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Q4WBS1

- MANF_ASPFU

UniProt

Q4WBS1 - MANF_ASPFU

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Protein
Mannan endo-1,4-beta-mannosidase F
Gene
manF, AFUA_8G07030
Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans.2 Publications

Catalytic activityi

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

Kineticsi

  1. KM=3.07 mM for locust bean galactomannan2 Publications

Vmax=1935 µmol/min/mg enzyme

pH dependencei

Optimum pH is 4.0 to 5.0.

Temperature dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei264 – 2641Proton donor By similarity
Active sitei373 – 3731Nucleophile By similarity

GO - Molecular functioni

  1. cellulase activity Source: ASPGD
  2. cellulose binding Source: ASPGD
  3. chitin binding Source: ASPGD
  4. mannan endo-1,4-beta-mannosidase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. carbohydrate metabolic process Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH5. Glycoside Hydrolase Family 5.
mycoCLAPiMAN5A_ASPFU.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan endo-1,4-beta-mannosidase F (EC:3.2.1.78)
Alternative name(s):
Endo-beta-1,4-mannanase F
Gene namesi
Name:manF
ORF Names:AFUA_8G07030
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 8

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 Publication
Add
BLAST
Chaini18 – 438421Mannan endo-1,4-beta-mannosidase F
PRO_0000393715Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi277 – 2771N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ4WBS1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 5436CBM1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni60 – 9637Ser-rich linker
Add
BLAST
Regioni97 – 438342Catalytic
Add
BLAST

Domaini

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 similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3934.
HOGENOMiHOG000169951.
KOiK01567.
OrthoDBiEOG7M3J90.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q4WBS1-1 [UniParc]FASTAAdd to Basket

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MHPLPSVALL SAIGAVAAQV GPWGQCGGRS YTGETSCVSG WSCVLFNEWY    50
SQCQPATTTS TSSVSATAAP SSTSSSKESV PSATTSKKPV PTGSSSFVKA 100
DGLKFNIDGE TKYFAGTNAY WLPFLTNDAD VDSVMDNLQK AGLKILRTWG 150
FNDVNSKPSS GTVYFQLHDP STGTTTINTG ADGLQRLDYV VSAAEKRGIK 200
LLIPLVNNWD DYGGMNAYVK AYGGSKTEWY TNSKIQSVYQ AYIKAVVSRY 250
RDSPAIMAWE LSNEARCQGC STDVIYNWTA KTSAYIKSLD PNHMVATGDE 300
GMGVTVDSDG SYPYSTYEGS DFAKNLAAPD IDFGVFHLYT EDWGIKDNSW 350
GNGWVTSHAK VCKAAGKPCL FEEYGLKDDH CSASLTWQKT SVSSGMAADL 400
FWQYGQTLST GPSPNDHFTI YYGTSDWQCG VADHLSTL 438
Length:438
Mass (Da):47,327
Last modified:April 20, 2010 - v2
Checksum:i8E55123506BD7E24
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 174GAVA → IYGS in ACH58410. 1 Publication
Sequence conflicti83 – 831A → S in ACH58411. 1 Publication
Sequence conflicti234 – 2363KIQ → QIP in ACH58411. 1 Publication
Sequence conflicti254 – 2541P → L in ACH58411. 1 Publication
Sequence conflicti279 – 2791T → A in ACH58411. 1 Publication
Sequence conflicti385 – 3851L → P in ACH58411. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000013 Genomic DNA. Translation: EAL85463.1. Different initiation.
EU925594 Genomic DNA. Translation: ACH58410.1.
EU925595 mRNA. Translation: ACH58411.1.
RefSeqiXP_747501.1. XM_742408.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00003026; CADAFUAP00003026; CADAFUAG00003026.
GeneIDi3504904.
KEGGiafm:AFUA_8G07030.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000013 Genomic DNA. Translation: EAL85463.1 . Different initiation.
EU925594 Genomic DNA. Translation: ACH58410.1 .
EU925595 mRNA. Translation: ACH58411.1 .
RefSeqi XP_747501.1. XM_742408.1.

3D structure databases

ProteinModelPortali Q4WBS1.
ModBasei Search...

Protein family/group databases

CAZyi CBM1. Carbohydrate-Binding Module Family 1.
GH5. Glycoside Hydrolase Family 5.
mycoCLAPi MAN5A_ASPFU.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFUAT00003026 ; CADAFUAP00003026 ; CADAFUAG00003026 .
GeneIDi 3504904.
KEGGi afm:AFUA_8G07030.

Phylogenomic databases

eggNOGi COG3934.
HOGENOMi HOG000169951.
KOi K01567.
OrthoDBi EOG7M3J90.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR000254. Cellulose-bd_dom_fun.
IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00734. CBM_1. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view ]
SMARTi SM00236. fCBD. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEi PS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiMANF_ASPFU
AccessioniPrimary (citable) accession number: Q4WBS1
Secondary accession number(s): B5LZ77, B5LZ78
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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