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Protein

Mannan endo-1,4-beta-mannosidase F

Gene

manF

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 4 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
  1. Vmax=1935 µmol/min/mg enzyme2 Publications

pH dependencei

Optimum pH is 4.0 to 5.0.2 Publications

Temperature dependencei

Optimum temperature is 65 degrees Celsius. Stable up to 55 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei264Proton donorBy similarity1
Active sitei373NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BRENDAi3.2.1.78. 508.

Protein family/group databases

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

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
Proteomesi
  • UP000002530 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiFungiDB:Afu8g07030.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 171 PublicationAdd BLAST17
ChainiPRO_000039371518 – 438Mannan endo-1,4-beta-mannosidase FAdd BLAST421

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi277N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ4WBS1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 54CBM1PROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni60 – 96Ser-rich linkerAdd BLAST37
Regioni97 – 438CatalyticAdd BLAST342

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

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

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000169951.
InParanoidiQ4WBS1.
KOiK19355.
OrthoDBiEOG092C2KMO.

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]
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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

« Hide

        10         20         30         40         50
MHPLPSVALL SAIGAVAAQV GPWGQCGGRS YTGETSCVSG WSCVLFNEWY
60 70 80 90 100
SQCQPATTTS TSSVSATAAP SSTSSSKESV PSATTSKKPV PTGSSSFVKA
110 120 130 140 150
DGLKFNIDGE TKYFAGTNAY WLPFLTNDAD VDSVMDNLQK AGLKILRTWG
160 170 180 190 200
FNDVNSKPSS GTVYFQLHDP STGTTTINTG ADGLQRLDYV VSAAEKRGIK
210 220 230 240 250
LLIPLVNNWD DYGGMNAYVK AYGGSKTEWY TNSKIQSVYQ AYIKAVVSRY
260 270 280 290 300
RDSPAIMAWE LSNEARCQGC STDVIYNWTA KTSAYIKSLD PNHMVATGDE
310 320 330 340 350
GMGVTVDSDG SYPYSTYEGS DFAKNLAAPD IDFGVFHLYT EDWGIKDNSW
360 370 380 390 400
GNGWVTSHAK VCKAAGKPCL FEEYGLKDDH CSASLTWQKT SVSSGMAADL
410 420 430
FWQYGQTLST GPSPNDHFTI YYGTSDWQCG VADHLSTL
Length:438
Mass (Da):47,327
Last modified:April 20, 2010 - v2
Checksum:i8E55123506BD7E24
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14 – 17GAVA → IYGS in ACH58410 (PubMed:15541293).Curated4
Sequence conflicti83A → S in ACH58411 (PubMed:19205049).Curated1
Sequence conflicti234 – 236KIQ → QIP in ACH58411 (PubMed:19205049).Curated3
Sequence conflicti254P → L in ACH58411 (PubMed:19205049).Curated1
Sequence conflicti279T → A in ACH58411 (PubMed:19205049).Curated1
Sequence conflicti385L → P in ACH58411 (PubMed:19205049).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ4WBS1.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:Afu8g07030.

Phylogenomic databases

HOGENOMiHOG000169951.
InParanoidiQ4WBS1.
KOiK19355.
OrthoDBiEOG092C2KMO.

Enzyme and pathway databases

BRENDAi3.2.1.78. 508.

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]
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 66 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.