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Reviewed, UniProtKB/Swiss-Prot O34645 (AGAL_BACSU)

Last modified November 25, 2008. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Alpha-galactosidase
    EC=3.2.1.22
Alternative name(s):
    Melibiase
Gene names
Name: melA
Ordered Locus Names: BSU30300
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase.

Cofactor

Binds 1 manganese ion per subunit By similarity.

Binds 1 NAD per subunit By similarity.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 4 family.

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Ontologies

Keywords

   Biological processCarbohydrate metabolism
   LigandManganese
Metal-binding
NAD
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionalpha-galactosidase activity

Inferred from electronic annotation. Source: EC

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Alpha-galactosidase
PRO_0000169851

Regions

Nucleotide binding2 – 6867NAD By similarity

Sites

Active site1701Proton donor By similarity
Metal binding1691Manganese By similarity
Metal binding1991Manganese By similarity
Binding site1481Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
O34645-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: E773A01018E65562

FASTA43249,264
        10         20         30         40         50         60 
MKKITFIGAG STIFAKNVLG DCLLTEALNG FEFALYDIDP KRLQESQLML ENLRDRYNPS 

        70         80         90        100        110        120 
VAINSYDDRK LALQNAGYVI NAIQVGGYKP STVIDFEIPK RYGLRQTIAD TVGIGGIFRS 

       130        140        150        160        170        180 
LRTIPVLFDI AKDMEEMCPD AWFLNYTNPM ATLTGAMLRY TNIKTIGLCH SVQVCTKDLF 

       190        200        210        220        230        240 
KALGMEHDGI EERIAGINHM AWLLEVKKDG TDLYPEIKRR AKEKQKTKHH DMVRFELMDK 

       250        260        270        280        290        300 
FGYYVTESSE HNAEYHPYFI KRNYPELISE LQIPLDEYPR RCVKQIENWE KMRDDIVNNK 

       310        320        330        340        350        360 
NLTHERSKEY GSRIIEAMET NEPFTFGGNV LNTGLITNLP SKAVVEVTCV ADRKKITPCF 

       370        380        390        400        410        420 
AGELPEQLAA LNRTNINTQL MTIEAAVTRK KEAVYQAAML DPHTSAELSM KDIISMCDDL 

       430 
FAAHGDWLPE YK

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References

« Hide 'large scale' references
[1]"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
Lapidus A., Galleron N., Sorokin A., Ehrlich S.-D.
Microbiology 143:3431-3441(1997) [PubMed: 9387221] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

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Cross-references

Sequence databases

AF008220 Genomic DNA. Translation: AAC00383.1.
Z99119 Genomic DNA. Translation: CAB15008.1.
PIRE69656.
RefSeqNP_390908.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID937255.
GenomeReviewsGene locus BSU30300 in contig AL009126_GR.
KEGGbsu:BSU30300.
NMPDRfig|224308.1.peg.3033.

Organism-specific databases

SubtiListBG12615. melA. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMO34645.

Enzyme and pathway databases

BioCycBSUB224308:BSU3025-MON.

Family and domain databases

InterProIPR001088. Glyco_hydro_4.
IPR015955. Lactate_DHase/Glyco_Ohase_4_C.
[Graphical view]
Gene3DG3DSA:3.90.110.10. lact_mal_DH. 1 hit.
PfamPF02056. Glyco_hydro_4. 1 hit.
[Graphical view]
PRINTSPR00732. GLHYDRLASE4.
ProDomPD006892. Glyco_hydro_4. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS01324. GLYCOSYL_HYDROL_F4. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAGAL_BACSU
AccessionPrimary (citable) accession number: O34645
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: November 25, 2008
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents