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O34364

- O16G2_BACSU

UniProt

O34364 - O16G2_BACSU

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Protein

Probable oligo-1,6-glucosidase 2

Gene

ycdG

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei199 – 1991NucleophileBy similarity
Active sitei255 – 2551Proton donorBy similarity
Sitei330 – 3301Transition 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:BSU02840-MONOMER.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable oligo-1,6-glucosidase 2 (EC:3.2.1.10)
Alternative name(s):
Oligosaccharide alpha-1,6-glucosidase 2
Sucrase-isomaltase 2
Short name:
Isomaltase 2
Gene namesi
Name:ycdG
Ordered Locus Names:BSU02840
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU02840.

Subcellular locationi

Cytoplasm By similarity

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 – 561561Probable oligo-1,6-glucosidase 2PRO_0000360818Add
BLAST

Proteomic databases

PaxDbiO34364.

Expressioni

Inductioni

By ethanol, heat and salt via sigma B-dependent promoter.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU02840.

Structurei

3D structure databases

ProteinModelPortaliO34364.
SMRiO34364. Positions 1-558.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Phylogenomic databases

eggNOGiCOG0366.
HOGENOMiHOG000220641.
InParanoidiO34364.
KOiK01182.
OMAiEERNDQT.
OrthoDBiEOG6RVFV2.
PhylomeDBiO34364.

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.

O34364-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKTDWWKDAV VYQIYPRSFQ DSNGDGIGDL RGIISRLDYI KELGADVIWI
60 70 80 90 100
CPIYPSPNVD YGYDVTNHKA IMDSYGTMDD FHELLDQVHQ RGLKLVMDFV
110 120 130 140 150
LNHTSVEHPW FKEAELDKNS KYRSYYYWRP GTKNGPPTDW LSNYGCPVWQ
160 170 180 190 200
YEEHTGEYYL HMNAVKQADL NWENPEVRQA VYDMMKFWLD KGVDGLRIDQ
210 220 230 240 250
LHLISKKEYL PSYEDYINQQ AEPKPFQPNG ERIHDYLKEI TDEVFSHYDV
260 270 280 290 300
MSVGEVGSVT PEEGLKYTGT DKHELNMIFH FQHMELDQQP GKEHWDLKPL
310 320 330 340 350
ELSDLKSVLT KWQKKLEHQG WNTLFWCNHD QPRIVSRFGD DGEYRKASAK
360 370 380 390 400
MLAAVIYFMK GTPYIYQGEE IGMTNAPFTR IEDYKDIQTI NMYHKRVFEK
410 420 430 440 450
GYDPNDVMRS ILAKSRDHAR TPMQWNSGKN AGFTDGTPWL KVNPNFTAIN
460 470 480 490 500
VEEAQGDPDS VLNYYKKLIS LRKQYADLMK GSFDLLLPDD PQLFVYMREN
510 520 530 540 550
SKQQLLSVNN FSKEQAVFQW PKNCGKAQAS LLLSNYNNDD LDDEMVFRPY
560
ESRVYLLDKT N
Length:561
Mass (Da):65,816
Last modified:January 1, 1998 - v1
Checksum:i1E879220CAE04BBF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB000617 Genomic DNA. Translation: BAA22245.1.
AL009126 Genomic DNA. Translation: CAB12078.1.
PIRiH69755.
RefSeqiNP_388166.1. NC_000964.3.
WP_003234736.1. NZ_CM000487.1.

Genome annotation databases

EnsemblBacteriaiCAB12078; CAB12078; BSU02840.
GeneIDi938375.
KEGGibsu:BSU02840.
PATRICi18972127. VBIBacSub10457_0292.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB000617 Genomic DNA. Translation: BAA22245.1 .
AL009126 Genomic DNA. Translation: CAB12078.1 .
PIRi H69755.
RefSeqi NP_388166.1. NC_000964.3.
WP_003234736.1. NZ_CM000487.1.

3D structure databases

ProteinModelPortali O34364.
SMRi O34364. Positions 1-558.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU02840.

Protein family/group databases

CAZyi GH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbi O34364.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12078 ; CAB12078 ; BSU02840 .
GeneIDi 938375.
KEGGi bsu:BSU02840.
PATRICi 18972127. VBIBacSub10457_0292.

Organism-specific databases

GenoListi BSU02840.

Phylogenomic databases

eggNOGi COG0366.
HOGENOMi HOG000220641.
InParanoidi O34364.
KOi K01182.
OMAi EERNDQT.
OrthoDBi EOG6RVFV2.
PhylomeDBi O34364.

Enzyme and pathway databases

BioCyci BSUB:BSU02840-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. "A 32 kb nucleotide sequence from the region of the lincomycin-resistance gene (22 degrees-25 degrees) of the Bacillus subtilis chromosome and identification of the site of the lin-2 mutation."
    Kumano M., Tamakoshi A., Yamane K.
    Microbiology 143:2775-2782(1997) [PubMed] [Europe PMC] [Abstract]
    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. "Global analysis of the general stress response of Bacillus subtilis."
    Petersohn A., Brigulla M., Haas S., Hoheisel J.D., Voelker U., Hecker M.
    J. Bacteriol. 183:5617-5631(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiO16G2_BACSU
AccessioniPrimary (citable) accession number: O34364
Secondary accession number(s): Q797R7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 91 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3