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Protein
Submitted name:

Beta-mannanase

Gene

man

Organism
Thermobifida fusca (Thermomonospora fusca)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei28 – 281Beta-D-mannoseCombined sources
Binding sitei57 – 571Beta-D-mannoseCombined sources
Sitei125 – 1251Important for catalytic activity
Sitei126 – 1261Important for catalytic activity
Sitei194 – 1941Important for catalytic activity
Sitei196 – 1961Important for catalytic activity
Sitei223 – 2231Important for catalytic activity

GO - Molecular functioni

  1. mannan endo-1,4-beta-mannosidase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

GlycosidaseUniRule annotationImported, Hydrolase

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Submitted name:
Beta-mannanaseImported (EC:3.2.1.78Imported)
Gene namesi
Name:manImported
OrganismiThermobifida fusca (Thermomonospora fusca)Imported
Taxonomic identifieri2021 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptosporangineaeNocardiopsaceaeThermobifida

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi72 ↔ 79Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BQCX-ray1.50A1-279[»]
2MANX-ray1.90A1-279[»]
3MANX-ray1.60A1-279[»]
ProteinModelPortaliQ9ZF13.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZF13.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni257 – 2582Mannose bindingCombined sources

Sequence similaritiesi

Belongs to the glycosyl hydrolase 5 family.UniRule annotation

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Fragment.

Q9ZF13-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GLHVKNGRLY EANGQEFIIR GVSHPHNWYP QHTQAFADIK SHGANTVRVV
60 70 80 90 100
LSNGVRWSKN GPSDVANVIS LCKQNRLICM LEVHDTTGYG EQSGASTLDQ
110 120 130 140 150
AVDYWIELKS VLQGEEDYVL INIGNEPYGN DSATVAAGAW DTSAAIQRLR
160 170 180 190 200
AAGFEHTLVV DAPNWGQDWT NTMRNNADQV YASDPTGNTV FSIHMYGVYS
210 220 230 240 250
QASTITSYLE HFVNAGLPLI IGEFGHDHSD GNPDEDTIMA EAERLKLGYI
260 270
GWSWSGNGGG VEYLDMVYNF DGDNLSPWG
Length:279
Mass (Da):30,657
Last modified:May 1, 1999 - v1
Checksum:i98A2850FAE013DB0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported
Non-terminal residuei279 – 2791Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006227 Genomic DNA. Translation: CAA06924.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006227 Genomic DNA. Translation: CAA06924.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BQCX-ray1.50A1-279[»]
2MANX-ray1.90A1-279[»]
3MANX-ray1.60A1-279[»]
ProteinModelPortaliQ9ZF13.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZF13.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Crystallization and preliminary crystallographic analysis of two beta-mannanase isoforms from Thermomonospora fusca KW3."
    Hilge M., Gloor S., Winterhalter K., Piontek K.
    Acta Crystallogr. 52:1224-1225(1995)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: KW3Imported.
  2. "High-resolution native and complex structures of thermostable beta-mannanase from Thermomonospora fusca - substrate specificity in glycosyl hydrolase family 5."
    Hilge M., Gloor S.M., Rypniewski W., Sauer O., Heightman T.D., Zimmermann W., Winterhalter K., Piontek K.
    Structure 6:1433-1444(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: KW3Imported.

Entry informationi

Entry nameiQ9ZF13_THEFU
AccessioniPrimary (citable) accession number: Q9ZF13
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: January 7, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.