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Protein

Alpha-galactosidase AgaA

Gene

agaA

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

Functioni

Hydrolyzes the short-chain alpha-galactosaccharides raffinose and stachyose.1 Publication

Catalytic activityi

Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.3 Publications

Enzyme regulationi

Not inhibited by D-galactose or sucrose (Ref. 1). Inhibited by pharmaceutical drug 1-deoxygalactonojirimycin (PubMed:23012371).2 Publications

Kineticsi

kcat is 105 s(-1) for p-nitrophenyl-alpha-galactopyranoside (at 25 degrees Celsius and pH 6.5). kcat is 180 s(-1) for raffinose (at 25 degrees Celsius and pH 6.5).1 Publication
  1. KM=0.21 mM for p-nitrophenyl-alpha-galactopyranoside (at 25 degrees Celsius and pH 6.5)1 Publication
  2. KM=3.8 mM for raffinose (at 25 degrees Celsius and pH 6.5)1 Publication

    pH dependencei

    Optimum pH is 6.5.1 Publication

    Temperature dependencei

    Optimum temperature is 65 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei53SubstrateCombined sources1 Publication1
    Binding sitei199SubstrateCombined sources1 Publication1
    Binding sitei443SubstrateCombined sources1 Publication1
    Active sitei478Nucleophile1 Publication1
    Binding sitei526SubstrateCombined sources1 Publication1
    Active sitei548Proton donor1 Publication1
    Binding sitei548SubstrateCombined sources1 Publication1

    GO - Molecular functioni

    • alpha-galactosidase activity Source: UniProtKB
    • raffinose alpha-galactosidase activity Source: UniProtKB-EC

    GO - Biological processi

    • protein homotetramerization Source: UniProtKB
    • raffinose catabolic process Source: UniProtKB
    • stachyose metabolic process Source: UniProtKB

    Keywordsi

    Molecular functionGlycosidase, Hydrolase
    Biological processCarbohydrate metabolism

    Protein family/group databases

    CAZyiGH36. Glycoside Hydrolase Family 36.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-galactosidase AgaA1 PublicationImported (EC:3.2.1.223 Publications)
    Gene namesi
    Name:agaA1 PublicationImported
    OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)Imported
    Taxonomic identifieri1422 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    Pathology & Biotechi

    Biotechnological usei

    Has properties that make it suitable for elimination of D-raffinose from low green syrup in sugar manufacturing process from beets in order to improve the yield of sucrose.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi336W → A: Very strongly reduced hydrolytic efficiency against raffinose, but displays medium level of transglycosylation activity compared to none with wild-type enzyme. 1 Publication1
    Mutagenesisi336W → F or S: Strongly reduced hydrolytic efficiency against raffinose, but displays high level of transglycosylation activity compared to none with wild-type enzyme. 1 Publication1
    Mutagenesisi336W → N: Very strongly reduced hydrolytic efficiency against raffinose, but displays low level of transglycosylation activity compared to none with wild-type enzyme. 1 Publication1
    Mutagenesisi478D → A: Loss of activity. 1 Publication1
    Mutagenesisi548D → N: Loss of activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004395851 – 729Alpha-galactosidase AgaAAdd BLAST729

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    Secondary structure

    1729
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi11 – 16Combined sources6
    Beta strandi19 – 26Combined sources8
    Turni27 – 29Combined sources3
    Beta strandi30 – 38Combined sources9
    Beta strandi45 – 47Combined sources3
    Beta strandi59 – 61Combined sources3
    Helixi69 – 71Combined sources3
    Beta strandi74 – 76Combined sources3
    Beta strandi79 – 82Combined sources4
    Beta strandi88 – 92Combined sources5
    Beta strandi103 – 112Combined sources10
    Helixi127 – 129Combined sources3
    Beta strandi130 – 139Combined sources10
    Turni140 – 143Combined sources4
    Beta strandi144 – 156Combined sources13
    Beta strandi158 – 167Combined sources10
    Beta strandi169 – 171Combined sources3
    Beta strandi173 – 186Combined sources14
    Beta strandi190 – 196Combined sources7
    Beta strandi206 – 209Combined sources4
    Beta strandi212 – 219Combined sources8
    Beta strandi221 – 223Combined sources3
    Beta strandi226 – 236Combined sources11
    Beta strandi241 – 244Combined sources4
    Beta strandi246 – 251Combined sources6
    Beta strandi257 – 263Combined sources7
    Beta strandi269 – 275Combined sources7
    Beta strandi282 – 284Combined sources3
    Beta strandi289 – 291Combined sources3
    Beta strandi295 – 302Combined sources8
    Helixi303 – 318Combined sources16
    Beta strandi325 – 327Combined sources3
    Beta strandi332 – 334Combined sources3
    Helixi336 – 339Combined sources4
    Helixi345 – 358Combined sources14
    Beta strandi362 – 365Combined sources4
    Beta strandi367 – 370Combined sources4
    Beta strandi374 – 378Combined sources5
    Turni387 – 389Combined sources3
    Helixi393 – 402Combined sources10
    Turni403 – 405Combined sources3
    Beta strandi407 – 412Combined sources6
    Beta strandi419 – 421Combined sources3
    Helixi422 – 426Combined sources5
    Helixi428 – 430Combined sources3
    Beta strandi441 – 444Combined sources4
    Beta strandi446 – 448Combined sources3
    Helixi453 – 468Combined sources16
    Turni469 – 471Combined sources3
    Beta strandi474 – 477Combined sources4
    Helixi493 – 498Combined sources6
    Helixi499 – 517Combined sources19
    Beta strandi522 – 525Combined sources4
    Helixi535 – 540Combined sources6
    Beta strandi541 – 545Combined sources5
    Helixi554 – 562Combined sources9
    Turni563 – 565Combined sources3
    Helixi568 – 570Combined sources3
    Beta strandi571 – 575Combined sources5
    Turni581 – 583Combined sources3
    Helixi589 – 596Combined sources8
    Beta strandi599 – 603Combined sources5
    Helixi607 – 609Combined sources3
    Helixi612 – 634Combined sources23
    Beta strandi635 – 641Combined sources7
    Turni643 – 645Combined sources3
    Beta strandi646 – 654Combined sources9
    Beta strandi658 – 667Combined sources10
    Beta strandi677 – 679Combined sources3
    Beta strandi688 – 692Combined sources5
    Turni693 – 695Combined sources3
    Beta strandi696 – 699Combined sources4
    Helixi700 – 705Combined sources6
    Beta strandi708 – 710Combined sources3
    Beta strandi715 – 726Combined sources12

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4FNPX-ray2.80A/B/C/D1-729[»]
    4FNRX-ray3.20A/B/C/D1-729[»]
    4FNSX-ray2.60A/B/C/D1-729[»]
    4FNTX-ray2.60A/B/C/D1-729[»]
    4FNUX-ray3.60A/B/C/D1-729[»]
    ProteinModelPortaliQ9ALJ4.
    SMRiQ9ALJ4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni366 – 367Substrate bindingCombined sources1 Publication2
    Regioni476 – 480Substrate bindingCombined sources1 Publication5

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 36 family.Curated

    Family and domain databases

    CDDicd14791. GH36. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    InterProiView protein in InterPro
    IPR013785. Aldolase_TIM.
    IPR000111. Glyco_hydro_27/36_CS.
    IPR002252. Glyco_hydro_36.
    IPR031705. Glyco_hydro_36_C.
    IPR031704. Glyco_hydro_36_N.
    IPR017853. Glycoside_hydrolase_SF.
    PfamiView protein in Pfam
    PF16874. Glyco_hydro_36C. 1 hit.
    PF16875. Glyco_hydro_36N. 1 hit.
    PF02065. Melibiase. 1 hit.
    PIRSFiPIRSF005536. Agal. 1 hit.
    PRINTSiPR00743. GLHYDRLASE36.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiView protein in PROSITE
    PS00512. ALPHA_GALACTOSIDASE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9ALJ4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSVAYNPQTK QFHLRAGKAS YVMQLFRSGY LAHVYWGKAV RDVRGARAFP
    60 70 80 90 100
    RLDRAFSPNP DPSDRTFSLD TLLQEYPAYG NTDFRAPAYQ VQLENGSTVT
    110 120 130 140 150
    DLRYKTHRIY KGKPRLNGLP ATYVEHEQEA ETLEIVLGDA LIGLEVTLQY
    160 170 180 190 200
    TAYEKWNVIT RSARFENKGG ERLKLLRALS MSVDFPTADY DWIHLPGAWG
    210 220 230 240 250
    RERWIERRPL VTGVQAAESR RGASSHQQNP FIALVAKNAD EHQGEVYGFS
    260 270 280 290 300
    FVYSGNFLAQ IEVDQFGTAR VSMGINPFDF TWLLQPGESF QTPEVVMVYS
    310 320 330 340 350
    DQGLNGMSQT YHELYRTRLA RGAFRDRERP ILINNWEATY FDFNEEKIVN
    360 370 380 390 400
    IARTAAELGI ELVVLDDGWF GERDDDRRSL GDWIVNRRKL PNGLDGLAKQ
    410 420 430 440 450
    VNELGLQFGL WVEPEMVSPN SELYRKHPDW CLHVPNRPRS EGRNQLVLDY
    460 470 480 490 500
    SREDVCDYII ETISNVLASA PITYVKWDMN RHMTEIGSSA LPPERQRETA
    510 520 530 540 550
    HRYMLGLYRV MDEITSRFPH ILFESCSGGG GRFDPGMLYY MPQTWTSDNT
    560 570 580 590 600
    DAVSRLKIQY GTSLVYPISA MGAHVSAVPN HQVGRVASLK TRGHVAMSGN
    610 620 630 640 650
    FGYELDITKL TETEKQMMKQ QVAFYKDVRR LVQFGTFYRL LSPFEGNEAA
    660 670 680 690 700
    WMFVSADRSE ALVAYFRVLA EANAPLSYLR LKGLDSNQDY EIEGLGVYGG
    710 720
    DELMYAGVAL PYRSSDFISM MWRLKAVQQ
    Length:729
    Mass (Da):83,211
    Last modified:June 1, 2001 - v1
    Checksum:i6E59129E1C3502A2
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY013286 Genomic DNA. Translation: AAG49420.1.

    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.

    Entry informationi

    Entry nameiAGAA_GEOSE
    AccessioniPrimary (citable) accession number: Q9ALJ4
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 12, 2017
    Last sequence update: June 1, 2001
    Last modified: July 5, 2017
    This is version 55 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families