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Protein
Submitted name:

Alpha-galactosidase AgaB

Gene

agaB

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. alpha-galactosidase activity Source: InterPro

GO - Biological processi

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

Protein family/group databases

CAZyiGH36. Glycoside Hydrolase Family 36.

Names & Taxonomyi

Protein namesi
Submitted name:
Alpha-galactosidase AgaBImported
Gene namesi
Name:agaBImported
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)Imported
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FNQX-ray1.80A1-729[»]
ProteinModelPortaliQ934H7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002252. Glyco_hydro_36.
IPR000111. Glyco_hydro_GHD.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02065. Melibiase. 1 hit.
[Graphical view]
PIRSFiPIRSF005536. Agal. 1 hit.
PRINTSiPR00743. GLHYDRLASE36.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q934H7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVTYNPQTK QFHLRAGKAS YVMQLFRSGY LAHIYWGKAV RDVRGERRFS
60 70 80 90 100
RLDRAFSPNP DPSDRTFSLD TLPQEYPAYG NTDFRSPAYQ VQLENGSTVT
110 120 130 140 150
DLRYKTHRIY KGKPRLNGLP ATYVEHEQEA ETLEIVLGDA LIGLEVTLQY
160 170 180 190 200
TAYEKWNVIT RAARFENKGG ERLKLLRALS MSVDFPTADY DWIHLPGAWG
210 220 230 240 250
RERWIERRPL VTGVQAAESR RGASSHQQNP FIALVAKNAD EHQGEVYGFS
260 270 280 290 300
FVYSGNFLAQ VEVDQFHTAR VSMGINPFDF TWLLQPGESF QTPEVVMVYS
310 320 330 340 350
DQGLNGMSQT YHELYRTRLA RGAFRDRERP ILINNWEATY FDFNEEKLVN
360 370 380 390 400
IAKTEAELGI ELFVLDDGWF GKRDDDRRSL GDWIVNRRKL PNGLDGLAKQ
410 420 430 440 450
VNELGMQFGL WVEPEMVSPN SELYRKHPDW CLHVPNRPRS EGRNQLVLDY
460 470 480 490 500
SREDVCDYII ETISNVLASA PITYVKWDMN RHMTEIGSSA LPPERQRETA
510 520 530 540 550
HRYMLGLYRV MDEMTSRFPH ILFESCSGGG GRFDPGMLYY MPQTWTSDNT
560 570 580 590 600
DAVSRLKIQY GTSLVYPISA MGAHVSAVPN HQVGRVASLK ARGHVAMSGN
610 620 630 640 650
FGYELDITKL TETEKQMIKQ QVAFYKDVRR LVQFGTFYRL LSPFEGNEAA
660 670 680 690 700
WMFVSADRSE ALVAYFRVLA EANAPLSYLR LKGLDPNQDY EIEGLGVYGG
710 720
DELMYAGVAL PYRSGDFISM MWRLKAVQQ
Length:729
Mass (Da):83,467
Last modified:December 1, 2001 - v1
Checksum:iDF7FF8E5D3A016C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY013287 Genomic DNA. Translation: AAG49421.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY013287 Genomic DNA. Translation: AAG49421.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FNQX-ray1.80A1-729[»]
ProteinModelPortaliQ934H7.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH36. Glycoside Hydrolase Family 36.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002252. Glyco_hydro_36.
IPR000111. Glyco_hydro_GHD.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02065. Melibiase. 1 hit.
[Graphical view]
PIRSFiPIRSF005536. Agal. 1 hit.
PRINTSiPR00743. GLHYDRLASE36.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Elucidation of functional domains in thermostable isoenzymes of alpha-galactosidase in Bacillus stearothermophilus. Enzymatic properties are encoded in a genetically exchangeable domain."
    Janz L., Ganter C., Stezowski J., Mattes R.
    (In) Reuss M., Chmiel H., Gilles E-.D., Knackmuss H-.J. (eds.); BIOCHEMICAL ENGINEERING, STUTTGART, pp.170-173, Unknown Publisher (1991)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: KVE39Imported.
  2. Watzlawick H., Ganter C., Mattes R.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: KVE39Imported.
  3. "The molecular mechanism of thermostable alpha-galactosidases AgaA and AgaB explained by x-ray crystallography and mutational studies."
    Merceron R., Foucault M., Haser R., Mattes R., Watzlawick H., Gouet P.
    J. Biol. Chem. 287:39642-39652(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).

Entry informationi

Entry nameiQ934H7_GEOSE
AccessioniPrimary (citable) accession number: Q934H7
Entry historyi
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: April 1, 2015
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.