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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)DescriptionActionsGraphical viewLength
    Metal bindingi174Calcium1 Publication1
    Active sitei415Nucleophile1 Publication1
    Metal bindingi464Calcium1 Publication1
    Active sitei470Proton donor/proton acceptor1 Publication1
    Metal bindingi470Calcium1 Publication1

    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

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi415D → N or G: Loss of catalytic activity. The activity is restored by adding an external nucleophilic azide ion. 1 Publication1
    Mutagenesisi470E → Q: Loss of catalytic activity. No change in substrate affinity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 19Sequence analysisAdd BLAST19
    ChainiPRO_000041527220 – 662Retaining alpha-galactosidaseAdd BLAST643

    Proteomic databases

    PaxDbiQ8A6L0.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi226186.BT_1871.

    Structurei

    Secondary structure

    1662
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi30 – 48Combined sources19
    Beta strandi51 – 63Combined sources13
    Turni70 – 72Combined sources3
    Beta strandi75 – 88Combined sources14
    Turni90 – 93Combined sources4
    Beta strandi94 – 108Combined sources15
    Turni109 – 111Combined sources3
    Beta strandi112 – 119Combined sources8
    Beta strandi122 – 129Combined sources8
    Beta strandi135 – 142Combined sources8
    Beta strandi151 – 154Combined sources4
    Helixi165 – 168Combined sources4
    Beta strandi178 – 181Combined sources4
    Helixi182 – 184Combined sources3
    Beta strandi195 – 200Combined sources6
    Beta strandi203 – 210Combined sources8
    Beta strandi219 – 232Combined sources14
    Beta strandi237 – 244Combined sources8
    Helixi245 – 247Combined sources3
    Beta strandi249 – 255Combined sources7
    Beta strandi257 – 262Combined sources6
    Beta strandi270 – 278Combined sources9
    Helixi279 – 284Combined sources6
    Helixi287 – 290Combined sources4
    Beta strandi306 – 309Combined sources4
    Turni312 – 316Combined sources5
    Beta strandi326 – 328Combined sources3
    Helixi329 – 341Combined sources13
    Beta strandi346 – 349Combined sources4
    Helixi370 – 379Combined sources10
    Beta strandi383 – 389Combined sources7
    Helixi390 – 394Combined sources5
    Helixi397 – 407Combined sources11
    Beta strandi411 – 415Combined sources5
    Helixi422 – 437Combined sources16
    Beta strandi441 – 444Combined sources4
    Helixi453 – 456Combined sources4
    Beta strandi460 – 463Combined sources4
    Helixi469 – 473Combined sources5
    Helixi481 – 485Combined sources5
    Helixi488 – 490Combined sources3
    Helixi492 – 495Combined sources4
    Beta strandi505 – 508Combined sources4
    Beta strandi517 – 519Combined sources3
    Beta strandi522 – 524Combined sources3
    Helixi526 – 535Combined sources10
    Beta strandi539 – 543Combined sources5
    Helixi547 – 551Combined sources5
    Helixi554 – 562Combined sources9
    Beta strandi568 – 576Combined sources9
    Turni577 – 579Combined sources3
    Beta strandi580 – 587Combined sources8
    Beta strandi590 – 597Combined sources8
    Beta strandi602 – 607Combined sources6
    Beta strandi616 – 623Combined sources8
    Turni625 – 629Combined sources5
    Beta strandi634 – 641Combined sources8
    Beta strandi646 – 651Combined sources6
    Beta strandi656 – 662Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3A24X-ray2.30A/B27-662[»]
    5E1QX-ray1.94A/B27-662[»]
    ProteinModelPortaliQ8A6L0.
    SMRiQ8A6L0.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3A24X-ray2.30A/B27-662[»]
    5E1QX-ray1.94A/B27-662[»]
    ProteinModelPortaliQ8A6L0.
    SMRiQ8A6L0.
    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

    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: November 30, 2016
    This is version 70 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.