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Protein
Submitted name:

Alpha-amylase

Gene

amyL

Organism
Bacillus megaterium (strain DSM 319)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Protein predictedi

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei233 – 2331NucleophileUniRule annotation
Active sitei263 – 2631Proton donorUniRule annotation

GO - Molecular functioni

  1. alpha-amylase activity Source: UniProtKB-EC
  2. calcium ion binding Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseImported, Hydrolase

Enzyme and pathway databases

BioCyciBMEG592022:GIVX-5229-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Alpha-amylaseImported (EC:3.2.1.1Imported)
Gene namesi
Name:amyLImported
Ordered Locus Names:BMD_5229Imported
OrganismiBacillus megaterium (strain DSM 319)Imported
Taxonomic identifieri592022 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000002365 Componenti: Chromosome

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000094847.
KOiK01176.
OMAiFFHWYYP.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013776. A-amylase_thermo.
IPR015237. Alpha-amylase_C_pro.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF09154. DUF1939. 1 hit.
[Graphical view]
PIRSFiPIRSF001021. Alph-amls_thrmst. 1 hit.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

D5DME4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERNHTIMQF FEWHVPADGE HWQRLKELAP QLKEQGIDSV WIPPVTKGVS
60 70 80 90 100
SEDNGYGVYD LYDLGEFDQK GTVRTKYGTK QELHEAIDAC HNHGINVYVD
110 120 130 140 150
IVMNHKAAAD EKETFHVIEV DPMNRTEEIS EPFEIEGWTK FTFEGRGDQY
160 170 180 190 200
SSFKWNFNHF NGTDYDDKNG KEGVFRIAGE NKSWNENVDQ EFGNYDYLMF
210 220 230 240 250
ANIDYNHPEV REEMIKWGKW LADTLQCDGY RLDAIKHINH DFIKEFAHEL
260 270 280 290 300
SSSQEKPFYF VGEFWNPELT ACQEFLDVID YQIDLFDVSL HYKLHEASQQ
310 320 330 340 350
GRDFDLTTIF DDTLVKTHPL NVVTFVDNHD SQPNESLESW VEDWFKQSAY
360 370 380 390 400
ALILLREDGY PCVFYGDYFG IGGEHPIKGK EKDISALLHV RYDKAYGQQD
410 420 430 440 450
DYFDHPNTIG WVRHGVEEFE KSGCAVVISN GEDGEKRMFV GEHRSGQTWI
460 470 480
DFTNNREDQV VIEEDGYGQF PVNGGSVSVW AEA
Length:483
Mass (Da):56,090
Last modified:June 15, 2010 - v1
Checksum:i872863FBA4031B1E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001982 Genomic DNA. Translation: ADF42028.1.
RefSeqiWP_013085538.1. NC_014103.1.
YP_003600378.1. NC_014103.1.

Genome annotation databases

EnsemblBacteriaiADF42028; ADF42028; BMD_5229.
GeneIDi9120620.
KEGGibmd:BMD_5229.
PATRICi37260651. VBIBacMeg104484_5209.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001982 Genomic DNA. Translation: ADF42028.1.
RefSeqiWP_013085538.1. NC_014103.1.
YP_003600378.1. NC_014103.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADF42028; ADF42028; BMD_5229.
GeneIDi9120620.
KEGGibmd:BMD_5229.
PATRICi37260651. VBIBacMeg104484_5209.

Phylogenomic databases

HOGENOMiHOG000094847.
KOiK01176.
OMAiFFHWYYP.

Enzyme and pathway databases

BioCyciBMEG592022:GIVX-5229-MONOMER.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013776. A-amylase_thermo.
IPR015237. Alpha-amylase_C_pro.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF09154. DUF1939. 1 hit.
[Graphical view]
PIRSFiPIRSF001021. Alph-amls_thrmst. 1 hit.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequences of the industrial vitamin B12-producers B. megaterium QM B1551 and DSM319 reveal new insights into the Bacillus genome evolution and pan-genome structure."
    Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J., Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J., Vary P.S.
    Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 319Imported.

Entry informationi

Entry nameiD5DME4_BACMD
AccessioniPrimary (citable) accession number: D5DME4
Entry historyi
Integrated into UniProtKB/TrEMBL: June 15, 2010
Last sequence update: June 15, 2010
Last modified: April 1, 2015
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.