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Q4X0A5

- ABNB_ASPFU

UniProt

Q4X0A5 - ABNB_ASPFU

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Protein

Probable arabinan endo-1,5-alpha-L-arabinosidase B

Gene

abnB

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan (By similarity).By similarity

Catalytic activityi

Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.

Pathwayi

GO - Molecular functioni

  1. arabinan endo-1,5-alpha-L-arabinosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. arabinan catabolic process Source: UniProtKB-UniPathway
  2. xylan catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayiUPA00667.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable arabinan endo-1,5-alpha-L-arabinosidase B (EC:3.2.1.99)
Alternative name(s):
Endo-1,5-alpha-L-arabinanase B
Short name:
ABN B
Gene namesi
Name:abnB
ORF Names:AFUA_2G14150
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 2

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 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 372356Probable arabinan endo-1,5-alpha-L-arabinosidase BPRO_0000394627Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUAP00004856.

Structurei

3D structure databases

ProteinModelPortaliQ4X0A5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 43 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3507.
HOGENOMiHOG000292006.
InParanoidiQ4X0A5.
KOiK06113.
OrthoDBiEOG761C4Q.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR006710. Glyco_hydro_43.
IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERiPTHR22925. PTHR22925. 1 hit.
PfamiPF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
PIRSFiPIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
SUPFAMiSSF75005. SSF75005. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q4X0A5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTVLVALFCL VTWTLCTRIP QYSTQGTQQP QQPEKTPHPH PQPEDAFPPT
60 70 80 90 100
HATDLKIHDP SIIHVDGTYY SYSVGRHIRI HQAPSLDGPW ERTGAVLNAD
110 120 130 140 150
SVIPKGDRKA PWAPQTVHHN DTYYCFYAVS NSGCRDSAIG VATSKSPGPG
160 170 180 190 200
GWTDHGLLVQ SGTGKGSDEH PFTSSNTIDP SVFVGEDGHG YLTFGSFWSG
210 220 230 240 250
IWQVPLDESL LSVAGDTSSE ARQLVYMEKA PLPASKHPNP LCREPSGARP
260 270 280 290 300
IEGSFLSYHE PWYYLWFSYG KCCKFDTKNL PPPGREYSIR VGRSKSPRGP
310 320 330 340 350
FVDKQGRDLA NGGGEIVYAS NRDVYAPGGQ GVLTEKSGDI LYYHYCRYPV
360 370
IQEIEVDADL TVNKSTSYDF WV
Length:372
Mass (Da):41,114
Last modified:June 15, 2010 - v2
Checksum:i0931A8923317F873
GO

Sequence cautioni

The sequence EAL93710.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000001 Genomic DNA. Translation: EAL93710.1. Different initiation.
RefSeqiXP_755748.1. XM_750655.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00004856; CADAFUAP00004856; CADAFUAG00004856.
GeneIDi3513128.
KEGGiafm:AFUA_2G14150.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000001 Genomic DNA. Translation: EAL93710.1 . Different initiation.
RefSeqi XP_755748.1. XM_750655.1.

3D structure databases

ProteinModelPortali Q4X0A5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5085.CADAFUAP00004856.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFUAT00004856 ; CADAFUAP00004856 ; CADAFUAG00004856 .
GeneIDi 3513128.
KEGGi afm:AFUA_2G14150.

Phylogenomic databases

eggNOGi COG3507.
HOGENOMi HOG000292006.
InParanoidi Q4X0A5.
KOi K06113.
OrthoDBi EOG761C4Q.

Enzyme and pathway databases

UniPathwayi UPA00667 .

Family and domain databases

Gene3Di 2.115.10.20. 1 hit.
InterProi IPR006710. Glyco_hydro_43.
IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view ]
PANTHERi PTHR22925. PTHR22925. 1 hit.
Pfami PF04616. Glyco_hydro_43. 1 hit.
[Graphical view ]
PIRSFi PIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
SUPFAMi SSF75005. SSF75005. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
    Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
    , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
    Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Entry informationi

Entry nameiABNB_ASPFU
AccessioniPrimary (citable) accession number: Q4X0A5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: October 29, 2014
This is version 56 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