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Q4WBS1 (MANF_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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:
Mannan endo-1,4-beta-mannosidase F

EC=3.2.1.78
Alternative name(s):
Endo-beta-1,4-mannanase F
Gene names
Name:manF
ORF Names:AFUA_8G07030
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length438 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.2 Ref.3

Catalytic activity

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

Subcellular location

Secreted By similarity.

Domain

Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in serines, and a C-terminal endo-1,4-mannanase catalytic module. The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.

Sequence similarities

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

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.

Biophysicochemical properties

Kinetic parameters:

KM=3.07 mM for locust bean galactomannan Ref.2 Ref.3

Vmax=1935 µmol/min/mg enzyme

pH dependence:

Optimum pH is 4.0 to 5.0.

Temperature dependence:

Optimum temperature is 65 degrees Celsius. Stable up to 55 degrees Celsius.

Sequence caution

The sequence EAL85463.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.2
Chain18 – 438421Mannan endo-1,4-beta-mannosidase F
PRO_0000393715

Regions

Domain19 – 5436CBM1
Region60 – 9637Ser-rich linker
Region97 – 438342Catalytic

Sites

Active site2641Proton donor By similarity
Active site3731Nucleophile By similarity

Amino acid modifications

Glycosylation2771N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict14 – 174GAVA → IYGS in ACH58410. Ref.2
Sequence conflict831A → S in ACH58411. Ref.3
Sequence conflict234 – 2363KIQ → QIP in ACH58411. Ref.3
Sequence conflict2541P → L in ACH58411. Ref.3
Sequence conflict2791T → A in ACH58411. Ref.3
Sequence conflict3851L → P in ACH58411. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q4WBS1 [UniParc].

Last modified April 20, 2010. Version 2.
Checksum: 8E55123506BD7E24

FASTA43847,327
        10         20         30         40         50         60 
MHPLPSVALL SAIGAVAAQV GPWGQCGGRS YTGETSCVSG WSCVLFNEWY SQCQPATTTS 

        70         80         90        100        110        120 
TSSVSATAAP SSTSSSKESV PSATTSKKPV PTGSSSFVKA DGLKFNIDGE TKYFAGTNAY 

       130        140        150        160        170        180 
WLPFLTNDAD VDSVMDNLQK AGLKILRTWG FNDVNSKPSS GTVYFQLHDP STGTTTINTG 

       190        200        210        220        230        240 
ADGLQRLDYV VSAAEKRGIK LLIPLVNNWD DYGGMNAYVK AYGGSKTEWY TNSKIQSVYQ 

       250        260        270        280        290        300 
AYIKAVVSRY RDSPAIMAWE LSNEARCQGC STDVIYNWTA KTSAYIKSLD PNHMVATGDE 

       310        320        330        340        350        360 
GMGVTVDSDG SYPYSTYEGS DFAKNLAAPD IDFGVFHLYT EDWGIKDNSW GNGWVTSHAK 

       370        380        390        400        410        420 
VCKAAGKPCL FEEYGLKDDH CSASLTWQKT SVSSGMAADL FWQYGQTLST GPSPNDHFTI 

       430 
YYGTSDWQCG VADHLSTL 

« Hide

References

« Hide 'large scale' references
[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
[2]"Purification and characterization of two forms of endo-beta-1,4-mannanase from a thermotolerant fungus, Aspergillus fumigatus IMI 385708 (formerly Thermomyces lanuginosus IMI 158749)."
Puchart V., Vrsanska M., Svoboda P., Pohl J., Ogel Z.B., Biely P.
Biochim. Biophys. Acta 1674:239-250(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-438, PROTEIN SEQUENCE OF 18-29; 113-133 AND 325-347, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: IMI 385708.
[3]"Cloning, expression and characterization of endo-beta-1,4-mannanase from Aspergillus fumigatus in Aspergillus sojae and Pichia pastoris."
Duruksu G., Ozturk B., Biely P., Bakir U., Ogel Z.B.
Biotechnol. Prog. 25:271-276(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-438, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: IMI 385708.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000013 Genomic DNA. Translation: EAL85463.1. Different initiation.
EU925594 Genomic DNA. Translation: ACH58410.1.
EU925595 mRNA. Translation: ACH58411.1.
RefSeqXP_747501.1. XM_742408.1.

3D structure databases

ProteinModelPortalQ4WBS1.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM1. Carbohydrate-Binding Module Family 1.
GH5. Glycoside Hydrolase Family 5.
mycoCLAPMAN5A_ASPFU.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00003026; CADAFUAP00003026; CADAFUAG00003026.
GeneID3504904.
KEGGafm:AFUA_8G07030.

Phylogenomic databases

eggNOGCOG3934.
HOGENOMHOG000169951.
KOK01567.
OrthoDBEOG7M3J90.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR000254. Cellulose-bd_dom_fun.
IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00734. CBM_1. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMANF_ASPFU
AccessionPrimary (citable) accession number: Q4WBS1
Secondary accession number(s): B5LZ77, B5LZ78
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 20, 2010
Last modified: February 19, 2014
This is version 55 of the entry and version 2 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