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Q2TXJ2 (MANA_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 50. 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

Names and origin

Protein namesRecommended name:
Probable 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
ORF Names:AO090010000122
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

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.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 386365Probable mannan endo-1,4-beta-mannosidase A
PRO_0000393705

Sites

Active site2081Proton donor By similarity
Active site3161Nucleophile By similarity

Amino acid modifications

Glycosylation3361N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q2TXJ2 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 53FFF34EB88378FA

FASTA38641,906
        10         20         30         40         50         60 
MKLNPSLLTA AGLVSAQLAS ALPQASSSTV SPSPSPSATP GSFVTTSGLN FVIDGKTGYF 

        70         80         90        100        110        120 
AGSNSYWIGF QKNNDDVDLV FSHLQESGLK ILRVWGFNDV NQKPTDGSVY YHLLADGTAT 

       130        140        150        160        170        180 
VNEGEDGLQR LDYVVSSAEK HGIKLIINFV NFWDDYGGIN AYVKAFGGSK EGFYTNDAMQ 

       190        200        210        220        230        240 
AAYRAYIKAV ISRYSDSTAI FAWELANEPR CQGCETTVLY NWIESTSQYI KSLDSKHLVC 

       250        260        270        280        290        300 
IGDEGFGLDT GSDGSYPYQY SEGSDFAKNL AIPTIDFGTF HLYPSSWGTT NDWGNGWVTS 

       310        320        330        340        350        360 
HGAACKAAGK PCLFEEYGVT SDHCAVEKPW QNTALNTTAI SGDLYWQYGD QLSGGPSPDD 

       370        380 
GNTFYYGTDD FKCLVTDHIA AINSRK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007175 Genomic DNA. Translation: BAE66031.1.

3D structure databases

ProteinModelPortalQ2TXJ2.
SMRQ2TXJ2. Positions 41-383.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00004159.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00004232; CADAORAP00004159; CADAORAG00004232.

Phylogenomic databases

eggNOGCOG3934.
HOGENOMHOG000169951.
OrthoDBEOG7M3J90.

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. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMANA_ASPOR
AccessionPrimary (citable) accession number: Q2TXJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: January 24, 2006
Last modified: March 19, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries