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Q00012

- MANA_ASPAC

UniProt

Q00012 - MANA_ASPAC

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Protein

Mannan endo-1,4-beta-mannosidase A

Gene

manA

Organism
Aspergillus aculeatus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

pH dependencei

Optimum pH is 5.0.1 Publication

Temperature dependencei

Optimum temperature is between 60 and 70 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei198 – 1981Proton donorBy similarity
Active sitei306 – 3061NucleophileBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.
mycoCLAPiMAN5A_ASPAC.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan endo-1,4-beta-mannosidase A (EC:3.2.1.78)
Alternative name(s):
Endo-beta-1,4-mannanase A
Gene namesi
Name:manA
Synonyms:man1
OrganismiAspergillus aculeatus
Taxonomic identifieri5053 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 377359Mannan endo-1,4-beta-mannosidase APRO_5000142576Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi255 – 2551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi357 – 3571N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ00012.
SMRiQ00012. Positions 30-373.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

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: Complete.

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

Q00012-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLSHMLLSL ASLGVATALP RTPNHNAATT AFPSTSGLHF TIDGKTGYFA
60 70 80 90 100
GTNSYWIGFL TNNDDVDLVM SQLAASDLKI LRVWGFNDVN TKPTDGTVWY
110 120 130 140 150
QLHANGTSTI NTGADGLQRL DYVVTSAEKY GVKLIINFVN EWTDYGGMQA
160 170 180 190 200
YVTAYGAAAQ TDFYTNTAIQ AAYKNYIKAV VSRYSSSAAI FAWELANEPR
210 220 230 240 250
CQGCDTSVLY NWISDTSKYI KSLDSKHLVT IGDEGFGLDV DSDGSYPYTY
260 270 280 290 300
GEGLNFTKNL GISTIDFGTL HLYPDSWGTS YDWGNGWITA HAAACKAVGK
310 320 330 340 350
PCLLEEYGVT SNHCAVESPW QQTAGNATGI SGDLYWQYGT TFSWGQSPND
360 370
GNTFYYNTSD FTCLVTDHVA AINAQSK
Length:377
Mass (Da):41,082
Last modified:November 1, 1996 - v1
Checksum:i10E6477555BE3CA2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35487 mRNA. Translation: AAA67426.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35487 mRNA. Translation: AAA67426.1 .

3D structure databases

ProteinModelPortali Q00012.
SMRi Q00012. Positions 30-373.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH5. Glycoside Hydrolase Family 5.
mycoCLAPi MAN5A_ASPAC.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "Expression cloning, purification and characterization of a beta-1,4-mannanase from Aspergillus aculeatus."
    Christgau S., Kauppinen S., Vind J., Kofod L.V., Dalboge H.
    Biochem. Mol. Biol. Int. 33:917-925(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: KSM 510.

Entry informationi

Entry nameiMANA_ASPAC
AccessioniPrimary (citable) accession number: Q00012
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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