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Protein
Submitted name:

Alpha amylase

Gene

amyA

Organism
Pyrococcus woesei
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi49 – 491Magnesium 1; via carbonyl oxygen
Metal bindingi58 – 581Zinc 1Combined sources
Metal bindingi61 – 611Zinc 1Combined sources
Metal bindingi105 – 1051Magnesium 1
Metal bindingi105 – 1051Zinc 2Combined sources
Metal bindingi113 – 1131Magnesium 1
Metal bindingi113 – 1131Zinc 2Combined sources
Metal bindingi135 – 1351Calcium
Metal bindingi172 – 1721Zinc 3; via tele nitrogen
Metal bindingi177 – 1771Zinc 3; via tele nitrogen
Metal bindingi180 – 1801Calcium
Metal bindingi182 – 1821Calcium; via carbonyl oxygen
Metal bindingi189 – 1891Calcium
Metal bindingi191 – 1911Zinc 3
Metal bindingi227 – 2271Calcium; via carbonyl oxygen
Metal bindingi277 – 2771Magnesium 2
Metal bindingi277 – 2771Zinc 4Combined sources
Metal bindingi281 – 2811Magnesium 2
Metal bindingi281 – 2811Zinc 4Combined sources
Metal bindingi317 – 3171Magnesium 2; via carbonyl oxygen
Metal bindingi317 – 3171Zinc 4Combined sources
Metal bindingi343 – 3431Zinc 1Combined sources
Binding sitei345 – 3451GlucoseCombined sources
Metal bindingi348 – 3481Zinc 1Combined sources
Metal bindingi372 – 3721Magnesium 3
Metal bindingi372 – 3721Zinc 5Combined sources
Metal bindingi374 – 3741Magnesium 3
Metal bindingi374 – 3741Zinc 5Combined sources
Metal bindingi375 – 3751Magnesium 3
Metal bindingi375 – 3751Zinc 5Combined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseImported, Hydrolase

Keywords - Ligandi

Calcium, MagnesiumCombined sources, Metal-binding, Zinc

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Submitted name:
Alpha amylaseImported (EC:3.2.1.1Imported)
Gene namesi
Name:amyAImported
OrganismiPyrococcus woeseiImported
Taxonomic identifieri2262 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi178 ↔ 179Combined sources
Disulfide bondi413 ↔ 457

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MWOX-ray2.20A26-460[»]
1MXDX-ray2.00A26-460[»]
1MXGX-ray1.60A26-460[»]
ProteinModelPortaliQ7LYT7.
SMRiQ7LYT7. Positions 26-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni316 – 3216Glucose bindingCombined sources

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.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_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.
PRINTSiPR00110. ALPHAAMYLASE.
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7LYT7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIKKLTPLL TLLLFFIVLA SPVSAAKYLE LEEGGVIMQA FYWDVPGGGI
60 70 80 90 100
WWDHIRSKIP EWYEAGISAI WLPPPSKGMS GGYSMGYDPY DYFDLGEYYQ
110 120 130 140 150
KGTVETRFGS KEELVRLIQT AHAYGIKVIA DVVINHRAGG DLEWNPFVGD
160 170 180 190 200
YTWTDFSKVA SGKYTANYLD FHPNELHCCD EGTFGGFPDI CHHKEWDQYW
210 220 230 240 250
LWKSNESYAA YLRSIGFDGW RFDYVKGYGA WVVRDWLNWW GGWAVGEYWD
260 270 280 290 300
TNVDALLSWA YESGAKVFDF PLYYKMDEAF DNNNIPALVY ALQNGQTVVS
310 320 330 340 350
RDPFKAVTFV ANHDTDIIWN KYPAYAFILT YEGQPVIFYR DFEEWLNKDK
360 370 380 390 400
LINLIWIHDH LAGGSTTIVY YDNDELIFVR NGDSRRPGLI TYINLSPNWV
410 420 430 440 450
GRWVYVPKFA GACIHEYTGN LGGWVDKRVD SSGWVYLEAP PHDPANGYYG
460
YSVWSYCGVG
Length:460
Mass (Da):52,910
Last modified:July 5, 2004 - v1
Checksum:i0E0A2AEB5FCAF541
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF177906 Genomic DNA. Translation: AAD54338.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF177906 Genomic DNA. Translation: AAD54338.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MWOX-ray2.20A26-460[»]
1MXDX-ray2.00A26-460[»]
1MXGX-ray1.60A26-460[»]
ProteinModelPortaliQ7LYT7.
SMRiQ7LYT7. Positions 26-460.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_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.
PRINTSiPR00110. ALPHAAMYLASE.
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and Expression of Alpha Amylase from Pyrococcus woesei."
    Chunlin Lu, Weizheng J., Yunyan Y.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: DSM3773Imported.
  2. "Differential regulation of a hyperthermophilic alpha-amylase with a novel (Ca,Zn) two-metal center by zinc."
    Linden A., Mayans O., Meyer-Klaucke W., Antranikian G., Wilmanns M.
    J. Biol. Chem. 278:9875-9884(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 26-460 IN COMPLEX WITH CALCIUM; GLUCOSE; MAGNESIUM AND ZINC, DISULFIDE BONDS.

Entry informationi

Entry nameiQ7LYT7_PYRWO
AccessioniPrimary (citable) accession number: Q7LYT7
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: May 27, 2015
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structure

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.