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P51529

- MANA_STRLI

UniProt

P51529 - MANA_STRLI

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Protein

Mannan endo-1,4-beta-mannosidase

Gene
manA
Organism
Streptomyces lividans
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

pH dependencei

Optimum pH is 6.8.

Temperature dependencei

Optimum temperature is 58 degrees Celsius.

GO - Molecular functioni

  1. cellulose binding Source: InterPro
  2. 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

Glycosidase, Hydrolase

Protein family/group databases

CAZyiCBM10. Carbohydrate-Binding Module Family 10.
GH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan endo-1,4-beta-mannosidase (EC:3.2.1.78)
Alternative name(s):
1,4-beta-D-mannan mannanohydrolase
Beta-mannanase
Gene namesi
Name:manA
OrganismiStreptomyces lividans
Taxonomic identifieri1916 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 35351 PublicationAdd
BLAST
Chaini36 – 383348Mannan endo-1,4-beta-mannosidasePRO_0000007900Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP51529.
SMRiP51529. Positions 37-336.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini345 – 37531CBM10Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi336 – 3405Poly-Gly

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR002883. CBM10/Dockerin_dom.
IPR009031. CBM_fam10.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02013. CBM_10. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM01064. CBM_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P51529-1 [UniParc]FASTAAdd to Basket

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MRNARSTLIT TAGMAFAVLG LLFALAGPSA GRAEAAAGGI HVSNGRVVEG    50
NGSAFVMRGV NHAYTWYPDR TGSIADIAAK GANTVRVVLS SGGRWTKTSA 100
SEVSALIGQC KANKVICVLE VHDTTGYGKD GATSLDQAGD YWVGVKSAAW 150
RAQEDYVVVN IGNEPFGNTN YAAWTDATKS AIGKLRGAGL GHALMVDAPN 200
WGQDWSGTMR SNAASVFASD PDRNTVFSIH MYGVYDTAAE VRDYLNAFVG 250
NGLPIVVGEF GDQHSDGNPD EDAIMATAQS LGVGYLGWSW SGNGGGVEYL 300
DMVNGFDPNS LTSWGNRILY GSNGIAATSR TATVYGGGGG STGGTAPNGY 350
PYCVNGGASD PDGDGWGWEN SRSCVVRGSA ADH 383
Length:383
Mass (Da):39,682
Last modified:May 30, 2000 - v2
Checksum:i5DB4B407C64E94C3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M92297 Genomic DNA. Translation: AAA26710.2.
PIRiS30386.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M92297 Genomic DNA. Translation: AAA26710.2 .
PIRi S30386.

3D structure databases

ProteinModelPortali P51529.
SMRi P51529. Positions 37-336.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM10. Carbohydrate-Binding Module Family 10.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR002883. CBM10/Dockerin_dom.
IPR009031. CBM_fam10.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF02013. CBM_10. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view ]
SMARTi SM01064. CBM_10. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Beta-mannanase of Streptomyces lividans 66: cloning and DNA sequence of the manA gene and characterization of the enzyme."
    Arcand N., Kluepfel D., Paradis F.W., Morosoli R., Shareck F.
    Biochem. J. 290:857-863(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-42.
    Strain: 66 / 1326.
  2. Shareck F.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO C-TERMINUS.

Entry informationi

Entry nameiMANA_STRLI
AccessioniPrimary (citable) accession number: P51529
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2000
Last modified: December 11, 2013
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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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