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P21543

- AMYB_PAEPO

UniProt

P21543 - AMYB_PAEPO

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Protein

Beta/alpha-amylase

Gene
N/A
Organism
Paenibacillus polymyxa (Bacillus polymyxa)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The precursor protein is proteolytically cleaved to produce multiform beta-amylases and a 48 kDa alpha-amylase after secretion.

Catalytic activityi

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 polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761Substrate By similarity
Binding sitei116 – 1161Substrate By similarity
Binding sitei124 – 1241Substrate By similarity
Active sitei198 – 1981Proton donor By similarity
Binding sitei314 – 3141Substrate By similarity
Binding sitei319 – 3191Substrate By similarity
Binding sitei357 – 3571Substrate By similarity
Active sitei394 – 3941Proton acceptor By similarity
Binding sitei423 – 4231Substrate By similarity

GO - Molecular functioni

  1. alpha-amylase activity Source: UniProtKB-EC
  2. beta-amylase activity Source: UniProtKB-EC
  3. cation binding Source: InterPro
  4. starch binding Source: InterPro

GO - Biological processi

  1. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Protein family/group databases

CAZyiCBM25. Carbohydrate-Binding Module Family 25.
GH13. Glycoside Hydrolase Family 13.
GH14. Glycoside Hydrolase Family 14.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta/alpha-amylase
Including the following 2 domains:
Beta-amylase (EC:3.2.1.2)
Alpha-amylase (EC:3.2.1.1)
OrganismiPaenibacillus polymyxa (Bacillus polymyxa)
Taxonomic identifieri1406 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi118 – 1181C → S: 5-fold decrease in activity. 1 Publication
Mutagenesisi126 – 1261C → V: 20-fold decrease in activity. 1 Publication
Mutagenesisi358 – 3581C → S: 60-fold decrease in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Add
BLAST
Chaini36 – 11961161Beta/alpha-amylasePRO_0000001457Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi118 ↔ 1261 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
1196
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 465
Helixi55 – 6713
Beta strandi72 – 787
Helixi79 – 824
Helixi93 – 10412
Beta strandi108 – 1147
Helixi132 – 1365
Helixi140 – 1434
Beta strandi144 – 1463
Helixi163 – 17917
Helixi180 – 1856
Beta strandi188 – 1914
Helixi195 – 1973
Beta strandi198 – 2003
Helixi206 – 2083
Helixi223 – 23715
Helixi240 – 2478
Helixi254 – 2563
Turni264 – 2696
Turni271 – 2733
Helixi275 – 30329
Turni304 – 3074
Beta strandi310 – 3145
Beta strandi325 – 3273
Helixi330 – 3356
Helixi340 – 35011
Beta strandi353 – 3564
Turni367 – 3693
Helixi373 – 38715
Beta strandi391 – 3944
Helixi402 – 41312
Beta strandi417 – 4226
Helixi424 – 4263
Helixi438 – 4447
Helixi446 – 4483
Beta strandi460 – 4667
Beta strandi468 – 4714
Beta strandi473 – 4786
Beta strandi485 – 4873
Beta strandi492 – 4943
Turni495 – 4984
Beta strandi499 – 5057
Beta strandi512 – 5176
Beta strandi519 – 5213
Beta strandi523 – 5253
Turni526 – 5283
Beta strandi531 – 5333
Beta strandi535 – 5417
Beta strandi544 – 5463
Beta strandi550 – 5545
Beta strandi570 – 5767
Beta strandi579 – 5813
Beta strandi583 – 5886
Beta strandi595 – 5973
Beta strandi605 – 61511
Beta strandi622 – 6276
Beta strandi629 – 6313
Beta strandi637 – 6393
Beta strandi641 – 6433
Beta strandi645 – 6517
Beta strandi654 – 6563
Beta strandi659 – 6646

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LAANMR-A455-558[»]
2LABNMR-A565-668[»]
3VOCX-ray1.95A36-454[»]
ProteinModelPortaliP21543.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati455 – 558104Add
BLAST
Repeati565 – 668104Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni36 – 454419Beta-amylaseAdd
BLAST
Regioni395 – 3962Substrate binding By similarity
Regioni669 – 1196528Alpha-amylaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the glycosyl hydrolase 14 family.
In the C-terminal section; belongs to the glycosyl hydrolase 13 family.

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR006048. A-amylase_b_C.
IPR005085. CBM_fam25.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
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.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF03423. CBM_25. 2 hits.
PF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSiPR00750. BETAAMYLASE.
PR00841. GLHYDLASE14A.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01066. CBM_25. 2 hits.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
PROSITEiPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21543-1 [UniParc]FASTAAdd to Basket

« Hide

MTLYRSLWKK GCMLLLSLVL SLTAFIGSPS NTASAAVADD FQASVMGPLA     50
KINDWGSFKK QLQTLKNNGV YAITTDVWWG YVESAGDNQF DWSYYKTYAN 100
AVKEAGLKWV PIISTHKCGG NVGDDCNIPL PSWLSSKGSA DEMQFKDESG 150
YANSEALSPL WSGTGKQYDE LYASFAENFA GYKSIIPKIY LSGGPSGELR 200
YPSYYPAAGW SYPGRGKFQA YTETAKNAFR TAMNDKYGSL DKINAAWGTK 250
LTSLSQINPP TDGDGFYTNG GYNSAYGKDF LSWYQSVLEK HLGVIGAAAH 300
KNFDSVFGVR IGAKISGLHW QMNNPAMPHG TEQAGGYYDY NRLIQKFKDA 350
DLDLTFTCLE MSDSGTAPNY SLPSTLVDTV SSIANAKGVR LNGENALPTG 400
GSGFQKIEEK ITKFGYHGFT LLRINNLVNN DGSPTGELSG FKQYIISKAK 450
PDNNGGTGNK VTIYYKKGFN SPYIHYRPAG GSWTAAPGVK MQDAEISGYA 500
KITVDIGSAS QLEAAFNDGN NNWDSNNTKN YSFSTGTSTY TPGNSGNAGT 550
ITSGAPAGAN PGDGGGTTNK VTVYYKKGFN SPYIHYRPAG GSWTAAPGVK 600
MQDAEISGYA KITVDIGSAS QLEAAFNDGN NNWDSNNTKN YLFSTGTSTY 650
TPGSNGAAGT IRTGAPSGSV LSVVTSTYAT DLNEVTGPIQ TEKLSGVSLN 700
VSTSTYAPNS NGVEVTAQTE APSGAFTSMD LGTLSNPTSL NTDWSKQSIY 750
FIMTDRFSNG DPSNDNYGGF NSNNSDQRKW HGGDFQGIIN KLDYIKNMGF 800
TAIWITPVTM QKSEYAYHGY HTYDFYAVDG HLGTMDKLQE LVRKAHDKNI 850
AVMVDVVVNH TGDFQPGNGF AKAPFDKADW YHHNGDITDG DYNSNNQWKI 900
ENGDVAGLDD LNHENPATAN ELKNWIKWLL NETGIDGLRL DTVKHVPKGF 950
LKDFDQAANT FTMGEIFHGD PAYVGDYTRY LDAALDFPMY YTIKDVFGHD 1000
QSMRKIKDRY SDDRYYRDAQ TNGVFIDNHD VKRFLNDASG KPGANYDKWP 1050
QLKAALGFTL TSRGIPIIYQ GTEQGYSGGD DPANRENMNF NANHDLYQYI 1100
AKLNYVRNNH PALQNGSQRE KWVDDSFYSF QRSKNGDEAI VFINNSWNSQ 1150
TRTIGNFDNL SNGTRLTNQL SNDSVQINNG SITVTLAPKE VKVFTK 1196
Length:1,196
Mass (Da):130,893
Last modified:May 1, 1991 - v1
Checksum:iA41EA6B70F257064
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → MIGL in CAA68344. 1 Publication
Sequence conflicti67 – 671N → S in CAA68344. 1 Publication
Sequence conflicti100 – 1001N → D in CAA68344. 1 Publication
Sequence conflicti154 – 1541S → N in CAA68344. 1 Publication
Sequence conflicti177 – 1771E → Q in CAA68344. 1 Publication
Sequence conflicti227 – 2282NA → KS in CAA68344. 1 Publication
Sequence conflicti330 – 3301G → S in CAA68344. 1 Publication
Sequence conflicti425 – 4251N → S in CAA68344. 1 Publication
Sequence conflicti493 – 4931D → A in CAA68344. 1 Publication
Sequence conflicti532 – 5321S → L in CAA68344. 1 Publication
Sequence conflicti559 – 5591A → T in CAA68344. 1 Publication
Sequence conflicti665 – 6651A → T in CAA68344. 1 Publication
Sequence conflicti681 – 6811D → N in CAA68344. 1 Publication
Sequence conflicti686 – 6861T → A in CAA68344. 1 Publication
Sequence conflicti725 – 7284AFTS → VFSP in CAA68344. 1 Publication
Sequence conflicti736 – 7361N → K in CAA68344. 1 Publication
Sequence conflicti741 – 7411N → S in CAA68344. 1 Publication
Sequence conflicti758 – 7581S → N in CAA68344. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15817 Genomic DNA. Translation: AAA85446.1.
Y00150 Other DNA. Translation: CAA68344.1.
PIRiA29130.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15817 Genomic DNA. Translation: AAA85446.1 .
Y00150 Other DNA. Translation: CAA68344.1 .
PIRi A29130.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LAA NMR - A 455-558 [» ]
2LAB NMR - A 565-668 [» ]
3VOC X-ray 1.95 A 36-454 [» ]
ProteinModelPortali P21543.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM25. Carbohydrate-Binding Module Family 25.
GH13. Glycoside Hydrolase Family 13.
GH14. Glycoside Hydrolase Family 14.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProi IPR006048. A-amylase_b_C.
IPR005085. CBM_fam25.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
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.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF03423. CBM_25. 2 hits.
PF01373. Glyco_hydro_14. 1 hit.
[Graphical view ]
PRINTSi PR00750. BETAAMYLASE.
PR00841. GLHYDLASE14A.
SMARTi SM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01066. CBM_25. 2 hits.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 2 hits.
PROSITEi PS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-776.
    Strain: ATCC 8523 / CCM 1465 / DSM 356 / VKM B-418.
  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] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BOND, MUTAGENESIS OF CYSTEINE RESIDUES.

Entry informationi

Entry nameiAMYB_PAEPO
AccessioniPrimary (citable) accession number: P21543
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: October 16, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Multifunctional enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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