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Q5AVP1 (MAND_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 D
EC=3.2.1.78
Alternative name(s):
Endo-beta-1,4-mannanase D
Gene names
Name:manD
ORF Names:AN7639
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella ›

Protein attributes

Sequence length381 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
Reference 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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 381359Mannan endo-1,4-beta-mannosidase D
PRO_0000393711

Sites

Active site1921Proton donor By similarity
Active site2991Nucleophile By similarity

Amino acid modifications

Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation2731N-linked (GlcNAc...) Potential
Glycosylation3341N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5AVP1 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 2D1871678CF69515

FASTA38141,603
        10         20         30         40         50         60 
MKHLLSLVCT LGAATLAASA AAEAGSMPSA NGLDFVIDGE ASYFAGSNAY WLSFLTNNAD 

        70         80         90        100        110        120 
VDLALDHFAE SGLKILRIWG FSDVTAEPSD NKVYFQLHQN GSSTVNTGPN GLERLDYIIS 

       130        140        150        160        170        180 
GAEKRGIKLV IPLVNYWDDF GGMNAYISAY GGDKPGWYTN DKIQAAYHAY VKAVVSRYVD 

       190        200        210        220        230        240 
SPAIFAWELA NEPRCSGCDT SIINQWATKT SSFIKSLDPN HMVAMGDEGM GLPGDSNYPY 

       250        260        270        280        290        300 
SYYEGNDFAL NLAIPDIDFG TLHLYTTDWG VSNNSWGNKW VQDHAAVCKS AGKPCLFEEY 

       310        320        330        340        350        360 
GMKGNHCTYE LAWQKTALAT PGMAADLFWQ FGENLSSGQT HNDKYTVYYG SNEWKCVVSD 

       370        380 
HVAAVAVRRY RLPVGGGQHG P

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AACD01000130 Genomic DNA. Translation: EAA61825.1.
BN001304 Genomic DNA. Translation: CBF79796.1.
RefSeqXP_680908.1. XM_675816.1.

3D structure databases

ProteinModelPortalQ5AVP1.
SMRQ5AVP1. Positions 26-365.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00000757; CADANIAP00000757; CADANIAG00000757.
GeneID2869716.
KEGGani:AN7639.2.

Phylogenomic databases

eggNOGCOG3934.
HOGENOMHOG000169951.
OMAFQNATIH.
OrthoDBEOG4G7G75.

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 nameMAND_EMENI
AccessionPrimary (citable) accession number: Q5AVP1
Secondary accession number(s): C8VBY8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 26, 2005
Last modified: May 1, 2013
This is version 54 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