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Protein

Mannan endo-1,4-beta-mannosidase

Gene

gmuG

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Seems to be involved in the degradation of glucomannan.1 Publication

Catalytic activityi

Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

BioCyciBSUB:BSU05880-MONOMER.
BRENDAi3.2.1.78. 658.

Protein family/group databases

CAZyiGH26. Glycoside Hydrolase Family 26.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan endo-1,4-beta-mannosidase (EC:3.2.1.78)
Alternative name(s):
1,4-beta-D-mannan mannanohydrolase
Beta-mannanase
Glucomannan utilization protein G
Gene namesi
Name:gmuG
Synonyms:ydhT
Ordered Locus Names:BSU05880
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU05880. [Micado]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 362336Mannan endo-1,4-beta-mannosidasePRO_0000360866Add
BLAST

Proteomic databases

PaxDbiO05512.

Expressioni

Inductioni

Up-regulated by konjac glucomannan and by cellobiose and mannobiose, the possible degradation products of glucomannan. Repressed by glucose via the carbon catabolite repression system. Also repressed by GmuR.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU05880.

Structurei

Secondary structure

1
362
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 4912Combined sources
Helixi50 – 523Combined sources
Beta strandi53 – 564Combined sources
Beta strandi61 – 666Combined sources
Turni67 – 704Combined sources
Helixi74 – 8310Combined sources
Beta strandi88 – 969Combined sources
Helixi104 – 1074Combined sources
Helixi113 – 1219Combined sources
Beta strandi125 – 1317Combined sources
Beta strandi137 – 1393Combined sources
Helixi148 – 1558Combined sources
Helixi160 – 18021Combined sources
Turni181 – 1833Combined sources
Beta strandi186 – 1894Combined sources
Beta strandi196 – 1994Combined sources
Helixi211 – 22919Combined sources
Beta strandi236 – 2416Combined sources
Turni250 – 2534Combined sources
Turni257 – 2593Combined sources
Beta strandi261 – 27010Combined sources
Helixi272 – 2743Combined sources
Helixi278 – 2825Combined sources
Beta strandi288 – 29710Combined sources
Helixi304 – 31411Combined sources
Beta strandi318 – 3236Combined sources
Helixi326 – 3283Combined sources
Helixi330 – 3323Combined sources
Helixi336 – 3416Combined sources
Beta strandi351 – 3533Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WHKX-ray1.70A27-362[»]
3CBWX-ray1.27A/B21-362[»]
ProteinModelPortaliO05512.
SMRiO05512. Positions 27-362.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO05512.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 26 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4124.
HOGENOMiHOG000009206.
InParanoidiO05512.
KOiK01218.
OMAiFLAWNDE.
OrthoDBiEOG6GXTPF.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR022790. EndoGluc_H/Glyco_hydro_26.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR016714. Mannan-1_4-b-mannosidase.
[Graphical view]
PfamiPF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PIRSFiPIRSF018168. Mannan-1_4-beta-mannosidase. 1 hit.
PRINTSiPR00739. GLHYDRLASE26.
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O05512-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKKHTISLL IIFLLASAVL AKPIEAHTVS PVNPNAQQTT KTVMNWLAHL
60 70 80 90 100
PNRTENRVLS GAFGGYSHDT FSMAEADRIR SATGQSPAIY GCDYARGWLE
110 120 130 140 150
TANIEDSIDV SCNGDLMSYW KNGGIPQISL HLANPAFQSG HFKTPITNDQ
160 170 180 190 200
YKKILDSSTV EGKRLNAMLS KIADGLQELE NQGVPVLFRP LHEMNGEWFW
210 220 230 240 250
WGLTSYNQKD NERISLYKQL YKKIYHYMTD TRGLDHLIWV YSPDANRDFK
260 270 280 290 300
TDFYPGASYV DIVGLDAYFQ DAYSINGYDQ LTALNKPFAF TEVGPQTANG
310 320 330 340 350
SFDYSLFINA IKQKYPKTIY FLAWNDEWSA AVNKGASALY HDSWTLNKGE
360
IWNGDSLTPI VE
Length:362
Mass (Da):40,892
Last modified:July 7, 2009 - v2
Checksum:iC7E1D527AA001B14
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531K → N in BAA19712 (PubMed:9202461).Curated
Sequence conflicti158 – 1603STV → ATA in BAA19712 (PubMed:9202461).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88802 Genomic DNA. Translation: BAA19712.1.
AL009126 Genomic DNA. Translation: CAB12407.2.
PIRiH69785.
RefSeqiNP_388469.2. NC_000964.3.
WP_003244107.1. NZ_JNCM01000031.1.

Genome annotation databases

EnsemblBacteriaiCAB12407; CAB12407; BSU05880.
GeneIDi938034.
KEGGibsu:BSU05880.
PATRICi18972792. VBIBacSub10457_0617.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88802 Genomic DNA. Translation: BAA19712.1.
AL009126 Genomic DNA. Translation: CAB12407.2.
PIRiH69785.
RefSeqiNP_388469.2. NC_000964.3.
WP_003244107.1. NZ_JNCM01000031.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WHKX-ray1.70A27-362[»]
3CBWX-ray1.27A/B21-362[»]
ProteinModelPortaliO05512.
SMRiO05512. Positions 27-362.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU05880.

Protein family/group databases

CAZyiGH26. Glycoside Hydrolase Family 26.

Proteomic databases

PaxDbiO05512.

Protocols and materials databases

DNASUi938034.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12407; CAB12407; BSU05880.
GeneIDi938034.
KEGGibsu:BSU05880.
PATRICi18972792. VBIBacSub10457_0617.

Organism-specific databases

GenoListiBSU05880. [Micado]

Phylogenomic databases

eggNOGiCOG4124.
HOGENOMiHOG000009206.
InParanoidiO05512.
KOiK01218.
OMAiFLAWNDE.
OrthoDBiEOG6GXTPF.

Enzyme and pathway databases

BioCyciBSUB:BSU05880-MONOMER.
BRENDAi3.2.1.78. 658.

Miscellaneous databases

EvolutionaryTraceiO05512.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR022790. EndoGluc_H/Glyco_hydro_26.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR016714. Mannan-1_4-b-mannosidase.
[Graphical view]
PfamiPF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PIRSFiPIRSF018168. Mannan-1_4-beta-mannosidase. 1 hit.
PRINTSiPR00739. GLHYDRLASE26.
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the Bacillus subtilis chromosome."
    Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y., Ogasawara N.
    Microbiology 143:1861-1866(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / JH642.
  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. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 153; 158 AND 160.
  4. "Proteome analysis of Bacillus subtilis extracellular proteins: a two-dimensional protein electrophoretic study."
    Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.
    Microbiology 146:65-75(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-37.
    Strain: 168.
  5. "Glucomannan utilization operon of Bacillus subtilis."
    Sadaie Y., Nakadate H., Fukui R., Yee L.M., Asai K.
    FEMS Microbiol. Lett. 279:103-109(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, FUNCTION IN GLUCOMANNAN UTILIZATION.
    Strain: 168.

Entry informationi

Entry nameiMANB1_BACSU
AccessioniPrimary (citable) accession number: O05512
Secondary accession number(s): Q797D6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: July 7, 2009
Last modified: May 27, 2015
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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

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 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.