Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q00012 (MANA_ASPAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mannan endo-1,4-beta-mannosidase A
EC=3.2.1.78
Alternative name(s):
Endo-beta-1,4-mannanase A
Gene names
Name:manA
Synonyms:man1
OrganismAspergillus aculeatus
Taxonomic identifier5053 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.0. Ref.1

Temperature dependence:

Optimum temperature is between 60 and 70 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmannan endo-1,4-beta-mannosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 377359Mannan endo-1,4-beta-mannosidase A
PRO_5000142576

Sites

Active site1981Proton donor By similarity
Active site3061Nucleophile By similarity

Amino acid modifications

Glycosylation1051N-linked (GlcNAc...) Potential
Glycosylation2551N-linked (GlcNAc...) Potential
Glycosylation3261N-linked (GlcNAc...) Potential
Glycosylation3571N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q00012 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 10E6477555BE3CA2

FASTA37741,082
        10         20         30         40         50         60 
MKLSHMLLSL ASLGVATALP RTPNHNAATT AFPSTSGLHF TIDGKTGYFA GTNSYWIGFL 

        70         80         90        100        110        120 
TNNDDVDLVM SQLAASDLKI LRVWGFNDVN TKPTDGTVWY QLHANGTSTI NTGADGLQRL 

       130        140        150        160        170        180 
DYVVTSAEKY GVKLIINFVN EWTDYGGMQA YVTAYGAAAQ TDFYTNTAIQ AAYKNYIKAV 

       190        200        210        220        230        240 
VSRYSSSAAI FAWELANEPR CQGCDTSVLY NWISDTSKYI KSLDSKHLVT IGDEGFGLDV 

       250        260        270        280        290        300 
DSDGSYPYTY GEGLNFTKNL GISTIDFGTL HLYPDSWGTS YDWGNGWITA HAAACKAVGK 

       310        320        330        340        350        360 
PCLLEEYGVT SNHCAVESPW QQTAGNATGI SGDLYWQYGT TFSWGQSPND GNTFYYNTSD 

       370 
FTCLVTDHVA AINAQSK

« Hide

References

[1]"Expression cloning, purification and characterization of a beta-1,4-mannanase from Aspergillus aculeatus."
Christgau S., Kauppinen S., Vind J., Kofod L.V., Dalboge H.
Biochem. Mol. Biol. Int. 33:917-925(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: KSM 510.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L35487 mRNA. Translation: AAA67426.1.

3D structure databases

HSSPHSSP built from PDB template 1QNR based on UniProtKB Q99036.
ProteinModelPortalQ00012.
SMRQ00012. Positions 30-373.
ModBaseSearch...

Protein family/group databases

CAZyGH5. Glycoside Hydrolase Family 5.
mycoCLAPMAN5A_ASPAC.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00659. GLYCOSYL_HYDROL_F5. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMANA_ASPAC
AccessionPrimary (citable) accession number: Q00012
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents