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Protein

Beta/alpha-amylase

Gene
N/A
Organism
Paenibacillus polymyxa (Bacillus polymyxa)
Status
Reviewed-Annotation score: 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.

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei76SubstrateBy similarity1
Metal bindingi83CalciumBy similarity1
Metal bindingi87CalciumBy similarity1
Binding sitei116SubstrateBy similarity1
Binding sitei124SubstrateBy similarity1
Metal bindingi170CalciumBy similarity1
Active sitei198Proton donorPROSITE-ProRule annotation1
Binding sitei314SubstrateBy similarity1
Binding sitei319SubstrateBy similarity1
Binding sitei357SubstrateBy similarity1
Active sitei394Proton acceptorBy similarity1
Binding sitei423SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Keywords - Ligandi

Metal-binding

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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi118C → S: 5-fold decrease in activity. 1 Publication1
Mutagenesisi126C → V: 20-fold decrease in activity. 1 Publication1
Mutagenesisi358C → S: 60-fold decrease in activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 35Add BLAST35
ChainiPRO_000000145736 – 1196Beta/alpha-amylaseAdd BLAST1161

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi118 ↔ 1261 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi886882.PPSC2_c5221.

Structurei

Secondary structure

11196
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi42 – 46Combined sources5
Helixi55 – 67Combined sources13
Beta strandi72 – 78Combined sources7
Helixi79 – 82Combined sources4
Helixi93 – 104Combined sources12
Beta strandi108 – 114Combined sources7
Helixi132 – 136Combined sources5
Helixi140 – 143Combined sources4
Beta strandi144 – 146Combined sources3
Helixi163 – 179Combined sources17
Helixi180 – 185Combined sources6
Beta strandi188 – 191Combined sources4
Helixi195 – 197Combined sources3
Beta strandi198 – 200Combined sources3
Helixi206 – 208Combined sources3
Helixi223 – 237Combined sources15
Helixi240 – 247Combined sources8
Helixi254 – 256Combined sources3
Turni264 – 269Combined sources6
Turni271 – 273Combined sources3
Helixi275 – 303Combined sources29
Turni304 – 307Combined sources4
Beta strandi310 – 314Combined sources5
Beta strandi325 – 327Combined sources3
Helixi330 – 335Combined sources6
Helixi340 – 350Combined sources11
Beta strandi353 – 356Combined sources4
Turni367 – 369Combined sources3
Helixi373 – 387Combined sources15
Beta strandi391 – 394Combined sources4
Helixi402 – 413Combined sources12
Beta strandi417 – 422Combined sources6
Helixi424 – 426Combined sources3
Helixi438 – 444Combined sources7
Helixi446 – 448Combined sources3
Beta strandi460 – 466Combined sources7
Beta strandi468 – 471Combined sources4
Beta strandi473 – 478Combined sources6
Beta strandi485 – 487Combined sources3
Beta strandi492 – 494Combined sources3
Turni495 – 498Combined sources4
Beta strandi499 – 505Combined sources7
Beta strandi512 – 517Combined sources6
Beta strandi519 – 521Combined sources3
Beta strandi523 – 525Combined sources3
Turni526 – 528Combined sources3
Beta strandi531 – 533Combined sources3
Beta strandi535 – 541Combined sources7
Beta strandi544 – 546Combined sources3
Beta strandi550 – 554Combined sources5
Beta strandi570 – 576Combined sources7
Beta strandi579 – 581Combined sources3
Beta strandi583 – 588Combined sources6
Beta strandi595 – 597Combined sources3
Beta strandi605 – 615Combined sources11
Beta strandi622 – 627Combined sources6
Beta strandi629 – 631Combined sources3
Beta strandi637 – 639Combined sources3
Beta strandi641 – 643Combined sources3
Beta strandi645 – 651Combined sources7
Beta strandi654 – 656Combined sources3
Beta strandi659 – 664Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LAANMR-A455-558[»]
2LABNMR-A565-668[»]
3VOCX-ray1.95A36-454[»]
ProteinModelPortaliP21543.
SMRiP21543.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati455 – 558Add BLAST104
Repeati565 – 668Add BLAST104

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni36 – 454Beta-amylaseAdd BLAST419
Regioni395 – 396Substrate bindingBy similarity2
Regioni669 – 1196Alpha-amylaseAdd BLAST528

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

Phylogenomic databases

eggNOGiENOG4105C9C. Bacteria.
COG0366. LUCA.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR031319. A-amylase_C.
IPR005085. CBM25.
IPR006047. Glyco_hydro_13_cat_dom.
IPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR000125. Glyco_hydro_14A_bac.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
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)DescriptionActionsGraphical viewLength
Sequence conflicti1M → MIGL in CAA68344 (PubMed:2438660).Curated1
Sequence conflicti67N → S in CAA68344 (PubMed:2438660).Curated1
Sequence conflicti100N → D in CAA68344 (PubMed:2438660).Curated1
Sequence conflicti154S → N in CAA68344 (PubMed:2438660).Curated1
Sequence conflicti177E → Q in CAA68344 (PubMed:2438660).Curated1
Sequence conflicti227 – 228NA → KS in CAA68344 (PubMed:2438660).Curated2
Sequence conflicti330G → S in CAA68344 (PubMed:2438660).Curated1
Sequence conflicti425N → S in CAA68344 (PubMed:2438660).Curated1
Sequence conflicti493D → A in CAA68344 (PubMed:2438660).Curated1
Sequence conflicti532S → L in CAA68344 (PubMed:2438660).Curated1
Sequence conflicti559A → T in CAA68344 (PubMed:2438660).Curated1
Sequence conflicti665A → T in CAA68344 (PubMed:2438660).Curated1
Sequence conflicti681D → N in CAA68344 (PubMed:2438660).Curated1
Sequence conflicti686T → A in CAA68344 (PubMed:2438660).Curated1
Sequence conflicti725 – 728AFTS → VFSP in CAA68344 (PubMed:2438660).Curated4
Sequence conflicti736N → K in CAA68344 (PubMed:2438660).Curated1
Sequence conflicti741N → S in CAA68344 (PubMed:2438660).Curated1
Sequence conflicti758S → N in CAA68344 (PubMed:2438660).Curated1

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.
PIRiA29130.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LAANMR-A455-558[»]
2LABNMR-A565-668[»]
3VOCX-ray1.95A36-454[»]
ProteinModelPortaliP21543.
SMRiP21543.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi886882.PPSC2_c5221.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105C9C. Bacteria.
COG0366. LUCA.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR031319. A-amylase_C.
IPR005085. CBM25.
IPR006047. Glyco_hydro_13_cat_dom.
IPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR000125. Glyco_hydro_14A_bac.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
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]
ProtoNetiSearch...

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 2, 2016
This is version 124 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.