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Q5BAP5 (EGLX_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Endo-1,3(4)-beta-glucanase xgeA

EC=3.2.1.6
Alternative name(s):
Mixed-linked glucanase xgeA
Gene names
Name:xgeA
ORF Names:AN2385
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length626 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Mixed-linked glucanase involved in the degradation of complex natural cellulosic substrates. Active on laminarin. lichenan, soluble carboxymethyl cellulose but not on pustulan. Ref.3

Catalytic activity

Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolyzed is itself substituted at C-3.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 16 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 603578Endo-1,3(4)-beta-glucanase xgeA
PRO_0000395093
Propeptide604 – 62623Removed in mature form Potential
PRO_0000395094

Regions

Compositional bias342 – 459118Thr-rich

Sites

Active site1421Nucleophile By similarity
Active site1471Proton donor By similarity

Amino acid modifications

Lipidation6031GPI-anchor amidated glycine Potential
Glycosylation611N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5BAP5 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: B18C705CD41F4045

FASTA62665,098
        10         20         30         40         50         60 
MSSSLMRRVG SLAASAIIFP GIAHAASNYK LKESWEGEKI LNHFHFFDNA DPTNGFVTYV 

        70         80         90        100        110        120 
NQSYAESAGL VKTTDSGSLY LGVDYENVLT VDGPGRESVR IESNEYYDQG LYVVDIQHMP 

       130        140        150        160        170        180 
GSICGTWPAF WTVGPDWPTD GEIDIIEGVN KHDANKIVLH TSDTCDVGGG YKMTGDMTSS 

       190        200        210        220        230        240 
ECGEASGTIG CVVQGKQGSS GDPFNEQGGG VYAMEWQEKY LKIWYFPRSS IPESLTAGTP 

       250        260        270        280        290        300 
DVSSFGTPMA HLQGSCNFKE RFTHQKLILD TTFCGDWAGG VFGDSGCPVS DPSDPMLSCK 

       310        320        330        340        350        360 
NYVAENPAVY KNAYWELNSI KIYQLGGTAE VEGTQSAAAE STAAEATAAE TTAAATQTAN 

       370        380        390        400        410        420 
GGSIEEITTS THSVTRTKTV SATHSTETAA VTETAAATTA AASVASEVDA TNTQPVSKTK 

       430        440        450        460        470        480 
STSYVTSTTT LCPVESSQAA ATESVSRTKT TSYVTITTTL CPVESLQTAN AVPSAKASTD 

       490        500        510        520        530        540 
AAAATTPAAE PHPSNAETPA DSKSSADAVT AQATKTTIAV NTPNPATDSA SSVPPDSIVY 

       550        560        570        580        590        600 
TAPEVTSSSS VPLFTIVSSS SQFVTVPTAA PSSFEPTDAV RDGADSYSTA ASPTTPSNPV 

       610        620 
FTGVGSKVSI SASVAIAAFV MLLLVN 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
[3]"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: FUNCTION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACD01000039 Genomic DNA. Translation: EAA64496.1.
BN001307 Genomic DNA. Translation: CBF86736.1.
RefSeqXP_659989.1. XM_654897.1.

3D structure databases

ProteinModelPortalQ5BAP5.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH16. Glycoside Hydrolase Family 16.
mycoCLAPMLG16A_EMENI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00009087; CADANIAP00009087; CADANIAG00009087.
GeneID2874796.
KEGGani:AN2385.2.

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000166269.
OMASCVNYVA.
OrthoDBEOG7HB5KN.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000757. Glyco_hydro_16.
[Graphical view]
PfamPF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 2 hits.
ProtoNetSearch...

Entry information

Entry nameEGLX_EMENI
AccessionPrimary (citable) accession number: Q5BAP5
Secondary accession number(s): C8VNP1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: February 19, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries