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Protein

Mannan endo-1,4-beta-mannosidase A and B

Gene
N/A
Organism
Bacillus mannanilyticus (strain DSM 16130 / JCM 10596 / AM-001)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Could be involved in the degradation of glucomannan and catalyzes the endo hydrolysis of beta-1,4-linked mannan, galactomannan and glucomannan.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei132SubstrateBy similarity1
Sitei194Plays an important role in maintaining the position of the catalytic nucleophileBy similarity1
Active sitei195Proton donorBy similarity1
Binding sitei200SubstrateBy similarity1
Binding sitei270SubstrateBy similarity1
Active sitei295NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Protein family/group databases

CAZyiCBM59. Carbohydrate-Binding Module Family 59.
GH26. Glycoside Hydrolase Family 26.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan endo-1,4-beta-mannosidase A and B1 Publication (EC:3.2.1.78By similarity)
Alternative name(s):
1,4-beta-D-mannan mannanohydrolase1 Publication
Beta-mannanase1 Publication
Endo-1,4-mannanase1 Publication
Cleaved into the following 2 chains:
OrganismiBacillus mannanilyticus (strain DSM 16130 / JCM 10596 / AM-001)
Taxonomic identifieri1236954 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 261 PublicationAdd BLAST26
ChainiPRO_000001216927 – 513Mannan endo-1,4-beta-mannosidase AAdd BLAST487
ChainiPRO_000001217027 – 365Mannan endo-1,4-beta-mannosidase BAdd BLAST339

Structurei

3D structure databases

ProteinModelPortaliP16699.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini41 – 353GH26PROSITE-ProRule annotationAdd BLAST313

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni429 – 430Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 26 family.PROSITE-ProRule annotationCurated
Contains 1 GH26 (glycosyl hydrolase family 26) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR022790. GH26_dom.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR40079. PTHR40079. 1 hit.
PfamiPF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PRINTSiPR00739. GLHYDRLASE26.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51764. GH26. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P16699-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVYKKVAFV MAFIMFFSVL PTISMSSEAN GAALSNPNAN QTTKNVYSWL
60 70 80 90 100
ANLPNKSNKR VVSGHFGGYS DSTLAWIKQC ARELTGKMPG ILSCDYKNWQ
110 120 130 140 150
TRLYVADQIS YGCNQELINF WNQGGLVTIS VHMPNPGFHS GENYKTILPT
160 170 180 190 200
SQFQNLTNHR TTEGRRWKDM LDKMADGLDE LQNNGVTVLF RPLHEMNGEW
210 220 230 240 250
FWWGAEGYNQ FDQTRANAYI SAWRDMYQYF THERKLNNLI WVYSPDVYRD
260 270 280 290 300
HVTSYYPGAN YVDIVALDSY HPDPHSLTDQ YNRMIALDKP FAFAEIGPPE
310 320 330 340 350
SMAGSFDYSN YIQAIKQKYP RTVYFLAWND KWSPHNNRGA WDLFNDSWVV
360 370 380 390 400
NRGEIDYGQS NPATVLYDFE NNTLSWSGCE FTDGGPWTSN EWSANGTQSL
410 420 430 440 450
KADVVLGNNS YHLQKTVNRN LSSFKNLEIK VSHSSWGNVG SGMTARVFVK
460 470 480 490 500
TGSAWRWNAG EFCQFAGKRT TALSIDLTKV SNLHDVREIG VEYKAPANSN
510
GKTAIYLDHV TVR
Length:513
Mass (Da):58,430
Last modified:August 1, 1990 - v1
Checksum:i88D105F622CDB5A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31797 Genomic DNA. Translation: AAA22586.1.
PIRiA37219.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31797 Genomic DNA. Translation: AAA22586.1.
PIRiA37219.

3D structure databases

ProteinModelPortaliP16699.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM59. Carbohydrate-Binding Module Family 59.
GH26. Glycoside Hydrolase Family 26.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR022790. GH26_dom.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR40079. PTHR40079. 1 hit.
PfamiPF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PRINTSiPR00739. GLHYDRLASE26.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51764. GH26. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMANB_BACMA
AccessioniPrimary (citable) accession number: P16699
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: October 5, 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

Miscellaneous

The production of the two beta-mannanases seems not to be caused by proteolytic cleavage.1 Publication

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.