Beta/alpha-amylase precursor - Paenibacillus polymyxa

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Reviewed, UniProtKB/Swiss-Prot P21543 (AMYB_PAEPO)

Last modified January 19, 2010. Version 88. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names	Recommended name: Beta/alpha-amylase Including the following 2 domains: 1- Recommended name: Beta-amylase EC=3.2.1.2 2- Recommended name: Alpha-amylase EC=3.2.1.1
Organism	Paenibacillus polymyxa (Bacillus polymyxa)
Taxonomic identifier	1406 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Paenibacillaceae › Paenibacillus

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Protein attributes

Sequence length	1196 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	The precursor protein is proteolytically cleaved to produce multiform beta-amylases and a 48 kDa alpha-amylase after secretion.
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. Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides.
Subcellular location	Secreted.
Sequence similarities	In the N-terminal section; belongs to the glycosyl hydrolase 14 family. In the C-terminal section; belongs to the glycosyl hydrolase 13 family.

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Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation
Cellular component	Secreted
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alpha-amylase activity Inferred from electronic annotation. Source: EC beta-amylase activity Inferred from electronic annotation. Source: EC cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 35

Chain

36 – 1196

1161

Beta/alpha-amylase

PRO_0000001457

Regions

Repeat

455 – 558

104

Repeat

565 – 668

104

Region

36 – 454

419

Beta-amylase

Region

669 – 1196

528

Alpha-amylase

Sites

Active site

198

By similarity

Active site

394

By similarity

Amino acid modifications

Disulfide bond

118 ↔ 126

Ref.4

Experimental info

Mutagenesis

118

C → S: 5-fold decrease in activity. Ref.4

Mutagenesis

126

C → V: 20-fold decrease in activity. Ref.4

Mutagenesis

358

C → S: 60-fold decrease in activity. Ref.4

Sequence conflict

M → MIGL Ref.3

Sequence conflict

N → S in CAA68344. Ref.3

Sequence conflict

100

N → D in CAA68344. Ref.3

Sequence conflict

154

S → N in CAA68344. Ref.3

Sequence conflict

177

E → Q in CAA68344. Ref.3

Sequence conflict

227 – 228

NA → KS in CAA68344. Ref.3

Sequence conflict

330

G → S in CAA68344. Ref.3

Sequence conflict

425

N → S in CAA68344. Ref.3

Sequence conflict

493

D → A in CAA68344. Ref.3

Sequence conflict

532

S → L in CAA68344. Ref.3

Sequence conflict

559

A → T in CAA68344. Ref.3

Sequence conflict

665

A → T in CAA68344. Ref.3

Sequence conflict

681

D → N in CAA68344. Ref.3

Sequence conflict

686

T → A in CAA68344. Ref.3

Sequence conflict

725 – 728

AFTS → VFSP in CAA68344. Ref.3

Sequence conflict

736

N → K in CAA68344. Ref.3

Sequence conflict

741

N → S in CAA68344. Ref.3

Sequence conflict

758

S → N in CAA68344. Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

P21543-1 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: A41EA6B70F257064
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FASTA

1,196

130,893

        10         20         30         40         50         60 
MTLYRSLWKK GCMLLLSLVL SLTAFIGSPS NTASAAVADD FQASVMGPLA KINDWGSFKK 

        70         80         90        100        110        120 
QLQTLKNNGV YAITTDVWWG YVESAGDNQF DWSYYKTYAN AVKEAGLKWV PIISTHKCGG 

       130        140        150        160        170        180 
NVGDDCNIPL PSWLSSKGSA DEMQFKDESG YANSEALSPL WSGTGKQYDE LYASFAENFA 

       190        200        210        220        230        240 
GYKSIIPKIY LSGGPSGELR YPSYYPAAGW SYPGRGKFQA YTETAKNAFR TAMNDKYGSL 

       250        260        270        280        290        300 
DKINAAWGTK LTSLSQINPP TDGDGFYTNG GYNSAYGKDF LSWYQSVLEK HLGVIGAAAH 

       310        320        330        340        350        360 
KNFDSVFGVR IGAKISGLHW QMNNPAMPHG TEQAGGYYDY NRLIQKFKDA DLDLTFTCLE 

       370        380        390        400        410        420 
MSDSGTAPNY SLPSTLVDTV SSIANAKGVR LNGENALPTG GSGFQKIEEK ITKFGYHGFT 

       430        440        450        460        470        480 
LLRINNLVNN DGSPTGELSG FKQYIISKAK PDNNGGTGNK VTIYYKKGFN SPYIHYRPAG 

       490        500        510        520        530        540 
GSWTAAPGVK MQDAEISGYA KITVDIGSAS QLEAAFNDGN NNWDSNNTKN YSFSTGTSTY 

       550        560        570        580        590        600 
TPGNSGNAGT ITSGAPAGAN PGDGGGTTNK VTVYYKKGFN SPYIHYRPAG GSWTAAPGVK 

       610        620        630        640        650        660 
MQDAEISGYA KITVDIGSAS QLEAAFNDGN NNWDSNNTKN YLFSTGTSTY TPGSNGAAGT 

       670        680        690        700        710        720 
IRTGAPSGSV LSVVTSTYAT DLNEVTGPIQ TEKLSGVSLN VSTSTYAPNS NGVEVTAQTE 

       730        740        750        760        770        780 
APSGAFTSMD LGTLSNPTSL NTDWSKQSIY FIMTDRFSNG DPSNDNYGGF NSNNSDQRKW 

       790        800        810        820        830        840 
HGGDFQGIIN KLDYIKNMGF TAIWITPVTM QKSEYAYHGY HTYDFYAVDG HLGTMDKLQE 

       850        860        870        880        890        900 
LVRKAHDKNI AVMVDVVVNH TGDFQPGNGF AKAPFDKADW YHHNGDITDG DYNSNNQWKI 

       910        920        930        940        950        960 
ENGDVAGLDD LNHENPATAN ELKNWIKWLL NETGIDGLRL DTVKHVPKGF LKDFDQAANT 

       970        980        990       1000       1010       1020 
FTMGEIFHGD PAYVGDYTRY LDAALDFPMY YTIKDVFGHD QSMRKIKDRY SDDRYYRDAQ 

      1030       1040       1050       1060       1070       1080 
TNGVFIDNHD VKRFLNDASG KPGANYDKWP QLKAALGFTL TSRGIPIIYQ GTEQGYSGGD 

      1090       1100       1110       1120       1130       1140 
DPANRENMNF NANHDLYQYI AKLNYVRNNH PALQNGSQRE KWVDDSFYSF QRSKNGDEAI 

      1150       1160       1170       1180       1190 
VFINNSWNSQ TRTIGNFDNL SNGTRLTNQL SNDSVQINNG SITVTLAPKE VKVFTK

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References

[1]	"Cloning and nucleotide sequence of the gene coding for enzymatically active fragments of the Bacillus polymyxa beta-amylase." Kawazu T., Nakanishi Y., Uozumi N., Sasaki T., Yamagata H., Tsukagoshi N., Udaka S. J. Bacteriol. 169:1564-1570(1987) [PubMed: 2435707] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-936, PARTIAL PROTEIN SEQUENCE. Strain: 72.
[2]	"A single gene directs synthesis of a precursor protein with beta- and alpha-amylase activities in Bacillus polymyxa." Uozumi N., Sakurai K., Sasaki T., Takekawa S., Yamagata H., Tsukagoshi N., Udaka S. J. Bacteriol. 171:375-382(1989) [PubMed: 2464578] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 689-1196, PARTIAL PROTEIN SEQUENCE. Strain: 72.
[3]	"Sequence of an active fragment of B. polymyxa beta amylase." Rhodes C., Strasser J., Friedberg F. Nucleic Acids Res. 15:3934-3934(1987) [PubMed: 2438660] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-776. Strain: ATCC 8523 / CCM 1465 / DSM 356.
[4]	"Structural and functional roles of cysteine residues of Bacillus polymyxa beta-amylase." Uozumi N., Matsuda T., Tsukagoshi N., Udaka S. Biochemistry 30:4594-4599(1991) [PubMed: 1827035] [Abstract] Cited for: DISULFIDE BOND, MUTAGENESIS OF CYSTEINE RESIDUES.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	M15817 Genomic DNA. Translation: AAA85446.1. Y00150 Other DNA. Translation: CAA68344.1.
PIR	A29130.
3D structure databases
SMR	P21543. Positions 35-542, 569-666.
ModBase	Search...
Protein family/group databases
CAZy	CBM25. Carbohydrate-Binding Module Family 25. GH13. Glycoside Hydrolase Family 13. GH14. Glycoside Hydrolase Family 14.
Enzyme and pathway databases
BRENDA	3.2.1.1. 276031. 3.2.1.2. 276031.
Family and domain databases
InterPro	IPR006048. A-amylase_b_C. IPR005085. Carb-bd_dom_fam25. IPR008985. ConA-like_lec_gl. IPR006047. Glyco_hydro_13_cat_dom. IPR006589. Glyco_hydro_13_sub_cat_dom. IPR001554. Glyco_hydro_14. IPR018238. Glyco_hydro_14_CS. IPR000125. Glyco_hydro_14A_bac. IPR017853. Glyco_hydro_catalytic_core. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits.
Pfam	PF00128. Alpha-amylase. 1 hit. PF03423. CBM_25. 2 hits. PF01373. Glyco_hydro_14. 1 hit. [Graphical view]
PRINTS	PR00750. BETAAMYLASE. PR00841. GLHYDLASE14A.
SMART	SM00642. Aamy. 1 hit. SM00632. Aamy_C. 1 hit. [Graphical view]
PROSITE	PS00506. BETA_AMYLASE_1. 1 hit. PS00679. BETA_AMYLASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

AMYB_PAEPO

Accession

Primary (citable) accession number: P21543

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	January 19, 2010
This is version 88 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)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents