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O06994

- O16G1_BACSU

UniProt

O06994 - O16G1_BACSU

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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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

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.
InParanoidiO06994.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEWWKEAVV YQIYPRSFYD ANGDGFGDLQ GVIQKLDYIK NLGADVIWLS
60 70 80 90 100
PVFDSPQDDN GYDISDYKNM YEKFGTNEDM FQLIDEVHKR GMKIVMDLVV
110 120 130 140 150
NHTSDEHAWF AESRKSKDNP YRDYYLWKDP KPDGSEPNNW GSIFSGSAWT
160 170 180 190 200
YDEGTGQYYL HYFSKKQPDL NWENEAVRRE VYDVMRFWMD RGVDGWRMDV
210 220 230 240 250
IGSISKYTDF PDYETDHSRS YIVGRYHSNG PRLHEFIQEM NREVLSHYDC
260 270 280 290 300
MTVGEANGSD IEEAKKYTDA SRQELNMIFT FEHMDIDKEQ NSPNGKWQIK
310 320 330 340 350
PFDLIALKKT MTRWQTGLMN VGWNTLYFEN HDQPRVISRW GNDRKLRKEC
360 370 380 390 400
AKAFATVLHG MKGTPFIYQG EEIGMVNSDM PLEMYDDLEI KNAYRELVVE
410 420 430 440 450
NKTMSEKEFV KAVMIKGRDH ARTPMQWDAG KHAGFTAGDP WIPVNSRYQD
460 470 480 490 500
INVKESLEDQ DSIFFYYQKL IQLRKQYKIM IYGDYQLLQE NDPQVFSYLR
510 520 530 540 550
EYRGEKLLVV VNLSEEKALF EAPPELIHER WKVLISNYPQ ERADLKSISL
560
KPYEAVMGIS I
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.
InParanoidi O06994.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 103 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