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Q5AU81

- AFCA_EMENI

UniProt

Q5AU81 - AFCA_EMENI

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Protein

Alpha-fucosidase A

Gene

afcA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Alpha-fucosidase involved in degradation of fucosylated xyloglucans. Hydrolyzes alpha-1,2-linked fucose. Active on cotton xyloglucan oligomers but not active on paranitrophenyl-fucoside.1 Publication

Catalytic activityi

An alpha-L-fucoside + H2O = L-fucose + an alcohol.

GO - Molecular functioni

  1. alpha-L-fucosidase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18214.

Protein family/group databases

CAZyiGH95. Glycoside Hydrolase Family 95.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-fucosidase A (EC:3.2.1.51)
Alternative name(s):
Alpha-L-fucoside fucohydrolase A
Gene namesi
Name:afcA
ORF Names:AN8149
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome II

Subcellular locationi

Secreted Curated

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 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 809790Alpha-fucosidase APRO_0000394704Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi452 – 4521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi614 – 6141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi642 – 6421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi681 – 6811N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5AU81.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 95 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG04067.
HOGENOMiHOG000235039.
InParanoidiQ5AU81.
OMAiSVDFSWD.
OrthoDBiEOG77HDP8.

Family and domain databases

Gene3Di2.70.98.50. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR016518. Alpha-L-fucosidase.
IPR027414. GH_fam_N_dom.
[Graphical view]
PfamiPF14498. Glyco_hyd_65N_2. 1 hit.
[Graphical view]
PIRSFiPIRSF007663. UCP007663. 1 hit.
SUPFAMiSSF48208. SSF48208. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5AU81-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRKTTLFLAV TFATSNAQGR ALRSSSPATY GTTDGSDYIL KTGYLIGNGK
60 70 80 90 100
LGVIPFGPPD TEKLNLNVDS LWSGGPFEVE NYTGGNPSSP IYDALPGIRE
110 120 130 140 150
RIFENGTGGM EELLGSGNHY GSSRVLGNIT IALDGVEAYS KYKRTLDLSD
160 170 180 190 200
GVHRTSFTIA NRTTAALKSS IFCSYPDQVC VYHLESASDA RLPKVTISIE
210 220 230 240 250
NLLVNQSLLQ TSCESEAKRA VLRHSGVTQA GPPEGMKYAA VAEVVNPRSS
260 270 280 290 300
VTTCLGEGAL QISSRKKQLT IIIGAATNYD QKAGNAKSGW SFKNAKDPAS
310 320 330 340 350
IVDGIASAAG WKGYQRLLDR HVKDYKKLMG DFSLELPDTT DSASKDTSEL
360 370 380 390 400
IEKYSYASAT GNPYLENLLL DYARHLLVSS SRPNSLPANL QGRWTESLTP
410 420 430 440 450
SWSADYHANI NLQMNYWLAD QTGLGETQHA LWNYMADTWV PRGTETARLL
460 470 480 490 500
YNASGWVVHN EINIFGFTAM KEDAGWANYP AAAAWMMQHV WDNFDYTHDT
510 520 530 540 550
AWLVSQGYAL LKGIASFWLS SLQEDKFFND GSLVVNPCNS PETGPTTFGC
560 570 580 590 600
THYQQLIHQV FETVLAAQEY IHESDTKFVD SVASALERLD TGLHLSSWGG
610 620 630 640 650
LKEWKLPDSY GYDNMSTHRH LSHLAGWYPG YSISSFAHGY RNKTIQDAVK
660 670 680 690 700
ETLTARGMGN AADANAGWAK VWRAACWARL NDSSMAYDEL RYAIDENFVG
710 720 730 740 750
NGLSMYWGAS PPFQIDANFG FAGAVLSMLV VDLPTPRSDP GQRTVVLGPA
760 770 780 790 800
IPSAWGGGRA KGLRLRGGAK VDFGWDKRGV VNWVNIVKRG KGTSRVKLVN

KEGDILAEM
Length:809
Mass (Da):88,536
Last modified:April 26, 2005 - v1
Checksum:iFDF201647A4BF899
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490516 mRNA. Translation: ABF50892.1.
AACD01000141 Genomic DNA. Translation: EAA59171.1.
BN001302 Genomic DNA. Translation: CBF73981.1.
RefSeqiXP_681418.1. XM_676326.1.

Genome annotation databases

EnsemblFungiiCADANIAT00004184; CADANIAP00004184; CADANIAG00004184.
GeneIDi2869274.
KEGGiani:AN8149.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490516 mRNA. Translation: ABF50892.1 .
AACD01000141 Genomic DNA. Translation: EAA59171.1 .
BN001302 Genomic DNA. Translation: CBF73981.1 .
RefSeqi XP_681418.1. XM_676326.1.

3D structure databases

ProteinModelPortali Q5AU81.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH95. Glycoside Hydrolase Family 95.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00004184 ; CADANIAP00004184 ; CADANIAG00004184 .
GeneIDi 2869274.
KEGGi ani:AN8149.2.

Phylogenomic databases

eggNOGi NOG04067.
HOGENOMi HOG000235039.
InParanoidi Q5AU81.
OMAi SVDFSWD.
OrthoDBi EOG77HDP8.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-18214.

Family and domain databases

Gene3Di 2.70.98.50. 1 hit.
InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR016518. Alpha-L-fucosidase.
IPR027414. GH_fam_N_dom.
[Graphical view ]
Pfami PF14498. Glyco_hyd_65N_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF007663. UCP007663. 1 hit.
SUPFAMi SSF48208. SSF48208. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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], FUNCTION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "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 nameiAFCA_EMENI
AccessioniPrimary (citable) accession number: Q5AU81
Secondary accession number(s): C8V6V7, Q1HFQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: October 29, 2014
This is version 53 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3