Q45101 (O16G_BACCO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Oligo-1,6-glucosidase
EC=3.2.1.10

Alternative name(s):
Dextrin 6-alpha-D-glucanohydrolase
Oligosaccharide alpha-1,6-glucosidase
Sucrase-isomaltase
Short name=Isomaltase

Gene names

Name:

malL

Organism

Bacillus coagulans

Taxonomic identifier

1398 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	555 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cation binding Inferred from electronic annotation. Source: InterPro oligo-1,6-glucosidase 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 – 555	555	Oligo-1,6-glucosidase		PRO_0000054314
Sites
	Active site	199	1	Nucleophile By similarity
	Active site	255	1	Proton donor By similarity
	Site	332	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q45101 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: CE2BB1D7B4E226D8	FASTA	555	64,991
	10 20 30 40 50 60 MTEWWKKAVV YQIYPRSFYD TNGDGIGDLR GIMDKLDYLK TLGIDCIWIS PVYDSPQDDN 70 80 90 100 110 120 GYDIRDYRKI DKMFGTNEDM DRLLDEAHAR GIKIVMDLVV NHTSDEHAWF VESRKSKDNP 130 140 150 160 170 180 YRDFYFWKDP KPDGTPPNNW GSMFSGSAWE YDETTGQYYL HYFSKKQPDL NWENEKVRKE 190 200 210 220 230 240 IYDMMKFWMD KGVDGWRMDV IGSISKFLDF PDYELPEGQK YGIGKYHANG PRLHAFIQEM 250 260 270 280 290 300 NREVLSKYDC MTVGEAIGSD VEIARKYTGP DRHELNMIFN FEHMDVDTKP GSPAGKWALK 310 320 330 340 350 360 PFDLVELKQI LSRWQYELAD TGWNALYFEN HDQARVVSRW GNDTTYRAEC AKAFATILHG 370 380 390 400 410 420 LKGTPFIYQG EEIGMVNADL ELEEYDDIEI RNAYQELVME NQIMSKDEFL TAVRKKGRDN 430 440 450 460 470 480 ARTPMQWDGS FNAGFTTGTP WLKVNSRYSE INVAKALQEP DSIFYYYQSL IKLRHSYDVF 490 500 510 520 530 540 TDGRYELLMP DHPHLYVYTR ENESEKLLVA ANLSENTVSF DQPDDNWKLL LGNYEDTGTS 550 TLFRPYEAAI YYLEK

References

[1]

"Analysis of the critical sites for protein thermostabilization by proline substitution in oligo-1,6-glucosidase from Bacillus coagulans ATCC 7050 and the evolutionary consideration of proline residues." Watanabe K., Kitamura K., Suzuki Y. Appl. Environ. Microbiol. 62:2066-2073(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 7050 / DSM 1 / JCM 2257 / NCIB 9365 / NCTC 10334.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D78342 Genomic DNA. Translation: BAA11354.1.
3D structure databases
ProteinModelPortal	Q45101.
SMR	Q45101. Positions 2-554.
ModBase	Search...
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	2.60.40.1180. 1 hit. 3.20.20.80. 2 hits.
InterPro	IPR022567. DUF3459. IPR015902. Glyco_hydro_13. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat_dom. IPR006589. Glyco_hydro_13_sub_cat_dom. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
PANTHER	PTHR10357. PTHR10357. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF11941. DUF3459. 1 hit. [Graphical view]
SMART	SM00642. Aamy. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

O16G_BACCO

Accession

Primary (citable) accession number: Q45101

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program