Reviewed, UniProtKB/Swiss-Prot P19584 (AMYB_THETU)

Names and origin

Protein names	Recommended name:     Thermophilic beta-amylase     EC=3.2.1.2 Alternative name(s):     1,4-alpha-D-glucan maltohydrolase
Organism	Thermoanaerobacter thermosulfurogenes (Clostridium thermosulfurogenes)
Taxonomic identifier	33950 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Thermoanaerobacterium

Protein attributes

Sequence length	551 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	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. Contains 1 CBM20 (carbohydrate binding type-20) domain.
Biophysicochemical properties	Temperature dependence: Optimum temperature is 75 degrees Celsius. Stable at 80 degrees Celsius.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
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 – 32	32	Ref.1
	Chain	33 – 551	519	Thermophilic beta-amylase		PRO_0000001456
Regions
	Domain	448 – 551	104	CBM20
Sites
	Active site	195	1	By similarity
	Active site	392	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P19584-1 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 58526A1067275AC2	FASTA	551	60,548
	10 20 30 40 50 60 MIGAFKRLGQ KLFLTLLTAS LIFASSIVTA NASIAPNFKV FVMGPLEKVT DFNAFKDQLI 70 80 90 100 110 120 TLKNNGVYGI TTDIWWGYVE NAGENQFDWS YYKTYADTVR AAGLKWVPIM STHACGGNVG 130 140 150 160 170 180 DTVNIPIPSW VWTKDTQDNM QYKDEAGNWD NEAVSPWYSG LTQLYNEFYS SFASNFSSYK 190 200 210 220 230 240 DIITKIYISG GPSGELRYPS YNPSHGWTYP GRGSLQCYSK AAITSFQNAM KSKYGTIAAV 250 260 270 280 290 300 NSAWGTSLTD FSQISPPTDG DNFFTNGYKT TYGNDFLTWY QSVLTNELAN IASVAHSCFD 310 320 330 340 350 360 PVFNVPIGAK IAGVHWLYNS PTMPHAAEYC AGYYNYSTLL DQFKASNLAM TFTCLEMDDS 370 380 390 400 410 420 NAYVSPYYSA PMTLVHYVAN LANNKGIVHN GENALAISNN NQAYVNCANE LTGYNFSGFT 430 440 450 460 470 480 LLRLSNIVNS DGSVTSEMAP FVINIVTLTP NGTIPVTFTI NNATTYYGQN VYIVGSTSDL 490 500 510 520 530 540 GNWNTTYARG PASCPNYPTW TITLNLLPGE QIQFKAVKID SSGNVTWEGG SNHTYTVPTS 550 GTGSVTITWQ N

References

[1]

"Cloning and sequencing of the gene encoding thermophilic beta-amylase of Clostridium thermosulfurogenes." Kitamoto N., Yamagata H., Kato T., Tsukagoshi N., Udaka S. J. Bacteriol. 170:5848-5854(1988) [PubMed: 2461360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 33-44. Strain: ATCC 33743 / DSM 2229 / 4BT.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M22471 Genomic DNA. Translation: AAA23204.1.
PIR	A31389.
3D structure databases
HSSP	HSSP built from PDB template 1J18 based on UniProtKB P36924.
ModBase	Search...
Protein family/group databases
CAZy	CBM20. Carbohydrate-Binding Module Family 20. GH14. Glycoside Hydrolase Family 14.
Enzyme and pathway databases
BRENDA	3.2.1.2. 281041.
Family and domain databases
InterPro	IPR001554. Glyco_hydro_14. IPR018238. Glyco_hydro_14_CS. IPR000125. Glyco_hydro_14A_bac. IPR002044. Glyco_hydro_carb-bd. IPR013781. Glyco_hydro_sg_catalytic. IPR013783. Ig-like_fold. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
Pfam	PF00686. CBM_20. 1 hit. PF01373. Glyco_hydro_14. 1 hit. [Graphical view]
PRINTS	PR00750. BETAAMYLASE. PR00841. GLHYDLASE14A.
ProDom	PD001568. Glyco_hydro_CBD. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00506. BETA_AMYLASE_1. 1 hit. PS00679. BETA_AMYLASE_2. 1 hit. PS51166. CBM20. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMYB_THETU

Accession

Primary (citable) accession number: P19584

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	June 16, 2009
This is version 66 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)