Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P21543

- AMYB_PAEPO

UniProt

P21543 - AMYB_PAEPO

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 761SubstrateBy similarity
    Binding sitei116 – 1161SubstrateBy similarity
    Binding sitei124 – 1241SubstrateBy similarity
    Active sitei198 – 1981Proton donorPROSITE-ProRule annotation
    Binding sitei314 – 3141SubstrateBy similarity
    Binding sitei319 – 3191SubstrateBy similarity
    Binding sitei357 – 3571SubstrateBy similarity
    Active sitei394 – 3941Proton acceptorPROSITE-ProRule annotation
    Binding sitei423 – 4231SubstrateBy 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

    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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 bindingBy similarity
    Regioni669 – 1196528Alpha-amylaseAdd
    BLAST

    Sequence similaritiesi

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

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 11M → MIGL in CAA68344. (PubMed:2438660)Curated
    Sequence conflicti67 – 671N → S in CAA68344. (PubMed:2438660)Curated
    Sequence conflicti100 – 1001N → D in CAA68344. (PubMed:2438660)Curated
    Sequence conflicti154 – 1541S → N in CAA68344. (PubMed:2438660)Curated
    Sequence conflicti177 – 1771E → Q in CAA68344. (PubMed:2438660)Curated
    Sequence conflicti227 – 2282NA → KS in CAA68344. (PubMed:2438660)Curated
    Sequence conflicti330 – 3301G → S in CAA68344. (PubMed:2438660)Curated
    Sequence conflicti425 – 4251N → S in CAA68344. (PubMed:2438660)Curated
    Sequence conflicti493 – 4931D → A in CAA68344. (PubMed:2438660)Curated
    Sequence conflicti532 – 5321S → L in CAA68344. (PubMed:2438660)Curated
    Sequence conflicti559 – 5591A → T in CAA68344. (PubMed:2438660)Curated
    Sequence conflicti665 – 6651A → T in CAA68344. (PubMed:2438660)Curated
    Sequence conflicti681 – 6811D → N in CAA68344. (PubMed:2438660)Curated
    Sequence conflicti686 – 6861T → A in CAA68344. (PubMed:2438660)Curated
    Sequence conflicti725 – 7284AFTS → VFSP in CAA68344. (PubMed:2438660)Curated
    Sequence conflicti736 – 7361N → K in CAA68344. (PubMed:2438660)Curated
    Sequence conflicti741 – 7411N → S in CAA68344. (PubMed:2438660)Curated
    Sequence conflicti758 – 7581S → N in CAA68344. (PubMed:2438660)Curated

    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 1, 2014
    This is version 113 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