Unreviewed, UniProtKB/TrEMBL Q9Z4N9 (Q9Z4N9_BACCE)

Names and origin

Protein names	Recommended name:     Beta-amylase RuleBase RU000509V3     EC=3.2.1.2
Organism	Bacillus cereus EMBL BAA34650.1
Taxonomic identifier	1396 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	546 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. RuleBase RU000509V3
Sequence similarities	Belongs to the glycosyl hydrolase 14 family. RuleBase RU004157V1

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation RuleBase RU000509V3
Domain	Signal
Molecular function	Glycosidase RuleBase RU000509V3 Hydrolase
Gene Ontology (GO)
Biological process	polysaccharide catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	beta-amylase activity Inferred from electronic annotation. Source: InterPro 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 – 30	30	Potential EMBL BAA34650.1
	Chain	31 – 546	516	beta-amylase EMBL BAA34650.1		PRO_5000049300

Sequences

	Sequence		Length	Mass (Da)
	Q9Z4N9-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: A8F7CFC96ED6979B	FASTA	546	61,629
	10 20 30 40 50 60 MKNQFQYCCI VILSVVMLFV SLLIPQASSA AVNGKGMNPD YKAYLMAPLK KIPEVTNWET 70 80 90 100 110 120 FENDLRWAKQ NGFYAITVDF WWGDMEKNGD QQFDFSYAQR FAQSVKNAGM KMIPIISTHQ 130 140 150 160 170 180 CGGNVGDDCN VPIPSWVWNQ KSDDSLYFKS ETGTVNKETL NPLASDVIRK EYGELYTAFA 190 200 210 220 230 240 AAMKPYKDVI AKIYLSGGPA GELRYPSYTT SDGTGYPSRG KFQAYTEFAK SKFRLWVLNK 250 260 270 280 290 300 YGSLNEVNKA WGTKLISELA ILPPSDGEQF LMNGYLSMYG KDYLEWYQGI LENHTKLIGE 310 320 330 340 350 360 LAHNAFDTTF QVPIGAKIAG VHWQYNNPTI PHGAEKPAGY NDYSHLLDAF KSAKLDVTFT 370 380 390 400 410 420 CLEMTDKGSY PEYSMPKTLV QNIATLANEK GIVLNGENAL SIGNEEEYKR VAEMAFNYNF 430 440 450 460 470 480 AGFTLLRYQD VMYNNSLMGK FKDLLGVTPV MQTIVVKNVP TTIGDTVYIT GNRAELGSWD 490 500 510 520 530 540 TKQYPIQLYY DSHSNDWRGN VVLPAERNIE FKAFIKSKDG TVKSWQTIQQ SWNPVPLKTT SHTSSW

References

[1]	"Kinetic study of active site structure of beta-amylase from Bacillus cereus var. mycoides." Nitta Y., Shirakawa M., Takasaki Y. Biosci. Biotechnol. Biochem. 60:823-827(1996) Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Cloning, sequencing, and expression of a beta-amylase gene from Bacillus cereus var. mycoides and characterization of its products." Yamaguchi T., Matsumoto Y., Shirakawa M., Kibe M., Hibino T., Kozaki S., Takasaki Y., Nitta Y. Biosci. Biotechnol. Biochem. 60:1255-1259(1996) [PubMed: 8987540] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[3]	Oyama T. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[4]	"Crystal structure of beta-amylase from Bacillus cereus var. mycoides at 2.2 A resolution." Oyama T., Kusunoki M., Kishimoto Y., Takasaki Y., Nitta Y. J. Biochem. 125:1120-1130(1999) [PubMed: 10348915] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 31-546.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB020313 Genomic DNA. Translation: BAA34650.1.
PIR	A48961.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	CBM20. Carbohydrate-Binding Module Family 20. GH14. Glycoside Hydrolase Family 14.
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

Q9Z4N9_BACCE

Accession

Primary (citable) accession number: Q9Z4N9

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 1999
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)