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Q9ZF13

- Q9ZF13_THEFU

UniProt

Q9ZF13 - Q9ZF13_THEFU

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Protein
Submitted name:

Beta-mannanase

Gene

man

Organism
Thermobifida fusca (Thermomonospora fusca)
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli

Functioni

Sites

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

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

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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 bindingImported

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:
EMBL
GenBank
DDBJ
Links Updated
AJ006227 Genomic DNA. Translation: CAA06924.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ006227 Genomic DNA. Translation: CAA06924.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BQC X-ray 1.50 A 1-279 [» ]
2MAN X-ray 1.90 A 1-279 [» ]
3MAN X-ray 1.60 A 1-279 [» ]
ProteinModelPortali Q9ZF13.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q9ZF13.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00150. Cellulase. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

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(1996)
    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(1998) [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: October 29, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3