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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, man1
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei198 – 1981Proton donor By similarity
Active sitei306 – 3061Nucleophile By 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-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed prediction
Add
BLAST
Chaini19 – 377359Mannan endo-1,4-beta-mannosidase A
PRO_5000142576Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ00012.
SMRiQ00012. Positions 30-373.

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

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MKLSHMLLSL ASLGVATALP RTPNHNAATT AFPSTSGLHF TIDGKTGYFA    50
GTNSYWIGFL TNNDDVDLVM SQLAASDLKI LRVWGFNDVN TKPTDGTVWY 100
QLHANGTSTI NTGADGLQRL DYVVTSAEKY GVKLIINFVN EWTDYGGMQA 150
YVTAYGAAAQ TDFYTNTAIQ AAYKNYIKAV VSRYSSSAAI FAWELANEPR 200
CQGCDTSVLY NWISDTSKYI KSLDSKHLVT IGDEGFGLDV DSDGSYPYTY 250
GEGLNFTKNL GISTIDFGTL HLYPDSWGTS YDWGNGWITA HAAACKAVGK 300
PCLLEEYGVT SNHCAVESPW QQTAGNATGI SGDLYWQYGT TFSWGQSPND 350
GNTFYYNTSD FTCLVTDHVA AINAQSK 377
Length:377
Mass (Da):41,082
Last modified:November 1, 1996 - v1
Checksum:i10E6477555BE3CA2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L35487 mRNA. Translation: AAA67426.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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: February 19, 2014
This is version 62 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

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