Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mannan endo-1,4-beta-mannosidase A

Gene

manA

Organism
Aspergillus aculeatus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans.1 Publication

Catalytic activityi

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

pH dependencei

Optimum pH is 5.0.1 Publication

Temperature dependencei

Optimum temperature is between 60 and 70 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei198Proton donorBy similarity1
Active sitei306NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BRENDAi3.2.1.78. 488.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.
mycoCLAPiMAN5A_ASPAC.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan endo-1,4-beta-mannosidase A (EC:3.2.1.78)
Alternative name(s):
Endo-beta-1,4-mannanase A
Gene namesi
Name:manA
Synonyms:man1
OrganismiAspergillus aculeatus
Taxonomic identifieri5053 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_500014257619 – 377Mannan endo-1,4-beta-mannosidase AAdd BLAST359

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi105N-linked (GlcNAc...)Sequence analysis1
Glycosylationi255N-linked (GlcNAc...)Sequence analysis1
Glycosylationi326N-linked (GlcNAc...)Sequence analysis1
Glycosylationi357N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ00012.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q00012-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLSHMLLSL ASLGVATALP RTPNHNAATT AFPSTSGLHF TIDGKTGYFA
60 70 80 90 100
GTNSYWIGFL TNNDDVDLVM SQLAASDLKI LRVWGFNDVN TKPTDGTVWY
110 120 130 140 150
QLHANGTSTI NTGADGLQRL DYVVTSAEKY GVKLIINFVN EWTDYGGMQA
160 170 180 190 200
YVTAYGAAAQ TDFYTNTAIQ AAYKNYIKAV VSRYSSSAAI FAWELANEPR
210 220 230 240 250
CQGCDTSVLY NWISDTSKYI KSLDSKHLVT IGDEGFGLDV DSDGSYPYTY
260 270 280 290 300
GEGLNFTKNL GISTIDFGTL HLYPDSWGTS YDWGNGWITA HAAACKAVGK
310 320 330 340 350
PCLLEEYGVT SNHCAVESPW QQTAGNATGI SGDLYWQYGT TFSWGQSPND
360 370
GNTFYYNTSD FTCLVTDHVA AINAQSK
Length:377
Mass (Da):41,082
Last modified:November 1, 1996 - v1
Checksum:i10E6477555BE3CA2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35487 mRNA. Translation: AAA67426.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35487 mRNA. Translation: AAA67426.1.

3D structure databases

ProteinModelPortaliQ00012.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.
mycoCLAPiMAN5A_ASPAC.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.78. 488.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMANA_ASPAC
AccessioniPrimary (citable) accession number: Q00012
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: November 1, 1996
Last modified: October 5, 2016
This is version 69 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.