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Q5BCI8

- MANBA_EMENI

UniProt

Q5BCI8 - MANBA_EMENI

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Protein

Beta-mannosidase A

Gene

mndA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of beta-mannosidic oligosaccharides of various complexity and length. Involved in the degradation of polymeric mannan and galactomannan (By similarity).By similarity

Catalytic activityi

Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei476 – 4761Proton donorBy similarity

GO - Molecular functioni

  1. beta-mannosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

UniPathwayiUPA00280.

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-mannosidase A (EC:3.2.1.25)
Alternative name(s):
Mannanase A
Short name:
Mannase A
Gene namesi
Name:mndA
ORF Names:AN1742
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome VII

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 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 940919Beta-mannosidase APRO_0000394649Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi15 – 151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi39 – 391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi245 – 2451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi314 – 3141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi534 – 5341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi605 – 6051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi626 – 6261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi653 – 6531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi733 – 7331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi761 – 7611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi785 – 7851N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi162425.CADANIAP00008389.

Structurei

3D structure databases

ProteinModelPortaliQ5BCI8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000216059.
InParanoidiQ5BCI8.
KOiK01192.
OMAiCHATQLF.
OrthoDBiEOG78D7TH.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR008979. Galactose-bd-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR006102. Glyco_hydro_2_Ig-like.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00703. Glyco_hydro_2. 1 hit.
[Graphical view]
SUPFAMiSSF49303. SSF49303. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5BCI8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHFHGIATQA VLASNITTGS GRHVSLSDVK WTLSSSALNS TVPASLPSQA
60 70 80 90 100
HLDLLNAGVI DDPYYGLNEI DLQWIAQANW TYTSDPIPDL LEEYESTWLV
110 120 130 140 150
FEGLDTFATV TFCGHNIAST NNQFRQYAFD VSSALKECTG GPVVRIDFAS
160 170 180 190 200
APNTVDAIAA DPKTPVWPVQ LTAQLPNRWL MRKQQSDFGW DWGPAFAPCG
210 220 230 240 250
PWKPAYVVQL EKTAPIHVLN TDLDIYRQGN INHLPPDQKQ PWVVNASIDF
260 270 280 290 300
IGRLPAEPRL LIEIKELETG DVLASQISDS VTLIGTSITG VTTLKDASPK
310 320 330 340 350
LWWPSSLGAQ NLYNVTITVF NKTEEVARIT KRTGFRTIFL NQRNITATQL
360 370 380 390 400
SQGIAPGANW HFEVNGKEFY AKGSNFIPPD TFWPRVTKQK MTRLLDAVVA
410 420 430 440 450
GNQNMLRIWS SGAYLPDFIY DLADERGILL WSEFQFSDSM YPVDEDFLDN
460 470 480 490 500
VAQEVVYNVR RVNHHPSLAL WAGGNEIESL MLPLTREADP DNYPKYLAEY
510 520 530 540 550
EKLYISLILP LVYENTRSIS YSPSSTTEGY LSVNLSAPVP MTERYENDEP
560 570 580 590 600
GAYYGDTDYY NYDTTVSFDY SIYPVGRFAN EFGFHSMPSL QTWQQVADPE
610 620 630 640 650
DLYFNSTTVV IHNRHYTSEG YGRIENSSRG MAEMTLGVER YYPIPDNPDS
660 670 680 690 700
VANFSAWCLA TQLFQADFYK SQIQFYRRGS GMPERQLGSL YWQLEDIWQG
710 720 730 740 750
PTWAGIEYDG RWKVLHYVAR DVYQPIIVSP FWNYTTGDLE IYVTADLWES
760 770 780 790 800
AAGTVNLKWL NLSGEQIIDN AGTPTEIPFT VGAINTTKVY STNIHDLNLP
810 820 830 840 850
DTRASILTLS LSSQANLPNA AVKTSLTHEN HFTPSFPKDL ELVNPGLELS
860 870 880 890 900
YDAHSGIFTV EAKSGVSLYT WLDYPAGLVG YFTENAFLLV PGQKKKVQFV
910 920 930 940
VQDGPKDQDW EWQSEVTVRS LWDQKSSTFL YALRVATGRP
Length:940
Mass (Da):105,765
Last modified:April 26, 2005 - v1
Checksum:i45E1CBB33D2AFAF0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACD01000027 Genomic DNA. Translation: EAA64028.1.
BN001307 Genomic DNA. Translation: CBF85479.1.
RefSeqiXP_659346.1. XM_654254.1.

Genome annotation databases

EnsemblFungiiCADANIAT00008389; CADANIAP00008389; CADANIAG00008389.
GeneIDi2874889.
KEGGiani:AN1742.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACD01000027 Genomic DNA. Translation: EAA64028.1 .
BN001307 Genomic DNA. Translation: CBF85479.1 .
RefSeqi XP_659346.1. XM_654254.1.

3D structure databases

ProteinModelPortali Q5BCI8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 162425.CADANIAP00008389.

Protein family/group databases

CAZyi GH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00008389 ; CADANIAP00008389 ; CADANIAG00008389 .
GeneIDi 2874889.
KEGGi ani:AN1742.2.

Phylogenomic databases

eggNOGi COG3250.
HOGENOMi HOG000216059.
InParanoidi Q5BCI8.
KOi K01192.
OMAi CHATQLF.
OrthoDBi EOG78D7TH.

Enzyme and pathway databases

UniPathwayi UPA00280 .

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProi IPR008979. Galactose-bd-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR006102. Glyco_hydro_2_Ig-like.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00703. Glyco_hydro_2. 1 hit.
[Graphical view ]
SUPFAMi SSF49303. SSF49303. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. "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 nameiMANBA_EMENI
AccessioniPrimary (citable) accession number: Q5BCI8
Secondary accession number(s): C8VP45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: October 29, 2014
This is version 66 of the entry and version 1 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