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Protein

Mannan endo-1,4-beta-mannosidase B

Gene

MANB

Organism
Piromyces sp.
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. cellulase activity Source: InterPro
  3. mannan endo-1,4-beta-mannosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. substituted mannan metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiCBM35. Carbohydrate-Binding Module Family 35.
GH26. Glycoside Hydrolase Family 26.
mycoCLAPiMAN26B_PIRSP.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan endo-1,4-beta-mannosidase B (EC:3.2.1.78)
Alternative name(s):
1,4-beta-D-mannan mannanohydrolase B
Beta-mannanase B
Gene namesi
Name:MANB
OrganismiPiromyces sp.
Taxonomic identifieri45796 [NCBI]
Taxonomic lineageiEukaryotaFungiNeocallimastigomycotaNeocallimastigomycetesNeocallimastigalesNeocallimastigaceaePiromyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 571552Mannan endo-1,4-beta-mannosidase BPRO_0000012175Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP55297.
SMRiP55297. Positions 534-571.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 141120CBM6PROSITE-ProRule annotationAdd
BLAST
Domaini491 – 52636CBM10 1Add
BLAST
Domaini535 – 57036CBM10 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi475 – 4795Poly-Asn
Compositional biasi482 – 4887Poly-Asn

Sequence similaritiesi

Belongs to the glycosyl hydrolase 26 family.Curated
Contains 1 CBM6 (carbohydrate binding type-6) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
3.90.1220.10. 2 hits.
InterProiIPR002883. CBM10/Dockerin_dom.
IPR005084. CMB_fam6.
IPR009034. Dockerin_dom_fun.
IPR022790. EndoGluc_H/Glyco_hydro_26.
IPR008979. Galactose-bd-like.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02013. CBM_10. 2 hits.
PF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PRINTSiPR00739. GLHYDRLASE26.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF64571. SSF64571. 2 hits.
PROSITEiPS51175. CBM6. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P55297-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNSLSLLLFC IFFVFSTFAK KVYYEAENGK LDGVTVYKSD LTGFSGTGYV
60 70 80 90 100
GRFENPGNSV TVTVEVPQTG MYDLTIVYCA NMGQKINSLT VNGQSAGDIT
110 120 130 140 150
FTENTKFEDL NVGAIYLNKG KNTIGLVSSW GWMWVDAFVI NDAPNAAKDV
160 170 180 190 200
TSKLNPTLIN PKAIPAAKKL YDFLKTNYGK RILSGQVGAA GQAGDEGQEI
210 220 230 240 250
QRIQKATGKL PAVWNMDFIF ESNDCTWRPQ NPDITEMAIN WWKKYQGKGI
260 270 280 290 300
MSAQWHWNIA GKTGDFAFYK KDTTFSIDNA VTEGTWEYEK IIKDIDRVAG
310 320 330 340 350
HIKKLQAVNM PLIWRPLHEN DGDWFWWGNN PKSCAKLWKI LYERMVNYHG
360 370 380 390 400
LNNLIWLWNG KNDANTPVDY IDIIGVDIYA NDHGPQTTAY NTHFDFYGGK
410 420 430 440 450
KMVVLSENGR IPDIQQCVDQ NAWWGYFQTW NSEFILQDSY HTDAQLKEYF
460 470 480 490 500
THKTVMNMDE LPSFNVNSYE YQSGNNNNNS SNNNNNNNSS ECFSIPLGYP
510 520 530 540 550
CCKGNTVVYT DNDGDWGVEN NEWCGIGNSS SAVVCWSEAL GYPCCVSSSD
560 570
VYYTDNDGEW GVENGDWCGI I
Length:571
Mass (Da):64,397
Last modified:October 1, 1996 - v1
Checksum:iB13E44581FAA9DAA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97408 mRNA. Translation: CAA66061.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97408 mRNA. Translation: CAA66061.1.

3D structure databases

ProteinModelPortaliP55297.
SMRiP55297. Positions 534-571.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM35. Carbohydrate-Binding Module Family 35.
GH26. Glycoside Hydrolase Family 26.
mycoCLAPiMAN26B_PIRSP.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
3.90.1220.10. 2 hits.
InterProiIPR002883. CBM10/Dockerin_dom.
IPR005084. CMB_fam6.
IPR009034. Dockerin_dom_fun.
IPR022790. EndoGluc_H/Glyco_hydro_26.
IPR008979. Galactose-bd-like.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02013. CBM_10. 2 hits.
PF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PRINTSiPR00739. GLHYDRLASE26.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF64571. SSF64571. 2 hits.
PROSITEiPS51175. CBM6. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Evidence that the Piromyces gene family encoding endo-1,4-mannanases arose through gene duplication."
    Millward-Sadler S.J., Hall J., Black G.W., Hazlewood G.P., Gilbert H.J.
    FEMS Microbiol. Lett. 141:183-188(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiMANB_PIRSP
AccessioniPrimary (citable) accession number: P55297
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 1, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

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