Reviewed, UniProtKB/Swiss-Prot P82993 (AMYB_HORSP)

Names and origin

Protein names

Recommended name:
    Beta-amylase
    EC=3.2.1.2
Alternative name(s):
    1,4-alpha-D-glucan maltohydrolase
    Beta-Amy1

Gene names

Name:

BMY1

Organism

Hordeum spontaneum (Barley)

Taxonomic identifier

77009 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

Protein attributes

Sequence length	535 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)

Function	Catalyzes the liberation of maltose from 1,4-alpha-D glucans. Ref.1 Ref.2
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 By similarity. UniProtKB P10538
Tissue specificity	Endosperm. Ref.2
Polymorphism	There are at least three alleles; SD2H; SD1 and SD2L. The sequence of SD2H is shown here. Ref.2
Miscellaneous	The three alleles show different thermostabilities and different affinities for soluble starch. Ref.2
Sequence similarities	Belongs to the glycosyl hydrolase 14 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation
Coding sequence diversity	Polymorphism
Domain	Repeat
Molecular function	Glycosidase Hydrolase
PTM	Acetylation
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
	Propeptide	1 – 2	2	Removed in mature form Ref.2		PRO_0000279693
	Chain	3 – 489	487	Beta-amylase Ref.2		PRO_0000279694
	Propeptide	490 – 535	46	Removed in mature form Ref.2		PRO_0000279695
Regions
	Repeat	489 – 499	11	1
	Repeat	500 – 510	11	2
	Repeat	511 – 521	11	3
	Repeat	522 – 532	11	4; approximate
	Region	489 – 532	44	4 X 11 AA tandem repeats
Sites
	Active site	184	1	By similarity UniProtKB P10538
	Active site	378	1	By similarity UniProtKB P10538
Amino acid modifications
	Modified residue	3	1	N-acetylvaline Ref.2
Natural variations
	Natural variant	165	1	E → D Ref.2
	Natural variant	254	1	T → S Ref.2
	Natural variant	472	1	K → Q Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P82993-1 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: 0B265EAEEF061C9B	FASTA	535	59,639
	10 20 30 40 50 60 MEVNVKGNYV QVYVMLPLDA VSVNNRFEKG DELRAQLRKL VEAGVDGVMV DVWWGLVEGK 70 80 90 100 110 120 GPKAYDWSAY KQLFELVQKA GLKLQAIMSF HQCGGNVGDA VNIPIPQWVR DVGTRDPDIF 130 140 150 160 170 180 YTDGHGTRNI EYLTLGVDNQ PLFHGRSAVQ MYADYMTSFR ENMKEFLDAG VIVDIEVGLG 190 200 210 220 230 240 PAGEMRYPSY PQSHGWSFPG IGEFICYDKY LQADFKAAAA AVGHPEWEFP NDAGQYNDTP 250 260 270 280 290 300 ERTQFFRDNG TYLTEKGRFF LAWYSNNLIK HGDRILDEAN KVFLGYKVQL AIKISGIHWW 310 320 330 340 350 360 YKVPSHAAEL TAGYYNLHDR DGYRTIARML KRHRASINFT CAEMRDSEQS SQAMSAPEEL 370 380 390 400 410 420 VQQVLSAGWR EGLNVACENA LPRYDPTAYN TILRNARPHG INQSGPPEHK LFGFTYLRLS 430 440 450 460 470 480 NQLVEGQNYV NFKTFVDRMH ANLPRDPYVD PMAPLPRSGP EISIEMILQA AKPKLQPFPF 490 500 510 520 530 QEHTDLPVGP TGGMGGQAEG PTCGMGGQVK GPTGGMGGQA EDPTSGMGGE LPATM

References

[1]	"Allele-dependent barley grain beta-amylase activity." Erkkila M.J., Leah R., Ahokas H., Cameron-Mills V. Plant Physiol. 117:679-685(1998) [PubMed: 9625721] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: cv. NPGS PI296897. Tissue: Endosperm.
[2]	"The structural basis for functional differences between allelic forms of barley (Hordeum vulgare) beta-amylase." Eglinton J.K., Lahnstein J., Shirley N., Evans D.E. Submitted (MAY-2001) to UniProtKB Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, TISSUE SPECIFICITY, POLYMORPHISM, ACETYLATION AT VAL-3, VARIANTS ASP-165; SER-254 AND GLN-472. Strain: cv. CPI77146-33. Tissue: Seed.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF061204 Genomic DNA. Translation: AAC67246.1.
3D structure databases
HSSP	HSSP built from PDB template 1B1Y based on UniProtKB P16098.
ModBase	Search...
Protein family/group databases
CAZy	GH14. Glycoside Hydrolase Family 14.
Organism-specific databases
Gramene	P82993.
Family and domain databases
InterPro	IPR001554. Glyco_hydro_14. IPR018238. Glyco_hydro_14_CS. IPR001371. Glyco_hydro_14B_pln. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF01373. Glyco_hydro_14. 1 hit. [Graphical view]
PRINTS	PR00750. BETAAMYLASE. PR00842. GLHYDLASE14B.
PROSITE	PS00506. BETA_AMYLASE_1. 1 hit. PS00679. BETA_AMYLASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMYB_HORSP

Accession

Primary (citable) accession number: P82993

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 6, 2007
Last sequence update:	October 1, 2001
Last modified:	June 16, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)