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O06994

- O16G1_BACSU

UniProt

O06994 - O16G1_BACSU

Protein

Oligo-1,6-glucosidase 1

Gene

malL

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Hydrolyzes various disaccharides such as sucrose, maltose, and isomaltose with different efficiencies. Also hydrolyzes longer maltodextrins from maltotriose up to maltohexaose, but not maltoheptaose, palatinose, isomaltotriose, or isomaltotetraose.

    Catalytic activityi

    Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.

    Temperature dependencei

    Optimum temperature is 42 degrees Celsius.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei199 – 1991NucleophileBy similarity
    Active sitei255 – 2551Proton donorBy similarity
    Sitei332 – 3321Transition state stabilizerBy similarity

    GO - Molecular functioni

    1. cation binding Source: InterPro
    2. oligo-1,6-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciBSUB:BSU34560-MONOMER.

    Protein family/group databases

    CAZyiGH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Oligo-1,6-glucosidase 1 (EC:3.2.1.10)
    Alternative name(s):
    Dextrin 6-alpha-D-glucanohydrolase
    Oligosaccharide alpha-1,6-glucosidase 1
    Sucrase-isomaltase 1
    Short name:
    Isomaltase 1
    Gene namesi
    Name:malL
    Synonyms:yvdL
    Ordered Locus Names:BSU34560
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU34560. [Micado]

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 561561Oligo-1,6-glucosidase 1PRO_0000054317Add
    BLAST

    Proteomic databases

    PaxDbiO06994.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU34560.

    Structurei

    Secondary structure

    1
    561
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni4 – 63
    Beta strandi10 – 134
    Helixi15 – 173
    Beta strandi21 – 266
    Helixi29 – 4214
    Beta strandi46 – 494
    Turni58 – 614
    Beta strandi65 – 706
    Turni72 – 743
    Helixi77 – 8913
    Beta strandi93 – 986
    Helixi108 – 1136
    Helixi122 – 1243
    Beta strandi145 – 1528
    Turni153 – 1564
    Beta strandi157 – 1604
    Helixi175 – 19016
    Beta strandi195 – 1984
    Helixi201 – 2033
    Beta strandi220 – 2223
    Helixi225 – 2273
    Helixi233 – 24311
    Helixi245 – 2473
    Beta strandi251 – 2555
    Helixi261 – 2688
    Helixi270 – 2723
    Beta strandi276 – 2794
    Turni282 – 2843
    Helixi295 – 2973
    Helixi304 – 31714
    Beta strandi319 – 3224
    Beta strandi324 – 3263
    Helixi336 – 3405
    Helixi347 – 35913
    Beta strandi361 – 3688
    Helixi371 – 3733
    Helixi382 – 3843
    Helixi388 – 39710
    Turni398 – 4003
    Helixi406 – 41611
    Helixi418 – 4214
    Beta strandi428 – 4303
    Helixi431 – 4344
    Turni446 – 4505
    Helixi453 – 4586
    Helixi463 – 47614
    Helixi479 – 4824
    Beta strandi486 – 4894
    Beta strandi493 – 50210
    Beta strandi505 – 5128
    Beta strandi514 – 5163
    Beta strandi518 – 5214
    Helixi524 – 5263
    Beta strandi531 – 5388
    Beta strandi547 – 5504
    Beta strandi555 – 5606

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4M56X-ray2.30A/B1-561[»]
    4M8UX-ray1.45A1-561[»]
    4MAZX-ray1.60A1-561[»]
    4MB1X-ray1.40A1-561[»]
    ProteinModelPortaliO06994.
    SMRiO06994. Positions 2-559.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    Phylogenomic databases

    eggNOGiCOG0366.
    HOGENOMiHOG000220641.
    KOiK01182.
    OMAiVGWNSLY.
    OrthoDBiEOG6RVFV2.
    PhylomeDBiO06994.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 2 hits.
    InterProiIPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 1 hit.
    PfamiPF00128. Alpha-amylase. 1 hit.
    [Graphical view]
    SMARTiSM00642. Aamy. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O06994-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEWWKEAVV YQIYPRSFYD ANGDGFGDLQ GVIQKLDYIK NLGADVIWLS    50
    PVFDSPQDDN GYDISDYKNM YEKFGTNEDM FQLIDEVHKR GMKIVMDLVV 100
    NHTSDEHAWF AESRKSKDNP YRDYYLWKDP KPDGSEPNNW GSIFSGSAWT 150
    YDEGTGQYYL HYFSKKQPDL NWENEAVRRE VYDVMRFWMD RGVDGWRMDV 200
    IGSISKYTDF PDYETDHSRS YIVGRYHSNG PRLHEFIQEM NREVLSHYDC 250
    MTVGEANGSD IEEAKKYTDA SRQELNMIFT FEHMDIDKEQ NSPNGKWQIK 300
    PFDLIALKKT MTRWQTGLMN VGWNTLYFEN HDQPRVISRW GNDRKLRKEC 350
    AKAFATVLHG MKGTPFIYQG EEIGMVNSDM PLEMYDDLEI KNAYRELVVE 400
    NKTMSEKEFV KAVMIKGRDH ARTPMQWDAG KHAGFTAGDP WIPVNSRYQD 450
    INVKESLEDQ DSIFFYYQKL IQLRKQYKIM IYGDYQLLQE NDPQVFSYLR 500
    EYRGEKLLVV VNLSEEKALF EAPPELIHER WKVLISNYPQ ERADLKSISL 550
    KPYEAVMGIS I 561
    Length:561
    Mass (Da):66,081
    Last modified:July 1, 1997 - v1
    Checksum:i2B43E9A4AD65A222
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z94043 Genomic DNA. Translation: CAB08041.1.
    AL009126 Genomic DNA. Translation: CAB15461.1.
    PIRiD70034.
    RefSeqiNP_391336.1. NC_000964.3.
    WP_003243333.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB15461; CAB15461; BSU34560.
    GeneIDi938623.
    KEGGibsu:BSU34560.
    PATRICi18978916. VBIBacSub10457_3620.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z94043 Genomic DNA. Translation: CAB08041.1 .
    AL009126 Genomic DNA. Translation: CAB15461.1 .
    PIRi D70034.
    RefSeqi NP_391336.1. NC_000964.3.
    WP_003243333.1. NZ_CM000487.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4M56 X-ray 2.30 A/B 1-561 [» ]
    4M8U X-ray 1.45 A 1-561 [» ]
    4MAZ X-ray 1.60 A 1-561 [» ]
    4MB1 X-ray 1.40 A 1-561 [» ]
    ProteinModelPortali O06994.
    SMRi O06994. Positions 2-559.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU34560.

    Protein family/group databases

    CAZyi GH13. Glycoside Hydrolase Family 13.

    Proteomic databases

    PaxDbi O06994.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15461 ; CAB15461 ; BSU34560 .
    GeneIDi 938623.
    KEGGi bsu:BSU34560.
    PATRICi 18978916. VBIBacSub10457_3620.

    Organism-specific databases

    GenoListi BSU34560. [Micado ]

    Phylogenomic databases

    eggNOGi COG0366.
    HOGENOMi HOG000220641.
    KOi K01182.
    OMAi VGWNSLY.
    OrthoDBi EOG6RVFV2.
    PhylomeDBi O06994.

    Enzyme and pathway databases

    BioCyci BSUB:BSU34560-MONOMER.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 2 hits.
    InterProi IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 1 hit.
    [Graphical view ]
    SMARTi SM00642. Aamy. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Denizot F.
      Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
      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.
      , 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "Identification and enzymatic characterization of the maltose-inducible alpha-glucosidase MalL (sucrase-isomaltase-maltase) of Bacillus subtilis."
      Schoenert S., Buder T., Dahl M.K.
      J. Bacteriol. 180:2574-2578(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    4. "Properties of maltose-inducible alpha-glucosidase MalL (sucrase-isomaltase-maltase) in Bacillus subtilis: evidence for its contribution to maltodextrin utilization."
      Schoenert S., Buder T., Dahl M.K.
      Res. Microbiol. 150:167-177(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.

    Entry informationi

    Entry nameiO16G1_BACSU
    AccessioniPrimary (citable) accession number: O06994
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2001
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 102 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. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3