O86960 (AGLA_THENE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-glucosidase
EC=3.2.1.20

Alternative name(s):
Maltase

Gene names

Name:

aglA

Organism

Thermotoga neapolitana

Taxonomic identifier

2337 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Thermotogae › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	480 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Is able to hydrolyze diverse types of alpha-glycoside bonds in di- and trisaccharides: alpha-1,4 bonds of maltose and maltotriose, alpha-1,1 bonds of trehalose, alpha-1,2 bonds of sucrose, alpha-1,3 bonds of turanose and melizitose, alpha-1,6 bonds of isomaltose and melibiose. AglA is not specific with respect to the configuration at the C-4 position of its substrates because it also possesses alpha-galactosidase activity. Acts on the substrate from the non-reducing end of the chain. The activity of AglA drops with increasing length of the saccharide chain. Does not hydrolyze alpha-, beta-, and gamma-cyclodextrins or polysaccharides (starch, pullulan, amylose, amylopectin, glycogen). Does not cleave beta-glycosidic bonds in di-, oligo-, or polysaccharides. Ref.2
Catalytic activity	Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose. Ref.2
Cofactor	Binds 1 NAD per subunit. Ref.2 Binds 1 manganese ion per subunit. Ref.2
Enzyme regulation	Inhibited by EDTA in vitro. Ref.2
Subunit structure	Homodimer. Ref.2
Sequence similarities	Belongs to the glycosyl hydrolase 4 family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.5. Ref.2 Temperature dependence: Optimum temperature is 85 degrees Celsius. Retains 80% activity after incubation at 85 degrees Celsius for 3 hours.
Sequence caution	The sequence CAA08868.1 differs from that shown. Reason: Frameshift at position 459.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	Manganese Metal-binding NAD
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	maltose alpha-glucosidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 480	480	Alpha-glucosidase		PRO_0000415284
Regions
	Nucleotide binding	4 – 70	67	NAD By similarity
Sites
	Active site	175	1	Proton donor By similarity
	Active site	260	1	Proton acceptor By similarity
	Metal binding	174	1	Manganese By similarity
	Metal binding	203	1	Manganese By similarity
	Binding site	119	1	Substrate By similarity
	Binding site	153	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O86960 [UniParc]. Last modified January 25, 2012. Version 2. Checksum: 93A471746B46B21B	FASTA	480	54,901
	10 20 30 40 50 60 MPAVKIGIIG AGSAVFSLRL VSDLCKTPGL SGSTVTLMDI DEERLDAVLT IAKKYVEEVG 70 80 90 100 110 120 ADLKFEKTTS VDEAIADADF VINTAMVGGH TYLEKVRRIS EKYGYYRGID AQEFNMVSDY 130 140 150 160 170 180 YTFSNYNQLK YFVDIARKIE RLSPKAWYSA AANPVFEGTT LVTRTVPIKA VGFCHGHYGV 190 200 210 220 230 240 MEIIEKLGLE RKQVDWQVAG VNHGIWLNRF RYNGEDAYPL LPRWISEKSK DWKPENPFND 250 260 270 280 290 300 QLSPAAIDMY KFYGVMPIGD TVRNASWRYH RDLETKKRWY GEPWGGADSE IGWKWYQDTL 310 320 330 340 350 360 GKVTDITKKV AKFIKENPAL KLSDLGSVLG KDLSEKQFVL EVEKILDPEK KSGEQHISFH 370 380 390 400 410 420 DALLNDNRSR FVINIPNKGI IQGIDDDVVV EVPAVVDRDG IHPEKIDPPL PERVVKYYLR 430 440 450 460 470 480 PRIMRMEMAL EAFLTGDIRI IKEVLYRDPR TKSDEQVEKV IEEILSLPEN EEMRKNYLKK

References

[1]

"Thermotoga neapolitana gene clusters participating in degradation of starch and maltodextins: molecular structure of the locus." Berezina O.V., Lunina N.A., Zverlov V.V., Naumoff D.G., Liebl W., Velikodvorskaya G.A. Mol. Biol. (Mosk.) 37:801-809(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Z2706-MC24.

[2]

"Thermotoga neopolitina gene cluster, participating in degradation of starch and maltodextrins: expression of aglB and aglA gene in Escherichia coli, properties of recombinant enzymes." Lunina N.A., Berezina O.V., Veith B., Zverlov V.V., Vorob'eva I.P., Chekanovskaia L.A., Khromov I.S., Raash G., Libel W., Velikodvorskaia G.A. Mol. Biol. (Mosk.) 37:810-819(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT. Strain: Z2706-MC24.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ009832 Genomic DNA. Translation: CAA08868.1. Frameshift.
3D structure databases
HSSP	HSSP built from PDB template 1OBB based on UniProtKB O33830.
ModBase	Search...
Protein family/group databases
CAZy	GH4. Glycoside Hydrolase Family 4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.40.50.720. 1 hit. 3.90.110.10. 2 hits.
InterPro	IPR001088. Glyco_hydro_4. IPR022616. Glyco_hydro_4_C. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR016040. NAD(P)-bd_dom. [Graphical view]
Pfam	PF02056. Glyco_hydro_4. 1 hit. PF11975. Glyco_hydro_4C. 1 hit. [Graphical view]
PRINTS	PR00732. GLHYDRLASE4.
SUPFAM	SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AGLA_THENE

Accession

Primary (citable) accession number: O86960

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 25, 2012
Last sequence update:	January 25, 2012
Last modified:	March 6, 2013
This is version 49 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program