Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q2UIE6

- EGLX_ASPOR

UniProt

Q2UIE6 - EGLX_ASPOR

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Probable endo-1,3(4)-beta-glucanase AO090023000083

Gene

AO090023000083

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Mixed-linked glucanase involved in the degradation of complex natural cellulosic substrates.By similarity

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei144 – 1441NucleophileBy similarity
Active sitei149 – 1491Proton donorBy similarity

GO - Molecular functioni

  1. glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group Source: UniProtKB-EC
  2. glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Probable endo-1,3(4)-beta-glucanase AO090023000083 (EC:3.2.1.6)
Alternative name(s):
Mixed-linked glucanase AO090023000083
Gene namesi
ORF Names:AO090023000083
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564: Chromosome 3

Subcellular locationi

Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 643619Probable endo-1,3(4)-beta-glucanase AO090023000083PRO_0000395091Add
BLAST
Propeptidei644 – 66724Removed in mature formSequence AnalysisPRO_0000395092Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
Lipidationi643 – 6431GPI-anchor amidated alanineSequence Analysis

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Structurei

3D structure databases

ProteinModelPortaliQ2UIE6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi583 – 61533Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 16 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000166269.
OMAiSCVNYVA.
OrthoDBiEOG7HB5KN.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.

Sequencei

Sequence statusi: Complete.

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

Q2UIE6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSSSFVWTV GSIALSSLIT PTIADGSGSR YQLTEAWQGE KFLDHFKFFS
60 70 80 90 100
GSDPTNGFVT YANQSYAESS GLIEVTESGS FYMGVDYKTK LSPNGPGRDS
110 120 130 140 150
VRIESKEYYD EGLYIIDLQH MPGSVCGTWP AFWSVGPNWP YDGEIDIIEG
160 170 180 190 200
VNKHEANEIV LHTSGSCSLS SENDMSGTMT SSECGESSGT IGCVVKGQDG
210 220 230 240 250
TSGAPFNEKN GGVYAMEWTS SFVKIWYFAR SEIPQSITEG NPDTTAFGTP
260 270 280 290 300
MAHLQGTCDF GERFKSQKFI LDTTFCGDWA GGVFGDSGCP VSDPSNPIQS
310 320 330 340 350
CVNYVAENPA AFKEAYWEIN YIKLFQTGTG HSTASVASQA ETATAVASNT
360 370 380 390 400
VDSIPSVTST AIPETTAPAP ETVSAEAPAT SSAVPEPANP QTSVAGAETT
410 420 430 440 450
AAPAPSPETT AAPASPSLDD SDGADAVSET TIYVTETTTI CGASTQKGTI
460 470 480 490 500
QTIGGGETEV SPASSTVESA ATPAAPTPTS QKPVASLPGT TVNGGTPVPT
510 520 530 540 550
DVSPETPAEE TAGESGAPTP SAEQPEQPQP AATSIETGTV PPAVSNPAPT
560 570 580 590 600
EQGTPEGASP VDATESRHDS DEPAPTSAAP IRSPSPSSWT ISSSSRVASS
610 620 630 640 650
SSFASTTSSA SRTTSATKEA TAPTETDSGA STGTNPESPV FTAGASKSVG
660
ISGLTGIVCG IAMAMLA
Length:667
Mass (Da):68,301
Last modified:January 24, 2006 - v1
Checksum:iA37D2DC90AF23769
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP007157 Genomic DNA. Translation: BAE58669.1.
RefSeqiXP_001820671.1. XM_001820619.1.

Genome annotation databases

EnsemblFungiiCADAORAT00007233; CADAORAP00007095; CADAORAG00007233.
GeneIDi5992673.
KEGGiaor:AOR_1_1840144.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP007157 Genomic DNA. Translation: BAE58669.1 .
RefSeqi XP_001820671.1. XM_001820619.1.

3D structure databases

ProteinModelPortali Q2UIE6.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAORAT00007233 ; CADAORAP00007095 ; CADAORAG00007233 .
GeneIDi 5992673.
KEGGi aor:AOR_1_1840144.

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000166269.
OMAi SCVNYVA.
OrthoDBi EOG7HB5KN.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR013320. ConA-like_dom.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 2 hits.
ProtoNeti Search...

Publicationsi

  1. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiEGLX_ASPOR
AccessioniPrimary (citable) accession number: Q2UIE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: January 24, 2006
Last modified: October 29, 2014
This is version 50 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