Reviewed, UniProtKB/Swiss-Prot Q08341 (CDAS_BACSH)

Names and origin

Protein names	Recommended name:     Cyclomaltodextrinase       Short name=CDase     EC=3.2.1.54 Alternative name(s):     Cyclomaltodextrin hydrolase, decycling
Organism	Bacillus sphaericus
Taxonomic identifier	1421 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Planococcaceae › Lysinibacillus

Protein attributes

Sequence length	591 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hydrolyzes cyclodextrins. Can also act on linear maltodextrins, with the exception of maltose.
Catalytic activity	Cyclomaltodextrin + H2O = linear maltodextrin.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subunit structure	Monomer.
Induction	By cyclodextrins.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.
biophysicochemical properties	pH dependence: Optimum pH is 8.0. Temperature dependence: Optimum temperature is 45 degrees Celsius.

Ontologies

Keywords
Ligand	Calcium Metal-binding
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW cyclomaltodextrinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 591	591	Cyclomaltodextrinase		PRO_0000054308
Sites
	Active site	327	1	Nucleophile By similarity
	Active site	356	1	Proton donor By similarity
	Active site	423	1	By similarity
	Metal binding	146	1	Calcium By similarity
	Metal binding	148	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	151	1	Calcium By similarity
	Metal binding	152	1	Calcium By similarity
	Metal binding	170	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	172	1	Calcium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q08341-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 702FD7BA99A23E3F	FASTA	591	67,899
	10 20 30 40 50 60 MIMLEAVYHR MGQNWSYAYN DSTLHIRIRT KRDNVPRIDL HCGEKYDPEK YKETIPMERM 70 80 90 100 110 120 ASDGLFDYWQ AAVQPRYRRL VYYFALHSDN GDAVYFMEKG FFDQPPKVMY EGLFDFPYLN 130 140 150 160 170 180 RQDVHTPPAW VKEAIFYQIF PERFANGDPS NDPEGVQEWG GTPSAGNFFG GDLQGVIDHL 190 200 210 220 230 240 DYLSDLGVNA LYFNPLFAAT TNHKYDTADY MKIDPQFGTN EKLKELVDAC HARGMRVLLD 250 260 270 280 290 300 AVFNHCGHTF PPFVDVLNNG LNSRYADWFH VREWPLRVVD GIPTYDTFAF EPIMPKLNTG 310 320 330 340 350 360 NEEVKAYLLN VGRYWLEEMG LDGWRLDVAN EVDHQFWREF RSEIKRINPS AYILGEIMHD 370 380 390 400 410 420 SMPWLQGDQF DAVMNYPFTN ILLNFFARRL TNAAEFAQAI GTQLAGYPQQ VTEVSFNLLG 430 440 450 460 470 480 SHDTTRLLTL CSGNVERMKL ATLFQLTYQG TPCIYYGDEI GMDGEYDPLN RKCMEWDKSK 490 500 510 520 530 540 QNTELLAFFR SMISLRKAHP ALRGSGLRFL PVLEHPQLLV YERWDDNERF LIMLNNEDAP 550 560 570 580 590 VNVVIPAAQP GASWRTVNGE PCAVVEESSI QAALPPYGYA ILHAPIAGTA E

References

[1]

"Cloning and sequence analysis of the cyclomaltodextrinase gene from Bacillus sphaericus and expression in Escherichia coli cells." Oguma T., Matsuyama A., Kikuchi M., Nakano E. Appl. Microbiol. Biotechnol. 39:197-203(1993) [PubMed: 7763728] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: E-244.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X62576 Genomic DNA. Translation: CAA44454.1.
PIR	S48130.
3D structure databases
HSSP	HSSP built from PDB template 1EA9 based on UniProtKB Q59226.
ModBase	Search...
Protein family/group databases
CAZy	CBM34. Carbohydrate-Binding Module Family 34. GH13. Glycoside Hydrolase Family 13.
Enzyme and pathway databases
BRENDA	3.2.1.54. 327.
Family and domain databases
InterPro	IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat. IPR004185. Glyco_hydro_13_lg-like. IPR006589. Glyco_hydro_13_sub_cat. IPR013781. Glyco_hydro_sg_catalytic. IPR013783. Ig-like_fold. [Graphical view]
Gene3D	G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF02903. Alpha-amylase_N. 1 hit. [Graphical view]
SMART	SM00642. Aamy. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CDAS_BACSH

Accession

Primary (citable) accession number: Q08341

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 57 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)