Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P21543

- AMYB_PAEPO

UniProt

P21543 - AMYB_PAEPO

(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)

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MTLYRSLWKK GCMLLLSLVL SLTAFIGSPS NTASAAVADD FQASVMGPLA
60 70 80 90 100
KINDWGSFKK QLQTLKNNGV YAITTDVWWG YVESAGDNQF DWSYYKTYAN
110 120 130 140 150
AVKEAGLKWV PIISTHKCGG NVGDDCNIPL PSWLSSKGSA DEMQFKDESG
160 170 180 190 200
YANSEALSPL WSGTGKQYDE LYASFAENFA GYKSIIPKIY LSGGPSGELR
210 220 230 240 250
YPSYYPAAGW SYPGRGKFQA YTETAKNAFR TAMNDKYGSL DKINAAWGTK
260 270 280 290 300
LTSLSQINPP TDGDGFYTNG GYNSAYGKDF LSWYQSVLEK HLGVIGAAAH
310 320 330 340 350
KNFDSVFGVR IGAKISGLHW QMNNPAMPHG TEQAGGYYDY NRLIQKFKDA
360 370 380 390 400
DLDLTFTCLE MSDSGTAPNY SLPSTLVDTV SSIANAKGVR LNGENALPTG
410 420 430 440 450
GSGFQKIEEK ITKFGYHGFT LLRINNLVNN DGSPTGELSG FKQYIISKAK
460 470 480 490 500
PDNNGGTGNK VTIYYKKGFN SPYIHYRPAG GSWTAAPGVK MQDAEISGYA
510 520 530 540 550
KITVDIGSAS QLEAAFNDGN NNWDSNNTKN YSFSTGTSTY TPGNSGNAGT
560 570 580 590 600
ITSGAPAGAN PGDGGGTTNK VTVYYKKGFN SPYIHYRPAG GSWTAAPGVK
610 620 630 640 650
MQDAEISGYA KITVDIGSAS QLEAAFNDGN NNWDSNNTKN YLFSTGTSTY
660 670 680 690 700
TPGSNGAAGT IRTGAPSGSV LSVVTSTYAT DLNEVTGPIQ TEKLSGVSLN
710 720 730 740 750
VSTSTYAPNS NGVEVTAQTE APSGAFTSMD LGTLSNPTSL NTDWSKQSIY
760 770 780 790 800
FIMTDRFSNG DPSNDNYGGF NSNNSDQRKW HGGDFQGIIN KLDYIKNMGF
810 820 830 840 850
TAIWITPVTM QKSEYAYHGY HTYDFYAVDG HLGTMDKLQE LVRKAHDKNI
860 870 880 890 900
AVMVDVVVNH TGDFQPGNGF AKAPFDKADW YHHNGDITDG DYNSNNQWKI
910 920 930 940 950
ENGDVAGLDD LNHENPATAN ELKNWIKWLL NETGIDGLRL DTVKHVPKGF
960 970 980 990 1000
LKDFDQAANT FTMGEIFHGD PAYVGDYTRY LDAALDFPMY YTIKDVFGHD
1010 1020 1030 1040 1050
QSMRKIKDRY SDDRYYRDAQ TNGVFIDNHD VKRFLNDASG KPGANYDKWP
1060 1070 1080 1090 1100
QLKAALGFTL TSRGIPIIYQ GTEQGYSGGD DPANRENMNF NANHDLYQYI
1110 1120 1130 1140 1150
AKLNYVRNNH PALQNGSQRE KWVDDSFYSF QRSKNGDEAI VFINNSWNSQ
1160 1170 1180 1190
TRTIGNFDNL SNGTRLTNQL SNDSVQINNG SITVTLAPKE VKVFTK
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:
EMBLi
GenBanki
DDBJi
Links Updated
M15817 Genomic DNA. Translation: AAA85446.1.
Y00150 Other DNA. Translation: CAA68344.1.
PIRiA29130.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15817 Genomic DNA. Translation: AAA85446.1 .
Y00150 Other DNA. Translation: CAA68344.1 .
PIRi A29130.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 115 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