Reviewed, UniProtKB/Swiss-Prot P06547 (AMYB_BACCI)

Names and origin

Protein names	Recommended name:     Beta-amylase     EC=3.2.1.2 Alternative name(s):     1,4-alpha-D-glucan maltohydrolase
Organism	Bacillus circulans
Taxonomic identifier	1397 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	575 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	Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.
Subunit structure	Monomer.
Sequence similarities	Belongs to the glycosyl hydrolase 14 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	beta-amylase activity Inferred from electronic annotation. Source: EC cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 36	36
	Chain	37 – 575	539	Beta-amylase		PRO_0000001454
Sites
	Active site	199	1	By similarity
	Active site	395	1	By similarity
Amino acid modifications
	Disulfide bond	119 ↔ 127		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P06547-1 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 724E8C0D66B4A258	FASTA	575	62,899
	10 20 30 40 50 60 MLHSQKRIWK KIGLCLLSFI LGITVFTGSF GSKAEAAVAG DFQVSVMGPL AKVTDWNSFK 70 80 90 100 110 120 NQLTTLKNNG VYAITTDVWW GYVESAGDNQ FDWSYYKTYA DTVKQAGLKW VPIISTHRCG 130 140 150 160 170 180 GNVGDDCNIP LPSWLWSKGS ADEMQFKDES GYVNNESLSP FWSGVGKQYD ELYASFAQNF 190 200 210 220 230 240 SAYKDMIPKI YLSGGPSGEL RYPSYYPAAG WSYPARGKFQ VYTETAKSAF RTAMTTKYGS 250 260 270 280 290 300 LDKINAAWGT NLTSMSQISP PTDSDGFYTG GGYNITYGKD FLSWYQSVLE NHLGVIGAAA 310 320 330 340 350 360 HKNFDPVFGV RIGAKISGIH WQMNNPSMPH SAEHAGGYYD YNRLIQKFKD TDLDLTFTAL 370 380 390 400 410 420 EMYDSGTAPN YSLPSTLVDT VSSIANSKGV RLNGENALPT GGSGFQKIEE KITRFGYNGF 430 440 450 460 470 480 TLLRINNIVN SDGSPTAEMS SFKNYVIKHA KPAGDGGGNP VNSVTIYYKK GFNSPYIHYR 490 500 510 520 530 540 PAGGTWTDVP GVKMPDSEIS GYAKITLDIG SASQLEAAFN DGNNQWDSNN MRNYFFSPGT 550 560 570 STYIPGTNGT AGSIQAGPPI TSSDFQALPA YEMSI

References

[1]	"Molecular cloning and characterization of the beta-amylase gene from Bacillus circulans." Siggens K.W. Mol. Microbiol. 1:86-91(1987) [PubMed: 2455212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NCIB 11033.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y00523 Genomic DNA. Translation: CAA68578.1.
PIR	S03745.
3D structure databases
SMR	P06547. Positions 35-544.
ModBase	Search...
Protein family/group databases
CAZy	CBM25. Carbohydrate-Binding Module Family 25. GH14. Glycoside Hydrolase Family 14.
Enzyme and pathway databases
BRENDA	3.2.1.2. 1207.
Family and domain databases
InterPro	IPR005085. Carb-bd_dom_fam25. IPR001554. Glyco_hydro_14. IPR018238. Glyco_hydro_14_CS. IPR000125. Glyco_hydro_14A_bac. IPR017853. Glyco_hydro_catalytic_core. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF03423. CBM_25. 1 hit. PF01373. Glyco_hydro_14. 1 hit. [Graphical view]
PRINTS	PR00750. BETAAMYLASE. PR00841. GLHYDLASE14A.
PROSITE	PS00506. BETA_AMYLASE_1. 1 hit. PS00679. BETA_AMYLASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMYB_BACCI

Accession

Primary (citable) accession number: P06547

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	January 19, 2010
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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