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Q5BF93

- MNS1B_EMENI

UniProt

Q5BF93 - MNS1B_EMENI

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Protein
Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B
Gene
mns1B, msdS, AN0787
Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Involved in the maturation of Asn-linked oligosaccharides. Progressively trims alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man5GlcNAc2.1 Publication

Catalytic activityi

Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.

Cofactori

Ca2+. Can also use Mg2+, but with lower efficiency By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei368 – 3681Proton donor By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

CAZyiGH47. Glycoside Hydrolase Family 47.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B (EC:3.2.1.113)
Alternative name(s):
Class I alpha-mannosidase 1B
Man(9)-alpha-mannosidase 1B
Gene namesi
Name:mns1B
Synonyms:msdS
ORF Names:AN0787
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome VIII

Subcellular locationi

GO - Cellular componenti

  1. cytoplasmic membrane-bounded vesicle lumen Source: UniProtKB-SubCell
  2. membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616 Reviewed prediction
Add
BLAST
Chaini17 – 505489Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B
PRO_0000394823Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi88 – 881N-linked (GlcNAc...) Reviewed prediction
Glycosylationi174 – 1741N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi325 ↔ 354 By similarity
Glycosylationi359 – 3591N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Monomer By similarity.

Protein-protein interaction databases

STRINGi162425.CADANIAP00001876.

Structurei

3D structure databases

ProteinModelPortaliQ5BF93.
SMRiQ5BF93. Positions 30-501.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG300315.
HOGENOMiHOG000181987.
KOiK01230.
OMAiYAFPHDS.
OrthoDBiEOG7BP8BH.

Family and domain databases

Gene3Di1.50.10.50. 1 hit.
InterProiIPR001382. Glyco_hydro_47.
[Graphical view]
PANTHERiPTHR11742. PTHR11742. 1 hit.
PfamiPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSiPR00747. GLYHDRLASE47.
SUPFAMiSSF48225. SSF48225. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5BF93-1 [UniParc]FASTAAdd to Basket

« Hide

MRTLLALAAL AGFAAARVPA YAITRPVMRS DSRADAVKEA FSHAWDGYYN    50
YAFPHDELHP ISNGYGDSRN HWGASAVDAL STAIMMRNAT IVNQILDHIA 100
AVDYSKTNAM VSLFETTIRY LAGMISGYDL LKGPAAGLVD DSRVDVLLEQ 150
SQNLAEVLKF AFDTPSGVPY NMINITSGGN DGATTNGLAV TGTLVLEWTR 200
LSDLTGNDEY ARLSQRAEDY LLHPEPAQYE PFPGLIGSAV NIADGKLANG 250
HISWNGGADS YYEYLIKMYV YDPERFGLYR DRWVAAAESS INHLASHPST 300
RPDVTFLATY NEEHQLGLTS QHLTCFDGGS FLLGGTLLDR QDFVDFGLDL 350
VAGCHETYNS TLTGIGPEQF SWDPNGVPDS QKELFERAGF YINSGQYILR 400
PEVIESFYYA WRVTGDGTYR EWVWNAFTNI NKYCRTATGF AGLENVNAAN 450
GGGRIDNQES FMFAEVLKYS FLTFAPEDDW QVQKGSGNTF VYNTEAHPFK 500
VYTPQ 505
Length:505
Mass (Da):55,881
Last modified:June 15, 2010 - v2
Checksum:iEC77168E8C363B6F
GO

Sequence cautioni

The sequence EAA65617.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101L → F in AAG48159. 1 Publication
Sequence conflicti420 – 4201R → L in AAG48159. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF129496 Genomic DNA. Translation: AAG48159.1.
DQ490469 mRNA. Translation: ABF50845.1.
AACD01000013 Genomic DNA. Translation: EAA65617.1. Sequence problems.
BN001308 Genomic DNA. Translation: CBF88785.1.
RefSeqiXP_658391.1. XM_653299.1.

Genome annotation databases

EnsemblFungiiCADANIAT00001876; CADANIAP00001876; CADANIAG00001876.
GeneIDi2876566.
KEGGiani:AN0787.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF129496 Genomic DNA. Translation: AAG48159.1 .
DQ490469 mRNA. Translation: ABF50845.1 .
AACD01000013 Genomic DNA. Translation: EAA65617.1 . Sequence problems.
BN001308 Genomic DNA. Translation: CBF88785.1 .
RefSeqi XP_658391.1. XM_653299.1.

3D structure databases

ProteinModelPortali Q5BF93.
SMRi Q5BF93. Positions 30-501.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 162425.CADANIAP00001876.

Protein family/group databases

CAZyi GH47. Glycoside Hydrolase Family 47.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00001876 ; CADANIAP00001876 ; CADANIAG00001876 .
GeneIDi 2876566.
KEGGi ani:AN0787.2.

Phylogenomic databases

eggNOGi NOG300315.
HOGENOMi HOG000181987.
KOi K01230.
OMAi YAFPHDS.
OrthoDBi EOG7BP8BH.

Enzyme and pathway databases

UniPathwayi UPA00378 .

Family and domain databases

Gene3Di 1.50.10.50. 1 hit.
InterProi IPR001382. Glyco_hydro_47.
[Graphical view ]
PANTHERi PTHR11742. PTHR11742. 1 hit.
Pfami PF01532. Glyco_hydro_47. 1 hit.
[Graphical view ]
PRINTSi PR00747. GLYHDRLASE47.
SUPFAMi SSF48225. SSF48225. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the class I alpha-mannosidase gene family in the filamentous fungus Aspergillus nidulans."
    Eades C.J., Hintz W.E.
    Gene 255:25-34(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: SM222.
  2. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
    Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
    Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  4. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiMNS1B_EMENI
AccessioniPrimary (citable) accession number: Q5BF93
Secondary accession number(s): C8VQU4, Q1HFV5, Q9HF85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: April 16, 2014
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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