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Protein

Probable mannan endo-1,4-beta-mannosidase A

Gene

manA

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
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.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei206 – 2061Proton donorBy similarity
Active sitei314 – 3141NucleophileBy similarity

GO - Molecular functioni

  1. mannan endo-1,4-beta-mannosidase activity Source: ASPGD

GO - Biological processi

  1. mannan catabolic process Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 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
ORF Names:An05g01320
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 7L

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: ASPGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 383362Probable mannan endo-1,4-beta-mannosidase APRO_5000220000Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi17 – 171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi194 – 1941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi263 – 2631N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1
383
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 443Combined sources
Beta strandi47 – 504Combined sources
Beta strandi53 – 553Combined sources
Beta strandi57 – 615Combined sources
Helixi65 – 673Combined sources
Helixi71 – 8414Combined sources
Beta strandi88 – 925Combined sources
Beta strandi96 – 994Combined sources
Beta strandi108 – 1125Combined sources
Beta strandi115 – 1184Combined sources
Turni122 – 1243Combined sources
Helixi125 – 13713Combined sources
Beta strandi141 – 1466Combined sources
Beta strandi148 – 1514Combined sources
Helixi155 – 1639Combined sources
Helixi169 – 1735Combined sources
Helixi175 – 19117Combined sources
Turni192 – 1943Combined sources
Beta strandi198 – 2036Combined sources
Helixi215 – 23117Combined sources
Beta strandi235 – 2384Combined sources
Helixi254 – 2563Combined sources
Helixi264 – 2685Combined sources
Beta strandi275 – 2806Combined sources
Helixi282 – 2854Combined sources
Helixi291 – 30616Combined sources
Beta strandi310 – 3156Combined sources
Helixi321 – 33414Combined sources
Beta strandi338 – 3447Combined sources
Helixi367 – 3726Combined sources
Helixi374 – 3818Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WH9X-ray1.57A/B39-383[»]
ProteinModelPortaliA2QKT4.
SMRiA2QKT4. Positions 38-380.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000169951.
OrthoDBiEOG7M3J90.

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.

A2QKT4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLSNALLTL ASLALANVST ALPKASPAPS TSSSAASTSF ASTSGLQFTI
60 70 80 90 100
DGETGYFAGT NSYWIGFLTD NADVDLVMGH LKSSGLKILR VWGFNDVTSQ
110 120 130 140 150
PSSGTVWYQL HQDGKSTINT GADGLQRLDY VVSSAEQHDI KLIINFVNYW
160 170 180 190 200
TDYGGMSAYV SAYGGSGETD FYTSDTMQSA YQTYIKTVVE RYSNSSAVFA
210 220 230 240 250
WELANEPRCP SCDTSVLYNW IEKTSKFIKG LDADRMVCIG DEGFGLNIDS
260 270 280 290 300
DGSYPYQFSE GLNFTMNLGI DTIDFGTLHL YPDSWGTSDD WGNGWITAHG
310 320 330 340 350
AACKAAGKPC LLEEYGVTSN HCSVEGSWQK TALSTTGVGA DLFWQYGDDL
360 370 380
STGKSPDDGN TIYYGTSDYQ CLVTDHVAAI GSA
Length:383
Mass (Da):41,247
Last modified:March 6, 2007 - v1
Checksum:i926472E9197CF491
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270105 Genomic DNA. Translation: CAK96471.1.
RefSeqiXP_001390707.1. XM_001390670.1.

Genome annotation databases

EnsemblFungiiCADANGAT00004881; CADANGAP00004785; CADANGAG00004881.
GeneIDi4980871.
KEGGiang:ANI_1_160044.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270105 Genomic DNA. Translation: CAK96471.1.
RefSeqiXP_001390707.1. XM_001390670.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WH9X-ray1.57A/B39-383[»]
ProteinModelPortaliA2QKT4.
SMRiA2QKT4. Positions 38-380.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANGAT00004881; CADANGAP00004785; CADANGAG00004881.
GeneIDi4980871.
KEGGiang:ANI_1_160044.

Phylogenomic databases

HOGENOMiHOG000169951.
OrthoDBiEOG7M3J90.

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...

Publicationsi

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiMANA_ASPNC
AccessioniPrimary (citable) accession number: A2QKT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: March 6, 2007
Last modified: March 4, 2015
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.