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Protein

Retaining alpha-galactosidase

Gene

BT_1871

Organism
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Galactosidase that is able to hydrolyze the alpha-1,6 disaccharide melibiose and the synthetic p-nitrophenyl alpha-galactoside substrate (pNP-Gal), with retention of the anomeric configuration. Does not hydrolyze DNP-Glc or pNP-Glc.2 Publications

Catalytic activityi

Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.2 Publications

Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.1 Publication

Enzyme regulationi

Inhibited by EDTA in vitro.1 Publication

Kineticsi

kcat is 244 sec(-1) with p-nitrophenyl alpha-galactoside as substrate (at pH 6.0 and 37 degrees Celsius).

  1. KM=0.31 mM for p-nitrophenyl alpha-galactoside (at pH 6.0 and 37 degrees Celsius)2 Publications
  2. KM=1.5 mM for melibiose (at pH 6.6 and 37 degrees Celsius)2 Publications

    pH dependencei

    Optimum pH is 8.0 with p-nitrophenyl alpha-galactoside as substrate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi174 – 1741Calcium1 Publication
    Active sitei415 – 4151Nucleophile1 Publication
    Metal bindingi464 – 4641Calcium1 Publication
    Active sitei470 – 4701Proton donor/proton acceptor1 Publication
    Metal bindingi470 – 4701Calcium1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BioCyciBTHE226186:GJXV-1909-MONOMER.
    BRENDAi3.2.1.22. 709.
    SABIO-RKQ8A6L0.

    Protein family/group databases

    CAZyiGH97. Glycoside Hydrolase Family 97.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Retaining alpha-galactosidase (EC:3.2.1.22)
    Alternative name(s):
    BtGH97b
    Melibiase
    Gene namesi
    Ordered Locus Names:BT_1871
    OrganismiBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
    Taxonomic identifieri226186 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
    Proteomesi
    • UP000001414 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi415 – 4151D → N or G: Loss of catalytic activity. The activity is restored by adding an external nucleophilic azide ion. 1 Publication
    Mutagenesisi470 – 4701E → Q: Loss of catalytic activity. No change in substrate affinity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence analysisAdd
    BLAST
    Chaini20 – 662643Retaining alpha-galactosidasePRO_0000415272Add
    BLAST

    Proteomic databases

    PaxDbiQ8A6L0.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi226186.BT_1871.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 4819Combined sources
    Beta strandi51 – 6313Combined sources
    Turni70 – 723Combined sources
    Beta strandi75 – 8814Combined sources
    Turni90 – 934Combined sources
    Beta strandi94 – 10815Combined sources
    Turni109 – 1113Combined sources
    Beta strandi112 – 1198Combined sources
    Beta strandi122 – 1298Combined sources
    Beta strandi135 – 1428Combined sources
    Beta strandi151 – 1544Combined sources
    Helixi165 – 1684Combined sources
    Beta strandi178 – 1814Combined sources
    Helixi182 – 1843Combined sources
    Beta strandi195 – 2006Combined sources
    Beta strandi203 – 2108Combined sources
    Beta strandi219 – 23214Combined sources
    Beta strandi237 – 2448Combined sources
    Helixi245 – 2473Combined sources
    Beta strandi249 – 2557Combined sources
    Beta strandi257 – 2626Combined sources
    Beta strandi270 – 2789Combined sources
    Helixi279 – 2846Combined sources
    Helixi287 – 2904Combined sources
    Beta strandi306 – 3094Combined sources
    Turni312 – 3165Combined sources
    Beta strandi326 – 3283Combined sources
    Helixi329 – 34113Combined sources
    Beta strandi346 – 3494Combined sources
    Helixi370 – 37910Combined sources
    Beta strandi383 – 3897Combined sources
    Helixi390 – 3945Combined sources
    Helixi397 – 40711Combined sources
    Beta strandi411 – 4155Combined sources
    Helixi422 – 43716Combined sources
    Beta strandi441 – 4444Combined sources
    Helixi453 – 4564Combined sources
    Beta strandi460 – 4634Combined sources
    Helixi469 – 4735Combined sources
    Helixi481 – 4855Combined sources
    Helixi488 – 4903Combined sources
    Helixi492 – 4954Combined sources
    Beta strandi505 – 5084Combined sources
    Beta strandi517 – 5193Combined sources
    Beta strandi522 – 5243Combined sources
    Helixi526 – 53510Combined sources
    Beta strandi539 – 5435Combined sources
    Helixi547 – 5515Combined sources
    Helixi554 – 5629Combined sources
    Beta strandi568 – 5769Combined sources
    Turni577 – 5793Combined sources
    Beta strandi580 – 5878Combined sources
    Beta strandi590 – 5978Combined sources
    Beta strandi602 – 6076Combined sources
    Beta strandi616 – 6238Combined sources
    Turni625 – 6295Combined sources
    Beta strandi634 – 6418Combined sources
    Beta strandi646 – 6516Combined sources
    Beta strandi656 – 6627Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3A24X-ray2.30A/B27-662[»]
    ProteinModelPortaliQ8A6L0.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8A6L0.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 97 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000291494.
    KOiK01187.
    OMAiFIRMMAG.
    OrthoDBiPOG091H0JWM.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR029483. GH97_C.
    IPR019563. GH97_catalytic.
    IPR029486. GH97_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF14509. GH97_C. 1 hit.
    PF14508. GH97_N. 1 hit.
    PF10566. Glyco_hydro_97. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8A6L0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKKLTFLLLC VLCTLSLQAQ KQFTLASPDG NLKTTITIGD RLTYDITCNG
    60 70 80 90 100
    RQILTPSPIS MTLDNGTVWG ENAKLSGTSR KSVDEMIPSP FYRASELRNH
    110 120 130 140 150
    YNGLTLRFKK DWNVEFRAYN DGIAYRFVNQ GKKPFRVVTE VSDYCFPSDM
    160 170 180 190 200
    TASVPYVKSG KDGDYNSQFF NSFENTYTTD KLSKLNKQRL MFLPLVVDAG
    210 220 230 240 250
    DGVKVCITES DLENYPGLYL SASEGANRLS SMHAPYPKRT VQGGHNQLQM
    260 270 280 290 300
    LVKEHEDYIA KVDKPRNFPW RIAVVTTTDK DLAATNLSYL LGAPSRMSDL
    310 320 330 340 350
    SWIKPGKVAW DWWNDWNLDG VDFVTGVNNP TYKAYIDFAS ANGIEYVILD
    360 370 380 390 400
    EGWAVNLQAD LMQVVKEIDL KELVDYAASK NVGIILWAGY HAFERDMENV
    410 420 430 440 450
    CRHYAEMGVK GFKVDFMDRD DQEMTAFNYR AAEMCAKYKL ILDLHGTHKP
    460 470 480 490 500
    AGLNRTYPNV LNFEGVNGLE QMKWSSPSVD QVKYDVMIPF IRQVSGPMDY
    510 520 530 540 550
    TQGAMRNASK GNYYPCYSEP MSQGTRCRQL ALYVVFESPF NMLCDTPSNY
    560 570 580 590 600
    MREPESTAFI AEIPTVWDES IVLDGKMGEY IVTARRKGDV WYVGGITDWS
    610 620 630 640 650
    ARDIEVDCSF LGDKSYHATL FKDGVNAHRA GRDYKCESFP IKKDGKLKVH
    660
    LAPGGGFALK IK
    Length:662
    Mass (Da):74,850
    Last modified:June 1, 2003 - v1
    Checksum:i18A74C4AA328CE80
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE015928 Genomic DNA. Translation: AAO76978.1.
    RefSeqiNP_810784.1. NC_004663.1.
    WP_011108029.1. NC_004663.1.

    Genome annotation databases

    EnsemblBacteriaiAAO76978; AAO76978; BT_1871.
    GeneIDi1075689.
    KEGGibth:BT_1871.
    PATRICi21058667. VBIBacThe70966_1923.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE015928 Genomic DNA. Translation: AAO76978.1.
    RefSeqiNP_810784.1. NC_004663.1.
    WP_011108029.1. NC_004663.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3A24X-ray2.30A/B27-662[»]
    ProteinModelPortaliQ8A6L0.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi226186.BT_1871.

    Protein family/group databases

    CAZyiGH97. Glycoside Hydrolase Family 97.

    Proteomic databases

    PaxDbiQ8A6L0.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAO76978; AAO76978; BT_1871.
    GeneIDi1075689.
    KEGGibth:BT_1871.
    PATRICi21058667. VBIBacThe70966_1923.

    Phylogenomic databases

    HOGENOMiHOG000291494.
    KOiK01187.
    OMAiFIRMMAG.
    OrthoDBiPOG091H0JWM.

    Enzyme and pathway databases

    BioCyciBTHE226186:GJXV-1909-MONOMER.
    BRENDAi3.2.1.22. 709.
    SABIO-RKQ8A6L0.

    Miscellaneous databases

    EvolutionaryTraceiQ8A6L0.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR029483. GH97_C.
    IPR019563. GH97_catalytic.
    IPR029486. GH97_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF14509. GH97_C. 1 hit.
    PF14508. GH97_N. 1 hit.
    PF10566. Glyco_hydro_97. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAGAL_BACTN
    AccessioniPrimary (citable) accession number: Q8A6L0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 25, 2012
    Last sequence update: June 1, 2003
    Last modified: September 7, 2016
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    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

    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.