Reviewed, UniProtKB/Swiss-Prot P00691 (AMY_BACSU)

Names and origin

Protein names

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

Gene names

Name:	amyE
Synonyms:	amyA
Ordered Locus Names:	BSU03040

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	659 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)

Catalytic activity	Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides.
Cofactor	Binds 2 calcium ions per subunit.
Subunit structure	Monomer.
Subcellular location	Secreted.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alpha-amylase activity Inferred from electronic annotation. Source: EC calcium 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 – 27

27

Propeptide

28 – 41

14

PRO_0000001335

Chain

42 – 659

618

Alpha-amylase

PRO_0000001336

Sites

Active site

217

1

Nucleophile By similarity

Active site

249

1

Proton donor By similarity

Active site

310

1

By similarity

Metal binding

142

1

Calcium 1

Metal binding

178

1

Calcium 1; via carbonyl oxygen

Metal binding

187

1

Calcium 1

Metal binding

210

1

Calcium 2; via carbonyl oxygen

Metal binding

212

1

Calcium 2

Metal binding

221

1

Calcium 1; via carbonyl oxygen

Natural variations

Natural variant

469 – 477

9

AKAPHVFLE → EMRCNTFFQ in strain: N7 AMYEN+.

Natural variant

478 – 659

182

Missing in strain: N7 AMYEN+.

Experimental info

Sequence conflict

22

1

H → Y in CAA26086. Ref.2

Sequence conflict

22

1

H → Y in AAA22234. Ref.6

Sequence conflict

22

1

H → Y in CAA23436. Ref.7

Sequence conflict

22

1

H → Y in AAA22230. Ref.8

Sequence conflict

146

1

S → F in CAA26086. Ref.2

Sequence conflict

146

1

S → F in AAA22234. Ref.6

Sequence conflict

204

1

D → E in CAA26086. Ref.2

Sequence conflict

204

1

D → E in AAA22234. Ref.6

Sequence conflict

284

1

N → K in CAA26086. Ref.2

Sequence conflict

332

1

A → S in AAA22234. Ref.6

Sequence conflict

513 – 529

17

ETAFK…GKGDP → DDRRLRMEINSQSEKEIQ in CAA23437. Ref.1

Sequence conflict

513 – 529

17

ETAFK…GKGDP → DDRRLRMEINSQSEKEIQ in BAA08938. Ref.3

Secondary structure

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659

Helix Strand Turn

Details...

Turn

47 – 49

3

Beta strand

52 – 54

3

Helix

60 – 65

6

Helix

67 – 72

6

Beta strand

76 – 80

5

Beta strand

84 – 86

3

Helix

90 – 92

3

Helix

96 – 103

8

Beta strand

105 – 112

8

Turn

113 – 115

3

Helix

118 – 129

12

Turn

130 – 132

3

Beta strand

134 – 139

6

Turn

148 – 150

3

Helix

153 – 156

4

Beta strand

162 – 164

3

Helix

174 – 179

6

Beta strand

180 – 182

3

Helix

193 – 208

16

Beta strand

213 – 216

4

Helix

219 – 221

3

Helix

228 – 230

3

Helix

234 – 238

5

Beta strand

244 – 248

5

Helix

258 – 262

5

Beta strand

265 – 268

4

Helix

270 – 282

13

Helix

287 – 290

4

Beta strand

294 – 297

4

Helix

299 – 301

3

Beta strand

302 – 304

3

Helix

309 – 313

5

Helix

324 – 335

12

Beta strand

337 – 345

9

Helix

369 – 372

4

Helix

374 – 386

13

Helix

396 – 398

3

Beta strand

402 – 407

6

Turn

408 – 410

3

Beta strand

411 – 416

6

Beta strand

418 – 420

3

Beta strand

422 – 427

6

Beta strand

432 – 436

5

Beta strand

443 – 447

5

Beta strand

450 – 455

6

Beta strand

459 – 463

5

Sequences

	Sequence		Length	Mass (Da)
	P00691-1 [UniParc]. Last modified June 16, 2009. Version 2. Checksum: 16BD6CB1E7C67BD6	FASTA	659	72,378
	10 20 30 40 50 60 MFAKRFKTSL LPLFAGFLLL FHLVLAGPAA ASAETANKSN ELTAPSIKSG TILHAWNWSF 70 80 90 100 110 120 NTLKHNMKDI HDAGYTAIQT SPINQVKEGN QGDKSMSNWY WLYQPTSYQI GNRYLGTEQE 130 140 150 160 170 180 FKEMCAAAEE YGIKVIVDAV INHTTSDYAA ISNEVKSIPN WTHGNTQIKN WSDRWDVTQN 190 200 210 220 230 240 SLLGLYDWNT QNTQVQSYLK RFLDRALNDG ADGFRFDAAK HIELPDDGSY GSQFWPNITN 250 260 270 280 290 300 TSAEFQYGEI LQDSASRDAA YANYMDVTAS NYGHSIRSAL KNRNLGVSNI SHYASDVSAD 310 320 330 340 350 360 KLVTWVESHD TYANDDEEST WMSDDDIRLG WAVIASRSGS TPLFFSRPEG GGNGVRFPGK 370 380 390 400 410 420 SQIGDRGSAL FEDQAITAVN RFHNVMAGQP EELSNPNGNN QIFMNQRGSH GVVLANAGSS 430 440 450 460 470 480 SVSINTATKL PDGRYDNKAG AGSFQVNDGK LTGTINARSV AVLYPDDIAK APHVFLENYK 490 500 510 520 530 540 TGVTHSFNDQ LTITLRADAN TTKAVYQINN GPETAFKDGD QFTIGKGDPF GKTYTIMLKG 550 560 570 580 590 600 TNSDGVTRTE KYSFVKRDPA SAKTIGYQNP NHWSQVNAYI YKHDGSRVIE LTGSWPGKPM 610 620 630 640 650 TKNADGIYTL TLPADTDTTN AKVIFNNGSA QVPGQNQPGF DYVLNGLYND SGLSGSLPH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the amylase gene from Bacillus subtilis." Yang M., Galizzi A., Henner D.J. Nucleic Acids Res. 11:237-249(1983) [PubMed: 6186986] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"Changes in the properties and molecular weights of Bacillus subtilis M-type and N-type alpha-amylases resulting from a spontaneous deletion." Yamane K., Hirata Y., Furusato T., Yamazaki H., Nakayama A. J. Biochem. 96:1849-1858(1984) [PubMed: 6099357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: N7 AMYEN+.
[3]	"The 25 degrees-36 degrees region of the Bacillus subtilis chromosome: determination of the sequence of a 146 kb segment and identification of 113 genes." Yamane K., Kumano M., Kurita K. Microbiology 142:3047-3056(1996) [PubMed: 8969502] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[4]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[5]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 0:0-0(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 513-529.
[6]	"Alpha-amylase genes (amyR2 and amyE+) from an alpha-amylase-hyperproducing Bacillus subtilis strain: molecular cloning and nucleotide sequences." Yamazaki H., Ohmura K., Nakayama A., Takeichi Y., Otozai K., Yamasaki M., Tamura G., Yamane K. J. Bacteriol. 156:327-337(1983) [PubMed: 6413492] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-557.
[7]	"Nucleotide sequence of the promoter and NH2-terminal signal peptide region of Bacillus subtilis alpha-amylase gene cloned in pUB110." Ohmura K., Yamazaki H., Takeichi Y., Nakayama A., Otozai K., Yamane K., Yamasaki M., Tamura G. Biochem. Biophys. Res. Commun. 112:678-683(1983) [PubMed: 6189486] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.
[8]	"Molecular cloning and expression of an alpha-amylase gene from an alpha-amylase extrahyper producing Bacillus subtilis." Emori M., Tojo T., Maruo B. Agric. Biol. Chem. 52:399-406(1988) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43. Strain: 168 / 2633.
[9]	"Membrane-bound and soluble extracellular alpha-amylase from Bacillus subtilis." Mantsala P., Zalkin H. J. Biol. Chem. 254:8540-8547(1979) [PubMed: 112102] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-58.
[10]	"Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus subtilis complexed with maltopentaose." Fujimoto Z., Takase K., Doui N., Momma M., Matsumoto T., Mizuno H. J. Mol. Biol. 277:393-407(1998) [PubMed: 9514750] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 42-466.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

V00101 Genomic DNA. Translation: CAA23437.1.
V00100 Genomic DNA. Translation: CAA23436.1.
D50453 Genomic DNA. Translation: BAA08938.1.
AL009126 Genomic DNA. Translation: CAB12098.2.
K00563 Genomic DNA. Translation: AAA22234.1.
X02150 Genomic DNA. Translation: CAA26086.1.
M35517 Genomic DNA. Translation: AAA22230.1.

PIR

ALBS. A00842.
ALBSNA. A91793.

RefSeq

NP_388186.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BAG	X-ray	2.50	A	42-466	[»]
1UA7	X-ray	2.21	A	45-466	[»]

ModBase

Search...

Protein family/group databases

CAZy

CBM26. Carbohydrate-Binding Module Family 26.
GH13. Glycoside Hydrolase Family 13.

Genome annotation databases

GeneID

938356.

GenomeReviews

Gene locus BSU03040 in contig AL009126_GR.

KEGG

bsu:BSU03040.

NMPDR

fig|224308.1.peg.305.

Organism-specific databases

SubtiList

BG10473. amyE. [Micado]

CMR

Search...

Phylogenomic databases

HOGENOM

P00691.

OMA

P00691. AKHIELP.

Enzyme and pathway databases

BioCyc

BSUB224308:BSU0305-MON.

BRENDA

3.2.1.1. 150.

Family and domain databases

InterPro

IPR006048. A-amylase_b_C.
IPR006046. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_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

SM00632. Aamy_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AMY_BACSU

Accession

Primary (citable) accession number: P00691

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	June 16, 2009
Last modified:	June 16, 2009
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)