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Protein

Mannan endo-1,4-beta-mannosidase A

Gene

MANA

Organism
Piromyces sp.
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans, one of the major hemicellulose components in hardwoods and softwoods. Shows very high activity against mannohexaose but not against mannopentaose and smaller mannooligosaccharides. The major products released from mannooligosaccharide hydrolysis are mannose and mannobiose. The reiterated 40 AA domain is involved in binding the cellulase-hemicellulase complex.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei318 – 3181Proton donorPROSITE-ProRule annotation
Active sitei406 – 4061NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiCBM35. Carbohydrate-Binding Module Family 35.
GH26. Glycoside Hydrolase Family 26.
mycoCLAPiMAN26A_PIRSP.

Names & Taxonomyi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 606587Mannan endo-1,4-beta-mannosidase APRO_0000012174Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP55296.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 140119CBM6PROSITE-ProRule annotationAdd
BLAST
Domaini164 – 458295GH26PROSITE-ProRule annotationAdd
BLAST
Domaini491 – 52737CBM10 1PROSITE-ProRule annotationAdd
BLAST
Domaini530 – 56637CBM10 2PROSITE-ProRule annotationAdd
BLAST
Domaini569 – 60537CBM10 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni472 – 48918LinkerAdd
BLAST

Domaini

Consists of a catalytic N-terminal domain linked to a reiterated non-catalytic C-terminal domain.

Sequence similaritiesi

Belongs to the glycosyl hydrolase 26 family.PROSITE-ProRule annotationCurated
Contains 3 CBM10 (carbohydrate binding type-10) domains.PROSITE-ProRule annotationCurated
Contains 1 CBM6 (carbohydrate binding type-6) domain.PROSITE-ProRule annotation
Contains 1 GH26 (glycosyl hydrolase family 26) 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. 3 hits.
InterProiIPR002883. CBM10/Dockerin_dom.
IPR005084. CMB_fam6.
IPR009034. Dockerin_dom_fun.
IPR008979. Galactose-bd-like.
IPR000805. Glyco_hydro_26.
IPR022790. Glyco_hydro_26_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02013. CBM_10. 3 hits.
PF16990. CBM_35. 1 hit.
PF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PRINTSiPR00739. GLHYDRLASE26.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF64571. SSF64571. 3 hits.
PROSITEiPS51763. CBM10. 3 hits.
PS51175. CBM6. 1 hit.
PS51764. GH26. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P55296-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSLNVILTL LSLIISVLSK KVYYEAEDGK LNGITVFKEL SGFSGKGYVG
60 70 80 90 100
RFENPGNSVT VTVDAPATGM YDLSIIYCAN MGQKINSLTV NDQSVGDITF
110 120 130 140 150
TENTKFETKD VGAVYLNKGK NTIGLVSSWG WMWVDAFVIN DAPNAAKDVS
160 170 180 190 200
SKLNPTLVNP KAIPAAKKLY DFLKTNYGKR ILSGQVGAAG QAGDEGQEIQ
210 220 230 240 250
RIQKATGKLP AVWNMDFIFE SNDCTWRPQN PDITEMAINW WKKYEGKGIM
260 270 280 290 300
AAQWHWNIAG KTGDFAFYSK DTTFNLENAV TEGTWEYEKI IKDIDRVSGH
310 320 330 340 350
IKKLQAVNMP LIWRPLHENN GDWFWWGNNP KACAKLWKIL YERMVNYHGL
360 370 380 390 400
NNLIWLWNGN NDANTPVDYI DIIGVDIYAN DHGPQTTAYN THFDFYGGKK
410 420 430 440 450
MVVLSENGRI PDIQQCVDQD VWWGYFQTWN SEFILQDSYH TDAQLKEYFN
460 470 480 490 500
HKTVMNMDEL PSFNVDSYNG DSGSSHNGNS ESNSNTGNSD ECWSINLGYP
510 520 530 540 550
CCIGDYVVTT DENGDWGVEN NEWCGIVHKS CWSEPLGYPC CVGNTVISAD
560 570 580 590 600
ESGDWGVENN EWCGIVHKSC WAEFLGYPCC VGNTVISTDE FGDWGVENDD

WCGILN
Length:606
Mass (Da):68,055
Last modified:October 1, 1996 - v1
Checksum:i79AAFEEFA2725D86
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91857 mRNA. Translation: CAA62968.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91857 mRNA. Translation: CAA62968.1.

3D structure databases

ProteinModelPortaliP55296.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM35. Carbohydrate-Binding Module Family 35.
GH26. Glycoside Hydrolase Family 26.
mycoCLAPiMAN26A_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. 3 hits.
InterProiIPR002883. CBM10/Dockerin_dom.
IPR005084. CMB_fam6.
IPR009034. Dockerin_dom_fun.
IPR008979. Galactose-bd-like.
IPR000805. Glyco_hydro_26.
IPR022790. Glyco_hydro_26_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02013. CBM_10. 3 hits.
PF16990. CBM_35. 1 hit.
PF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PRINTSiPR00739. GLHYDRLASE26.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF64571. SSF64571. 3 hits.
PROSITEiPS51763. CBM10. 3 hits.
PS51175. CBM6. 1 hit.
PS51764. GH26. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein docking domain."
    Fanutti C., Ponyi T., Black G.W., Hazlewood G.P., Gilbert H.J.
    J. Biol. Chem. 270:29314-29322(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiMANA_PIRSP
AccessioniPrimary (citable) accession number: P55296
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 11, 2015
This is version 80 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

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.