

Entry name

AMYB_DROME

Accession

Primary (citable) accession number: P81641
Secondary accession number(s): Q27578 , Q27581, Q27585, Q27882, Q27885, Q27897, Q8WP56, Q95NK4, Q969D1, Q9BH39, Q9BH72, Q9BPS5, Q9BPS6, Q9BPS7, Q9BPS8, Q9BPT0, Q9BPT1, Q9BPT2, Q9BPT3, Q9V7Z0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	September 1, 2009
This is version 86 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project